|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
434-2258 |
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: 1234.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 434 NHTKDFLTYKLTKEQIAskYGIPINSTPFCFSLYKDIINMPAGPVIWAFLKPMLLGRILYAPYNPVTKAIMEKSNVTLRQ 513
Cdd:TIGR01257 343 NNYKAFLGIDSTRKDPI--YSYDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 514 LAELREKSQEWMDKSPLFMNSFHLLNQaIPMLQNTLRNPFVQVFVKFSVGLDAV--ELL----------KQIDELDILRL 581
Cdd:TIGR01257 421 LERVRKLVKAWEEVGPQIWYFFDKSTQ-MTMIRDTLQNPTVKDFINRQLGEEGItaEAVlnflyngpreKQADDMTNFDW 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 582 KlenniDIIDQLNTLSSLTVNISSCVLYDRIQAAKTIDEMEREAKRLYKSNELFGSVIFklPSNRSWHRGydsgnvfLPP 661
Cdd:TIGR01257 500 R-----DIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVF--PDMYPWTSS-------LPP 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 662 VIKYTIRMSLKTAQTTRSLRTKIWAPGPHNSPSHN--QIYGrAFIYLQDSIERAIIELQTgRNSQEIAVQVQAIPYPCFM 739
Cdd:TIGR01257 566 HVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDfrYIWG-GFAYLQDMVEQGITRSQM-QAEPPVGIYLQQMPYPCFV 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 740 KDNFLTSVSYSLPIVLMVAWVVFIAAFVKKLVYEKDLRLHEYMKMMGVNSCSHFFAWLIESVGFLLVTIVILIIILKFGN 819
Cdd:TIGR01257 644 DDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGR 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 820 ILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYIIAFFPFIVLVTVENELSYVLKVFMSLLSPTAFS 899
Cdd:TIGR01257 724 ILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFG 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 900 YASQYIARYEEQGIGLQWENMYTSPVQDDTTSFGWLCCLILADSFIYFLIAWYVRNVFPGTYGMAAPWYFPILPSYWKER 979
Cdd:TIGR01257 804 FGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGG 883
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 980 FGCAeVKPEKSngLMFTNIMMQNTNPSASPEYMFSSNIEPEPKDLTVGVALHGVTKIY--GSKVAVDNLNLNFYEGHITS 1057
Cdd:TIGR01257 884 EGCS-TREERA--LEKTEPLTEEMEDPEHPEGINDSFFERELPGLVPGVCVKNLVKIFepSGRPAVDRLNITFYENQITA 960
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1058 LLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVPHWTKKQL 1137
Cdd:TIGR01257 961 FLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQL 1040
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1138 heEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTH 1217
Cdd:TIGR01257 1041 --EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH 1118
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1218 HLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKK----KSPNLNANAVC--------------------- 1272
Cdd:TIGR01257 1119 HMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKmkniQSQRGGCEGTCsctskgfstrcparvdeitpe 1198
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1273 -----DTMAVTAMIQSHLPEAYLKEDIGGELVYVLPPFSTKvSGAYLSLLRALDNGMGDLNIGCYGISDTTVEEVFLNLT 1347
Cdd:TIGR01257 1199 qvldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFK-QRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVT 1277
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1348 KES-----------QKNSAMSLEH----LTQKKIGNSNANGISTPDDLSVSSSN--FTDRDDKiltrGERLD-GFGLLLK 1409
Cdd:TIGR01257 1278 EDAdsgslfaggaqQKRENANLRHpcsgPTEKAGQTPQASHTCSPGQPAAHPEGqpPPEPEDP----GVPLNtGARLILQ 1353
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1410 KIMAILIKRFHHTRRNWKGLIAQVILPIVFVTTAMGLGTLRNSSNSYPEIQISPSLYGtsEQTAFYANYHPSTE---ALV 1486
Cdd:TIGR01257 1354 HVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYG--QQYTFFSMDEPNSEhleVLA 1431
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1487 SAMWDFPGIDNMCLNTS---DLQCLNKDSL---------------EKWnTSGEPITNfgvCSCSEN-----VQECPK--F 1541
Cdd:TIGR01257 1432 DVLLNKPGFGNRCLKEEwlpEYPCGNSTPWktpsvspnithlfqkQKW-TAAHPSPS---CRCSTRekltmLPECPEgaG 1507
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1542 NYSPPHRRTYSSQVIYNLTGQRVENYLISTANEFV-----------QKRYGGWSFG-----LPLT--------KDL--RF 1595
Cdd:TIGR01257 1508 GLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIrsslkskfwvnEQRYGGISIGgklpaIPITgealvgflSDLgqMM 1587
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1596 DITGVPANRTLA----------------KVWYDPEGYHSLPAYLNSLNNFLLRVNMSK-YDAARHGIIMYSHPYPGVQDQ 1658
Cdd:TIGR01257 1588 NVSGGPVTREASkempdflkhletedniKVWFNNKGWHALVSFLNVAHNAILRASLPKdRDPEEYGITVISQPLNLTKEQ 1667
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1659 --EQATISSLIDILVALSILMGYSVTTASFVTYVVREHQTKAKQLQHISGIGVTCYWVTNFIYDMVFYLVPVAFSIGIIA 1736
Cdd:TIGR01257 1668 lsEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFI 1747
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1737 IFKLPAFYSENNLGAVSLLLLLFGYATFSWMYLLAGLFHETGMAFITYVCVNLFFGINSivslSVVYFLSKEKPNDPTLE 1816
Cdd:TIGR01257 1748 GFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINS----SAITFVLELFENNRTLL 1823
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1817 LISETLKRIFLIFPQFCFGYGLIELSQQQSVLDFLKAYGVEYPNETFEMNKLGAMFVALVSQGTMFFSLRLLINEslikk 1896
Cdd:TIGR01257 1824 RFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQH----- 1898
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1897 lRLFFRKFNSSHVRETI-DEDEDVRAERLRVESGAAEFDLVQLYCLTKTYQLIHKKiiAVNNISIGIPAGECFGLLGVNG 1975
Cdd:TIGR01257 1899 -HFFLSRWIAEPAKEPIfDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP--AVDRLCVGVRPGECFGLLGVNG 1975
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1976 AGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLvGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKL 2055
Cdd:TIGR01257 1976 AGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM-GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWS 2054
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2056 LRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECE 2135
Cdd:TIGR01257 2055 IQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECE 2134
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2136 ALCTRLAIMVNGKFQCIGSLQHIKSRFGRGFTVKVHLKNNK----VTMETLTKFMQLHFPKTYLKDQHLSMLEYHVPVTA 2211
Cdd:TIGR01257 2135 ALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS 2214
|
1930 1940 1950 1960
....*....|....*....|....*....|....*....|....*..
gi 27881501 2212 ggVANIFDLLETNKTALNITNFLVSQTTLEEVFINFAKDQKsyETAD 2258
Cdd:TIGR01257 2215 --LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQT--ETYD 2257
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1936-2159 |
1.18e-97 |
|
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: 314.06 E-value: 1.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1936 VQLYCLTKTYqliHKKI-IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrNKTGSLGHVDSHSSL 2014
Cdd:cd03263 1 LQIRNLTKTY---KKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI-NGYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILL 2094
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2095 LDEPSSGMDPKSKRHLWKIISEEVQNKcSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIK 2159
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGR-SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1032-1247 |
2.50e-97 |
|
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: 312.90 E-value: 2.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGS--KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHD 1109
Cdd:cd03263 5 NLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHLLLYGSIK-VPHWTKKqlhEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:cd03263 85 ALFDELTVREHLRFYARLKgLPKSEIK---EEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1189 TGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLK 1247
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1028-1263 |
1.28e-78 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 260.00 E-value: 1.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQ 1107
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLLLYGSIK-VPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYgLP---RKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1187 PSTGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKKKS 1263
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEEA 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1941-2162 |
3.83e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 244.20 E-value: 3.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrnktgsLGH-VDSHS----SLV 2015
Cdd:COG1131 6 LTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV------LGEdVARDPaevrRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLL 2095
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 2096 DEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKSRF 2162
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1028-1237 |
1.41e-61 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 208.41 E-value: 1.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQ 1107
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLllygsikvphwtkkqlheevkrtlkdtglyshrhkrvgTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:cd03230 81 EPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1188 STGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:cd03230 123 TSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1035-1252 |
1.35e-58 |
|
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: 205.32 E-value: 1.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1035 KIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHDVLFSY 1114
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTTKEHLLLYGSIK-VPHWTKKQLHEEVkrtLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDP 1193
Cdd:TIGR01188 81 LTGRENLEMMGRLYgLPKDEAEERAEEL---LELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1194 CSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGD 1252
Cdd:TIGR01188 158 RTRRAIWDYIRAlKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGK 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1032-1247 |
2.40e-58 |
|
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: 201.44 E-value: 2.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHDVL 1111
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1112 FSYLTTKEHLLLYGSIK-VPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTG 1190
Cdd:cd03265 85 DDELTGWENLYIHARLYgVP---GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1191 VDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLK 1247
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1030-1252 |
6.77e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 195.08 E-value: 6.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHD 1109
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHLLLYGSIKvpHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:COG4555 84 GLYDRLTVRENIRYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1190 GVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGD 1252
Cdd:COG4555 162 GLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1941-2164 |
5.33e-55 |
|
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: 192.38 E-value: 5.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtGSLGHVDSHSSLVGYCPQ 2020
Cdd:COG4555 7 LSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE-DVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKSRFGR 2164
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1941-2149 |
1.30e-54 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 188.76 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrNKTGSLGHVDSHSSLVGYCPQ 2020
Cdd:cd03230 6 LSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-LGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTVEEHLYFyarvhgipekdiketvhkllrrlhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1030-1358 |
2.83e-51 |
|
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: 201.40 E-value: 2.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYG--SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQ 1107
Cdd:TIGR01257 1940 LNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLLLYGSIK-VPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:TIGR01257 2020 FDAIDDLLTGREHLYLYARLRgVP---AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1187 PSTGVDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLtKKKSPN 1265
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTM-KIKSPK 2175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1266 lnANAVCDTMAVTAMIQSHLPEAYLKEDIGGELVYVLPpfstkvSGAYLSLLRALDNGMGDLNIGCYGISDTTVEEVFLN 1345
Cdd:TIGR01257 2176 --DDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVS------SSSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVN 2247
|
330
....*....|...
gi 27881501 1346 LTKESQKNSAMSL 1358
Cdd:TIGR01257 2248 FAKQQTETYDLPL 2260
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1028-1241 |
1.08e-50 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 178.93 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGhITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQ 1107
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHL----LLYGsikVPHwtkKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:cd03264 80 EFGVYPNFTVREFLdyiaWLKG---IPS---KEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCG 1241
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1954-2159 |
2.53e-50 |
|
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: 178.33 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNilirnktgslGHVDSHSSL---------VGYCPQEDAL 2024
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR----------ATVAGHDVVreprevrrrIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2025 DDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDP 2104
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2105 KSKRHLWKIISEEVQ-NKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIK 2159
Cdd:cd03265 165 QTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1941-2251 |
5.41e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 177.22 E-value: 5.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDshssLVGYCPQ 2020
Cdd:COG4152 7 LTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR----RIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK--FQciGSLQHIKSRFGRGfTVKVHLKNNKVT 2178
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRkvLS--GSVDEIRRQFGRN-TLRLEADGDAGW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2179 METLTKfmqlhfpktyLKDQHLSMLEYHVPVTAGGVANifDLLETNKTALNITNFLVSQTTLEEVFINFAKDQ 2251
Cdd:COG4152 236 LRALPG----------VTVVEEDGDGAELKLEDGADAQ--ELLRALLARGPVREFEEVRPSLNEIFIEVVGEK 296
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1032-1238 |
1.69e-48 |
|
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: 172.40 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQHDVL 1111
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1112 FSYLTTKEHLLLYGSIkvphwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGV 1191
Cdd:cd03268 84 YPNLTARENLRLLARL------LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 1192 DPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:cd03268 158 DPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1936-2150 |
2.13e-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: 169.30 E-value: 2.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1936 VQLYCLTKTYqlihKKIIAVNNISIGIPAGeCFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrNKTGSLGHVDSHSSLV 2015
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI-DGQDVLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLL 2095
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2096 DEPSSGMDPKSK---RHLwkiISEEVQNKCsVILTSHSMEECEALCTRLAIMVNGKFQ 2150
Cdd:cd03264 155 DEPTAGLDPEERirfRNL---LSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1028-1256 |
3.93e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 169.44 E-value: 3.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNMGVC 1105
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 MQH------------DVLFSylttkehLLLYGsikvphWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISI 1173
Cdd:COG1122 81 FQNpddqlfaptveeDVAFG-------PENLG------LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1174 ALIGGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEAFGD 1252
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP---REVFSD 224
|
....
gi 27881501 1253 GYHL 1256
Cdd:COG1122 225 YELL 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1030-1235 |
3.30e-45 |
|
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: 163.02 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGS--KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNMGVCM 1106
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QH-DVLFSYLTTKE----HLLLYGsikvphWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRV 1181
Cdd:cd03225 82 QNpDDQFFGPTVEEevafGLENLG------LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1182 VILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1941-2148 |
2.24e-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: 160.91 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslGHVDSHSSLVGYCPQ 2020
Cdd:cd03269 6 VTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----PLDIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1030-1251 |
2.30e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 163.74 E-value: 2.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKtdlHTVRKNMGvcmqhd 1109
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIG------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 vlfsYL----------TTKEHLLLYGSIKvpHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGS 1179
Cdd:COG4152 75 ----YLpeerglypkmKVGEQLVYLARLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1180 RVVILDEPSTGVDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFG 1251
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1954-2158 |
7.77e-44 |
|
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: 159.81 E-value: 7.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQeDALDDLV--TVE 2031
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQ-NPDDQLFapTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 EHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLW 2111
Cdd:COG1122 95 EDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881501 2112 KIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:COG1122 175 ELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1936-2148 |
3.29e-43 |
|
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: 157.38 E-value: 3.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1936 VQLYCLTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHSSLV 2015
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETvhklLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLL 2095
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2096 DEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1030-1235 |
3.94e-43 |
|
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: 157.30 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQHD 1109
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHlLLYGsIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:cd03259 82 ALFPHLTVAEN-IAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 1190 GVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03259 160 ALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1941-2148 |
1.50e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 155.70 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQliHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQ 2020
Cdd:cd03225 5 LSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 eDALDDLV--TVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEP 2098
Cdd:cd03225 83 -NPDDQFFgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881501 2099 SSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1935-2148 |
2.85e-42 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 155.22 E-value: 2.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1935 LVQLYCLTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNktgslghVDSHSS- 2013
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-------FDVVKEp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2014 -----LVGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIG 2088
Cdd:cd03266 74 aearrRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2089 KPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1025-1246 |
3.84e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 158.84 E-value: 3.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1025 TVGVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGV 1104
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHDVLFSYLTTKEHLLLYGsiKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFG--RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1185 DEPSTGVDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYL 1246
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1028-1249 |
8.97e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 156.89 E-value: 8.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQ 1107
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLLLYGsiKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFG--RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1188 STGVDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEA 1249
Cdd:PRK13537 166 TTGLDPQARHLMWERLrSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1028-1256 |
2.04e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.71 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVrknmG-VCM 1106
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI----GyVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSY-LTTKEHLL--LYGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:COG1121 83 RAEVDWDFpITVRDVVLmgRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEqGGLRCCGSP------FYLKEAFGDGYHL 1256
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPeevltpENLSRAYGGPVAL 241
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1028-1243 |
3.85e-41 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 152.44 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTVRKNMG 1103
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VCMQHDVLFSYLTT--------KEHLLLygsikvphwTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIAL 1175
Cdd:COG1127 86 MLFQGGALFDSLTVfenvafplREHTDL---------SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1176 IGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTAR--TIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1028-1235 |
4.17e-41 |
|
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: 151.28 E-value: 4.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDlhtVRKNMGVCMQ 1107
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLLLYGSIKvpHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLK--GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 1188 STGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1957-2129 |
6.53e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 147.63 E-value: 6.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLgHVDSHSSLVGYCPQEDALDDLVTVEEHLYF 2036
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 YARVHGIPEKDikETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISE 2116
Cdd:COG4133 99 WAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|...
gi 27881501 2117 EVQNKCSVILTSH 2129
Cdd:COG4133 177 HLARGGAVLLTTH 189
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1941-2188 |
6.83e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 151.78 E-value: 6.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQlIHKK------------------IIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRnkt 2002
Cdd:COG4586 7 LSKTYR-VYEKepglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2003 gslghvdshsslvGYCPQEDALD-----------------DLvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFK 2065
Cdd:COG4586 83 -------------GYVPFKRRKEfarrigvvfgqrsqlwwDL-PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2066 DRATsmcsygtkRKLS--------TALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQ-NKCSVILTSHSMEECEA 2136
Cdd:COG4586 149 DTPV--------RQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEA 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2137 LCTRLAIMVNGKFQCIGSLQHIKSRFGRGFTVKVHLKNNkVTMETLTKFMQL 2188
Cdd:COG4586 221 LCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEP-VPPLELPRGGEV 271
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1032-1243 |
9.50e-40 |
|
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: 148.35 E-value: 9.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCM--QHD 1109
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtfQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHLLLYGSIKVPHWT--------KKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRV 1181
Cdd:cd03219 85 RLFPELTVLENVMVAAQARTGSGLllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1182 VILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1028-1238 |
1.74e-39 |
|
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: 147.13 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSK----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMG 1103
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VCMQHDVLFSYLTTKEHLLLYGSIkvpHWTKK-QLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVV 1182
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGL---YGLKGdELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1183 ILDEPSTGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1028-1232 |
5.43e-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: 145.69 E-value: 5.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSK----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKtdlhTVRKNMG 1103
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VCMQHDVLFSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVAL--GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFL 1232
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1030-1223 |
1.10e-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: 144.16 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHD 1109
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHLLLYGSIKVPHWTkkqlHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:COG4133 85 GLKPELTVRENLRFWAALYGLRAD----REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 27881501 1190 GVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAE 1223
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARgGAVLLTTHQPLELA 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1936-2148 |
2.00e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 148.06 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1936 VQLYCLTKTYQlihKKIIaVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrnktgsLG-HVDSHSSL 2014
Cdd:PRK13536 42 IDLAGVSKSYG---DKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV------LGvPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 ----VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:PRK13536 112 ararIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1030-1243 |
2.05e-38 |
|
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: 145.18 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHT---VRKNMGVCM 1106
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPhriARLGIARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSYLTTKEHLLL-----------YGSIKVPHWTK--KQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISI 1173
Cdd:COG0411 86 QNPRLFPELTVLENVLVaaharlgrgllAALLRLPRARReeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1174 ALIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRlrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1030-1243 |
3.02e-38 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 144.18 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHTVRKNMGVC 1105
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 MQHDVLFSYLTT--------KEHLLLygsikvphwTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIG 1177
Cdd:cd03261 83 FQSGALFDSLTVfenvafplREHTRL---------SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1178 GSRVVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1028-1243 |
1.25e-37 |
|
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: 141.99 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQ 1107
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHlLLYGsIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:cd03300 80 NYALFPHLTVFEN-IAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1188 STGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03300 158 LGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1953-2148 |
1.86e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 144.18 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSlGHVDSHSSLVGYCPQEDALDDLVTVEE 2032
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-SRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:PRK13537 100 NLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 27881501 2113 IISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13537 180 RLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1030-1235 |
2.82e-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: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNMGVCMQh 1108
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 dvlfsylttkehlllygsikvphwtkkqlheevkrtlkdtglyshrhkrvgtLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 1189 TGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd00267 109 SGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1028-1243 |
3.88e-37 |
|
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: 141.28 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIK-TDLHTVRKNMGVC 1105
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 MQHDVLFSYLTTKEHLLLygsikVP---HWTKKQLHEEVKRTLKDTGL----YSHRHKRvgTLSGGMKRKLSISIALIGG 1178
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL-----VPkllKWPKEKIRERADELLALVGLdpaeFADRYPH--ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1179 SRVVILDEPSTGVDPCSRRSIWDVISKNKTA--RTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1028-1243 |
6.83e-37 |
|
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: 140.95 E-value: 6.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCM 1106
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSYLTTKEhLLLYGsiKVPH-----WTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRV 1181
Cdd:COG1120 82 QEPPAPFGLTVRE-LVALG--RYPHlglfgRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1182 VILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1022-1235 |
2.87e-36 |
|
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: 137.66 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1022 KDLTVGvalhgvtkiYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDlhtvRKN 1101
Cdd:cd03235 3 EDLTVS---------YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1102 MG-VCMQHDVLFSY-LTTKEHLL--LYGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIG 1177
Cdd:cd03235 70 IGyVPQRRSIDRDFpISVRDVVLmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1178 GSRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1941-2148 |
5.79e-36 |
|
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: 137.29 E-value: 5.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL-VGYCP 2019
Cdd:cd03218 6 LSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2020 QEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPS 2099
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2100 SGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1941-2153 |
6.57e-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: 136.50 E-value: 6.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQlihkKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgsLGHVDSHSSLVGYCPQ 2020
Cdd:cd03259 6 LSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD--VTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 2101 GMDPKSKRHLWKIISE-EVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIG 2153
Cdd:cd03259 160 ALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1028-1232 |
8.27e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.91 E-value: 8.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIY----GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIktdlHTVRKNMG 1103
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VCMQHDVLFSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVAL--GLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFL 1232
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1955-2100 |
1.40e-35 |
|
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: 133.16 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHL 2034
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2035 YFYARVHGIPEKDIKETVHKLLRRLHLMPFKDR----ATSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1030-1235 |
2.98e-35 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 133.47 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTV---RKNMGVCM 1106
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSYLTTKEHLLLygsikvphwtkkqlheevkrtlkdtglyshrhkrvgTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:cd03229 83 QDFALFPHLTVLENIAL------------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1187 PSTGVDPCSRRSIWDVISKNKT--ARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1941-2148 |
5.30e-35 |
|
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: 131.98 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQ 2020
Cdd:cd00267 5 LSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 edalddlvtveehlyfyarvhgipekdiketvhkllrrlhlmpfkdratsmCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1043-1189 |
1.64e-34 |
|
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: 130.08 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1043 VDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNMGVCMQHDVLFSYLTTKEHL 1121
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1122 LLYGSIKvpHWTKKQLHEEVKRTLKDTGLYSHRHKRVG----TLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:pfam00005 81 RLGLLLK--GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1028-1243 |
2.53e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.38 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQ 1107
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHlLLYGsIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:COG3842 85 DYALFPHLTVAEN-VAFG-LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1188 STGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG3842 163 LSALDAKLREEMREELRRlqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1030-1235 |
3.31e-34 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 131.79 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHT-VRKNMGVCMQ 1107
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHErARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLLLYGSIKVPHWTKKQLhEEVKRTLKDtgLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:cd03224 83 GRRIFPELTVEENLLLGAYARRRAKRKARL-ERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 1188 STGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1032-1243 |
5.75e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 131.51 E-value: 5.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHT---VRKNMGVCMQH 1108
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMhkrARLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYLTTKEHLLLYGSIKVPhwTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGL--SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1189 TGVDPCSRRSIWDVIsKNKTARTI-ILST-HHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03218 162 AGVDPIAVQDIQKII-KILKDRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1028-1235 |
5.91e-34 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 131.53 E-value: 5.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGA-----SAGTIFVYGKDI---KTDLHTVR 1099
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydlDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 KNMGVCMQHDVLFSyLTTKEHLL----LYGSikvphWTKKQLHEEVKRTLKDTGL--YSHRHKRVGTLSGGMKRKLSISI 1173
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAyglrLHGI-----KLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1174 ALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1028-1235 |
1.91e-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: 130.01 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSK----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTVR 1099
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 KNMGVCMQHDVLFSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGS 1179
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVAL--PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1180 RVVILDEPSTGVDPCSRRSIWDVISK-NKTAR-TIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDiNRELGlTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1954-2154 |
1.94e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslgHVDSHSSLVGYCPQEDALDDL--VTVE 2031
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIGYVPQRAEVDWDfpITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 E----HLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSK 2107
Cdd:COG1121 96 DvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881501 2108 RHLWKIISEEVQNKCSVILTSHSMEECEALCTRLaIMVNGKFQCIGS 2154
Cdd:COG1121 176 EALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGP 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1028-1235 |
3.66e-33 |
|
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: 128.80 E-value: 3.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI---KTDLHTVRKNMGV 1104
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHDVLFSYLTTKEHLLLyGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1185 DEPSTGVDPCSRRSIWDVIsKN--KTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03262 160 DEPTSALDPELVGEVLDVM-KDlaEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1031-1238 |
5.18e-33 |
|
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: 128.67 E-value: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1031 HGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKD-IKTDLHtvrkNMGVCMQHD 1109
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKDLH----KIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHLllygsiKVpHWTKKQLHE-EVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:TIGR03740 80 PLYENLTARENL------KV-HTTLLGLPDsRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1189 TGVDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:TIGR03740 153 NGLDPIGIQELRELIrSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1029-1241 |
1.02e-32 |
|
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: 126.01 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1029 ALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVcmq 1107
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 hdvlfsylttkehlllygsikVPhwtkkQLheevkrtLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:cd03214 78 ---------------------VP-----QA-------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 1188 STGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCG 1241
Cdd:cd03214 125 TSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1028-1235 |
1.55e-32 |
|
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: 127.89 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTG-LFGASAGTIFVYGKDI-KTDLHTVRKNMGVC 1105
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRgGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 ---MQHDvlFSYLTTKEHLLL---YGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGS 1179
Cdd:COG1119 84 spaLQLR--FPRDETVLDVVLsgfFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1180 RVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDE--AEVlsDRIAFLEQG 1235
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEipPGI--THVLLLKDG 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1028-1261 |
2.23e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 134.26 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSK-----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTV 1098
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1099 RKNMGVCMQH--DVLFSYLTTKEH----LLLYGsikvpHWTKKQLHEEVKRTLKDTGL-YSHRHKRVGTLSGGMKRKLSI 1171
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIiaepLRLHG-----LLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1172 SIALIGGSRVVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEA 1249
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT---EEV 492
|
250
....*....|..
gi 27881501 1250 FGDGYHLtLTKK 1261
Cdd:COG1123 493 FANPQHP-YTRA 503
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1936-2144 |
2.81e-32 |
|
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: 126.43 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1936 VQLYCLTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghVDSHSSLV 2015
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLL 2095
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2096 DEPSSGMDPKSKRH----LWKIISEEVQnkcSVILTSHSMEECEALCTRLAIM 2144
Cdd:cd03293 156 DEPFSALDALTREQlqeeLLDIWRETGK---TVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1013-1243 |
3.89e-32 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 127.76 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1013 FSSNIEPEPKDLTVGVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI- 1091
Cdd:cd03294 10 FGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1092 ---KTDLHTVR-KNMGVCMQHDVLFSYLTTKEHLLlYGsIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKR 1167
Cdd:cd03294 90 amsRKELRELRrKKISMVFQSFALLPHRTVLENVA-FG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQ 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1168 KLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1941-2158 |
5.82e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.91 E-value: 5.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK--TG-------SLGhvdsh 2011
Cdd:COG1137 9 LVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdiTHlpmhkraRLG----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2012 sslVGYCPQEDAL-DDLvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:COG1137 80 ---IGYLPQEASIfRKL-TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1028-1235 |
5.94e-32 |
|
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: 123.65 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGS--KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGV 1104
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHDVLFSylttkehlllyGSIKvphwtkkqlhEEVkrtlkdtglyshrhkrvgtLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:cd03228 81 VPQDPFLFS-----------GTIR----------ENI-------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1185 DEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEvLSDRIAFLEQG 1235
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1949-2148 |
1.08e-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: 125.14 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1949 HKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI---RNKTGSLGHVDSHSSLVGycpQEDALD 2025
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglVPWKRRKKFLRRIGVVFG---QKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 DLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPK 2105
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881501 2106 SKRHLWKIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1941-2158 |
2.38e-31 |
|
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: 124.31 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL-VGYCP 2019
Cdd:TIGR04406 7 LIKSY----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2020 QEDALDDLVTVEEHLY-FYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEP 2098
Cdd:TIGR04406 83 QEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2099 SSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:TIGR04406 163 FAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1030-1235 |
4.54e-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: 123.45 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGS-KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHTVRKNMGV 1104
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHDVLFSYLTTKEHLLlygSIKVPHWTK-----KQLHEEVKR----TLKDTGLYSHRHKRVGTLSGGMKRKLSISIAL 1175
Cdd:cd03256 83 IFQQFNLIERLSVLENVL---SGRLGRRSTwrslfGLFPKEEKQralaALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1176 IGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTAR--TIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1952-2160 |
5.91e-31 |
|
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: 122.93 E-value: 5.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1952 IIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslghvdshsSLVGYCPQEDA-------- 2023
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE-----------DITGLPPHEIArlgigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2024 -----LDDLvTVEE----------HLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIG 2088
Cdd:cd03219 82 qiprlFPEL-TVLEnvmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2089 KPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKS 2160
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1028-1235 |
7.91e-31 |
|
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: 122.21 E-value: 7.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGS----KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-------KTDLh 1096
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekeLAAF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1097 tVRKNMGVCMQHDVLFSYLTTKEHLLLYGSI-KVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIAL 1175
Cdd:cd03255 80 -RRRHIGFVFQSFNLLPDLTALENVELPLLLaGVP---KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1176 IGGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTA-RTIILSTHHLDEAEvLSDRIAFLEQG 1235
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRElNKEAgTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1022-1235 |
3.13e-30 |
|
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: 120.86 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1022 KDLTVGvalhgvtkiYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHT---V 1098
Cdd:COG0410 7 ENLHAG---------YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLPPhriA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1099 RKNMGVCMQHDVLFSYLTTKEHLLL----YGSIKVPHWTKKQLHEEVKRtlkdtgLYSHRHKRVGTLSGGMKRKLSISIA 1174
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLLgayaRRDRAEVRADLERVYELFPR------LKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1175 LIGGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEIADRAYVLERG 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1028-1238 |
5.52e-30 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 119.67 E-value: 5.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQ 1107
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:cd03301 80 NYALYPHMTVYDNIAF--GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1188 STGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1954-2148 |
9.05e-30 |
|
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: 120.14 E-value: 9.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSH-------------SSLvgycpq 2020
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR--DITGLPPHriarlgiartfqnPRL------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 edaLDDLvTVEEHL----------YFYARVHGIP-----EKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALA 2085
Cdd:COG0411 91 ---FPEL-TVLENVlvaaharlgrGLLAALLRLPrarreEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2086 LIGKPSILLLDEPSSGMDPKSKRHLWKIIsEEV--QNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELI-RRLrdERGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1953-2153 |
1.40e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 118.40 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslgHVDSHSSLVGYCPQEDALD-DL-VTV 2030
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQRRSIDrDFpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EE----HLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2106
Cdd:cd03235 88 RDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881501 2107 KRHLWKIISEEVQNKCSVILTSHSMEECEALCTRlAIMVNGKFQCIG 2153
Cdd:cd03235 168 QEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1035-1235 |
1.50e-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: 118.13 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1035 KIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKtdLHTVRKNMGVCMQH--DVLF 1112
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGYVMQDvdYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1113 SYlTTKEHLLLygsikvphwTKKQLHEEVKRT---LKDTGLYS--HRHKRvgTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:cd03226 86 TD-SVREELLL---------GLKELDAGNEQAetvLKDLDLYAlkERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 1188 STGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03226 154 TSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1941-2148 |
1.85e-29 |
|
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: 118.38 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK---TGSLGHVDSHSSLVGY 2017
Cdd:cd03257 7 LSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2018 CPQE--DALDDLVTVEEHLYFYARVHGIPEKD--IKETVHKLLRRLHLMP-FKDRATSMCSYGTKRKLSTALALIGKPSI 2092
Cdd:cd03257 87 VFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 2093 LLLDEPSSGMDPKSKRHLWKIISE-EVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKlQEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1941-2158 |
1.94e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 125.40 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKKII-AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK-TGSLGHVD--SHSSLVG 2016
Cdd:COG1123 266 LSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdLTKLSRRSlrELRRRVQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2017 YCPQ--EDALDDLVTVEEHLYFYARVHGI-PEKDIKETVHKLLRRLHLMP-FKDRATSMCSYGTKRKLSTALALIGKPSI 2092
Cdd:COG1123 346 MVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2093 LLLDEPSSGMDPKSKRHLWKIIsEEVQNK--CSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:COG1123 426 LILDEPTSALDVSVQAQILNLL-RDLQRElgLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1953-2166 |
4.06e-29 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 117.72 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHSSLVGYCPQEDALDDLVTVEE 2032
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK--DITNLPPHKRPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLwK 2112
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM-Q 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2113 IISEEVQNKC--SVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI----KSRFGRGF 2166
Cdd:cd03300 171 LELKRLQKELgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRFVADF 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1031-1250 |
5.49e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.44 E-value: 5.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1031 HGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDL--HT-VRKNMGVCMQ 1107
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLpmHKrARLGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLLLYGSIKVPhwTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:COG1137 86 EASIFRKLTVEDNILAVLELRKL--SKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 1188 STGVDPCSRRSIWDVISKNKTaRTI-ILST-HHLDEAEVLSDRIAFLEQGGLRCCGSP-----------FYLKEAF 1250
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKE-RGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPeeilnnplvrkVYLGEDF 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1018-1256 |
2.50e-28 |
|
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: 122.57 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1018 EPEPKDLTVGVALHGVTKIY--GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-D 1094
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1095 LHTVRKNMGVCMQHDVLFSylTT-KEHLLLygsikvphwTKKQL-HEEVKRTLKDTGLyshrHK-----------RVG-- 1159
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFD--TTlRENLRL---------ARPDAtDEELWAALERVGL----GDwlaalpdgldtWLGeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1160 --TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEvLSDRIAFLEQGGL 1237
Cdd:COG4987 469 grRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRI 547
|
250
....*....|....*....
gi 27881501 1238 RCCGSPFYLKEAFGDGYHL 1256
Cdd:COG4987 548 VEQGTHEELLAQNGRYRQL 566
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1923-2172 |
2.54e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 119.55 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1923 RLRVESGAAEFDLVQLYCLTKTYQLIHkkiiAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKt 2002
Cdd:PRK11607 7 RPQAKTRKALTPLLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2003 gSLGHVDSHSSLVGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLST 2082
Cdd:PRK11607 82 -DLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2083 ALALIGKPSILLLDEPSSGMDPKSK-RHLWKI--ISEEVQNKCsvILTSHSMEECEALCTRLAIMVNGKFQCIGS----L 2155
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRdRMQLEVvdILERVGVTC--VMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiY 238
|
250
....*....|....*..
gi 27881501 2156 QHIKSRFGRGFTVKVHL 2172
Cdd:PRK11607 239 EHPTTRYSAEFIGSVNV 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1028-1235 |
2.75e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.67 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKdiKTDLHTVRK--NMGVC 1105
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK--PVRIRSPRDaiALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 M--QHDVLFSYLTTKEHLLL-YGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVV 1182
Cdd:COG3845 84 MvhQHFMLVPNLTVAENIVLgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1183 ILDEPSTGVDPCSRRSIWDVIsKNKTA--RTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:COG3845 164 ILDEPTAVLTPQEADELFEIL-RRLAAegKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1948-2149 |
3.14e-28 |
|
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: 114.28 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1948 IHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGhvdSHSSLVGYCPQEdaLDD- 2026
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQD--VDYq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2027 --LVTVEEHLYFyarvhGIPEK-DIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:cd03226 84 lfTDSVREELLL-----GLKELdAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 2104 PKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1018-1243 |
5.24e-28 |
|
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: 121.79 E-value: 5.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1018 EPEPKDLTVGVALHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DL 1095
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1096 HTVRKNMGVCMQHDVLFsYLTTKEHLLLYGsikvPHWTKKQLHE--------EVKRTLKDtGLyshrHKRVG----TLSG 1163
Cdd:COG4988 407 ASWRRQIAWVPQNPYLF-AGTIRENLRLGR----PDASDEELEAaleaagldEFVAALPD-GL----DTPLGeggrGLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1164 GMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEvLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTH 555
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1017-1251 |
5.29e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 123.70 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1017 IEPEPKDLTVGVAL--HGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTD 1094
Cdd:NF033858 254 IPPRPADDDDEPAIeaRGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1095 LHTVRKNMGVCMQHDVLFSYLTTKEHLLLYGsiKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIA 1174
Cdd:NF033858 334 DIATRRRVGYMSQAFSLYGELTVRQNLELHA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1175 LIGGSRVVILDEPSTGVDPCSRRSIWDVISknKTAR----TIILSTHHLDEAEvLSDRIAFLEQGGLRCCGSPFYLKEAF 1250
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLI--ELSRedgvTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAAR 488
|
.
gi 27881501 1251 G 1251
Cdd:NF033858 489 G 489
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1032-1243 |
1.74e-27 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 113.14 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDL--HT-VRKNMGVCMQH 1108
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLpmHErARLGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYLTTKEHLLLYGSIkVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:TIGR04406 85 ASIFRKLTVEENIMAVLEI-RKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1189 TGVDPCSRRSIWDVISKNKtARTI-ILST-HHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLK-ERGIgVLITdHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1043-1243 |
1.76e-27 |
|
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: 113.20 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1043 VDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQHDVLFSYLTTKEHLL 1122
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1123 lYGsIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIW-- 1200
Cdd:cd03299 94 -YG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRee 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881501 1201 --DVISKNKTarTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03299 172 lkKIRKEFGV--TVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1028-1243 |
3.10e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.56 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGvcM- 1106
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIA--Mv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 -QHDVLFSYLTTKEHlLLYGsIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:COG3839 81 fQSYALYPHMTVYEN-IAFP-LKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1186 EPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTP 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1045-1241 |
3.49e-27 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 111.98 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1045 NLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF---GASAGTIFVYGKDIKTdlHTVRKNMGVCMQHDVLFSYLTTKEHL 1121
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKP--DQFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1122 LLYGSIKVP-HWTKKQLHEEVKRT-LKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSI 1199
Cdd:cd03234 103 TYTAILRLPrKSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881501 1200 WDVISK-NKTARTIILSTHHlDEAEV--LSDRIAFLEQGGLRCCG 1241
Cdd:cd03234 183 VSTLSQlARRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1941-2154 |
3.99e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 115.20 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgsLGHVDSHSSLVGYCPQ 2020
Cdd:COG3842 11 VSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD--VTGLPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTK-RklsTALA--LIGKPSILLLDE 2097
Cdd:COG3842 85 DYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VALAraLAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2098 PSSGMDPKSKRHLWkiisEEV-----QNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGS 2154
Cdd:COG3842 162 PLSALDAKLREEMR----EELrrlqrELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1028-1254 |
4.17e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 111.89 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHT---VRKNMGV 1104
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTakiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHDVLFSYLTTKEHLLLYGSIKvphwTKKQLHEEVKRTLK-DTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFA----ERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGG--LRCCGSPFYLKEAFGDGY 1254
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDALLANEAVRSAY 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1028-1237 |
7.28e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.90 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSK----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTVR 1099
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 -KNMGVCMQHDVLFSYLTTKEHL---LLYGSIKvphwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIAL 1175
Cdd:COG1136 85 rRHIGFVFQFFNLLPELTALENValpLLLAGVS-----RKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1176 IGGSRVVILDEPsTG-VDPCSRRSIWDVISK-NKTA-RTIILSTHHLDEAEvLSDRIAFLEQGGL 1237
Cdd:COG1136 160 VNRPKLILADEP-TGnLDSKTGEEVLELLRElNRELgTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1027-1243 |
7.86e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 111.28 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1027 GVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCM 1106
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSYLTTKEHLLLYGSIK--VPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1185 DEPSTGVDPCSRRSI--WDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03296 161 DEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1948-2148 |
8.46e-27 |
|
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: 108.67 E-value: 8.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1948 IHKK---IIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghVDSHSslvgycPQEdal 2024
Cdd:cd03216 6 ITKRfggVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-----VSFAS------PRD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2025 ddlvtveehlyfyARVHGIpekdikETVHKLlrrlhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSSGMDP 2104
Cdd:cd03216 72 -------------ARRAGI------AMVYQL-----------------SVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881501 2105 KSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1955-2154 |
1.24e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 111.29 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSH--SSLVGYCPQEDALDDLVTVEE 2032
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR--DLASLSRRelARRIAYVPQEPPAPFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 --------HLYFYARVhgiPEKDiKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDP 2104
Cdd:COG1120 95 lvalgrypHLGLFGRP---SAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2105 KSKRHLWKIISEEVQNK-CSVILTSHSMEECEALCTRLAIMVNGKFQCIGS 2154
Cdd:COG1120 171 AHQLEVLELLRRLARERgRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1030-1237 |
1.29e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.52 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQH 1108
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYlTTKEHLLLYGSIKVPHWTKKQLHEEVKRTLKDTGLyshRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:COG4619 83 PALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDI---LDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1189 TGVDPCSRRSIWDVISKNKTA--RTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1957-2161 |
1.39e-26 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 110.50 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSslVGYCPQEDALDDLVTVEEHLYF 2036
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 YARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSK---RHLWKI 2113
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKeklREELKK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 2114 ISEEvqNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKSR 2161
Cdd:cd03299 175 IRKE--FGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1030-1235 |
1.62e-26 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 109.90 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIY----GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHTVRKN 1101
Cdd:cd03257 4 VKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1102 MGVCMQhDVLFS---YLTTKEHL---LLygsIKVPHWTKKQLHEEVKRTLKDTGLYSHR-HKRVGTLSGGMKRKLSISIA 1174
Cdd:cd03257 84 IQMVFQ-DPMSSlnpRMTIGEQIaepLR---IHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1175 LIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTAR--TIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1950-2148 |
2.16e-26 |
|
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: 110.17 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1950 KKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGN---IL-----------IRNKtgsLGHVDShsSLV 2015
Cdd:COG1119 16 KTIL--DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerrggedvweLRKR---IGLVSP--ALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 GYCPQEDalddlvTVEEHLY--FYARVhGI---PEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:COG1119 89 LRFPRDE------TVLDVVLsgFFDSI-GLyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1041-1252 |
2.43e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.94 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1041 VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTD---LHTVRKNMGVCMQH--DVLFSyl 1115
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIVFQNpdDQLFA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1116 TTKEHLLLYG--SIKVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDP 1193
Cdd:PRK13639 94 PTVEEDVAFGplNLGLS---KEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1194 CSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEAFGD 1252
Cdd:PRK13639 171 MGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP---KEVFSD 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1941-2148 |
5.37e-26 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 108.82 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI-------------RNKTGSLGH 2007
Cdd:cd03258 7 VSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdgtdltllsgkelRKARRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2008 VDSHSSLvgycpqedaLDDLvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALI 2087
Cdd:cd03258 87 IFQHFNL---------LSSR-TVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2088 GKPSILLLDEPSSGMDPKSKRHLWKIISeEVQNK--CSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLR-DINRElgLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1954-2158 |
6.55e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 114.62 E-value: 6.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGdIIPS----SGNILIRNKTGSLGHVDSHSSLVGYCPQE-DALDDLV 2028
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHggriSGEVLLDGRDLLELSEALRGRRIGMVFQDpMTQLNPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2029 TVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKR 2108
Cdd:COG1123 100 TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2109 HLWKIISEEVQNK-CSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:COG1123 180 EILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1954-2148 |
8.21e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 116.76 E-value: 8.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrnktgsLGH-VDSHS----SLVGYCPQEDALDDLV 2028
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL------FGQpVDAGDiatrRRVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2029 TVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKR 2108
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27881501 2109 HLWKIISE-EVQNKCSVILTSHSMEECEaLCTRLAIMVNGK 2148
Cdd:NF033858 435 MFWRLLIElSREDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1038-1243 |
1.08e-25 |
|
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: 113.84 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1038 GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF---GASAGTIFVYGKDIKTDLHTVR-KNMGVCMQH-DVLF 1112
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGRDLLELSEALRgRRIGMVFQDpMTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1113 SYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVD 1192
Cdd:COG1123 97 NPVTVGDQIAE--ALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1193 PCSRRSIWDVISKNKTAR--TIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG1123 175 VTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1028-1235 |
1.18e-25 |
|
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: 105.20 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIktDLHTVR--KNMGVC 1105
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV--SFASPRdaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 MQHdvlfsylttkehlllygsikvphwtkkQlheevkrtlkdtglyshrhkrvgtLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:cd03216 79 MVY---------------------------Q------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1186 EPSTGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1954-2154 |
1.19e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRN-----KTGSLGHVDSHSSLVGYCPQEDALDDlv 2028
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIRKKVGLVFQYPEYQLFEE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2029 TVEEHLYFYARVHGIPEKDIKETVHKLLR--RLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2106
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2107 KRHLWKIISE-EVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGS 2154
Cdd:PRK13637 180 RDEILNKIKElHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1954-2148 |
1.27e-25 |
|
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: 107.27 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTG--DII---PSSGNILIRNKT--GSLGHVDSHSSLVGYCPQEDALDD 2026
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIpgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2027 LvTVEEHLYFYARVHGI-PEKDIKETVHKLLRRLHLMP-FKDRATSM-CSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:cd03260 95 G-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDeVKDRLHALgLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881501 2104 PKSKRHLWKIIsEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03260 174 PISTAKIEELI-AELKKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1936-2132 |
1.69e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.68 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1936 VQLYCLTKTYQlihKKIIAVNNISIGIPAGE-CFgLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVdSHSSL 2014
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ--DLSRL-KRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 ------VGYCPQeDA--LDDLvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLmpfKDRATSMC---SYGTKRKLSTA 2083
Cdd:COG2884 75 pylrrrIGVVFQ-DFrlLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGL---SDKAKALPhelSGGEQQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2084 LALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSME 2132
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1020-1256 |
2.40e-25 |
|
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: 114.55 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1020 EPKDLTVGVALHGVTKIYG--SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLH 1096
Cdd:COG2274 466 SLPRLKGDIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1097 TVRKNMGVCMQHDVLFSylttkehlllyGSIK------VPHWTKkqlhEEVKRTLKDTGLYS--HRHK-----RVG---- 1159
Cdd:COG2274 546 SLRRQIGVVLQDVFLFS-----------GTIRenitlgDPDATD----EEIIEAARLAGLHDfiEALPmgydtVVGeggs 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1160 TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEvLSDRIAFLEQGGLRC 1239
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVE 689
|
250
....*....|....*..
gi 27881501 1240 CGSPFYLKEAFGDGYHL 1256
Cdd:COG2274 690 DGTHEELLARKGLYAEL 706
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1950-2148 |
2.48e-25 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 106.46 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1950 KKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghvdshSSLVGYcpqEDALDDLVT 2029
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---------SSLLGL---GGGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2030 VEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRH 2109
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 27881501 2110 LWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1030-1235 |
2.72e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.85 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHD 1109
Cdd:COG1118 5 VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVFQHY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHlLLYGsIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:COG1118 85 ALFPHMTVAEN-IAFG-LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 1190 GVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:COG1118 163 ALDAKVRKELRRWLRRlhDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1954-2158 |
4.67e-25 |
|
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: 106.27 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSlgHVDSHSSLVGYCPQEDALDDLVTVEEH 2033
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARVHGI----PEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRH 2109
Cdd:cd03296 95 VAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2110 L--W-KIISEEVqNKCSVILTsHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:cd03296 175 LrrWlRRLHDEL-HVTTVFVT-HDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1941-2158 |
7.50e-25 |
|
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: 105.46 E-value: 7.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKkiiAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK-TGSLGHVDSHSSLvGYCP 2019
Cdd:cd03295 6 VTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdIREQDPVELRRKI-GYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2020 QEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMP--FKDRATSMCSYGTKRKLSTALALIGKPSILLLDE 2097
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 2098 PSSGMDPKSKRHL---WKIISEEVqNKcSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:cd03295 162 PFGALDPITRDQLqeeFKRLQQEL-GK-TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1941-2148 |
1.15e-24 |
|
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: 103.04 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK--TGSLGHVDSHSSLVGYC 2018
Cdd:cd03229 6 VSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdlTDLEDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2019 PQEDALddlvtveehlyfyarvhgIPEKDIKETVHKLLrrlhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEP 2098
Cdd:cd03229 82 FQDFAL------------------FPHLTVLENIALGL----------------SGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2099 SSGMDPKSKRHLWKIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1955-2158 |
1.17e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.98 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL-VGYCPQEDALDDLVTVEEH 2033
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARV-HGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:PRK10895 99 LMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 2113 IISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:PRK10895 179 IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1955-2153 |
1.31e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 102.90 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSH--SSLVGYCPQedalddlvtvee 2032
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK--DLASLSPKelARKIAYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 hlyfyarvhgipekdiketvhkLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:cd03214 81 ----------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27881501 2113 IISEEVQNK-CSVILTSHSMEECEALCTRLAIMVNGKFQCIG 2153
Cdd:cd03214 139 LLRRLARERgKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1956-2159 |
1.39e-24 |
|
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: 104.51 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1956 NNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI------RNKTGSLGHVDSHsslVGYCPQEDALDDLVT 2029
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedisGLSEAELYRLRRR---MGMLFQSGALFDSLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2030 VEEHLYFYARVHGI-PEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKR 2108
Cdd:cd03261 94 VFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 2109 ---HLwkIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIK 2159
Cdd:cd03261 174 vidDL--IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1235 |
2.27e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNMGVCMQ--HDVLFSylTTK 1118
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGLVFQdpDDQVFS--STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1119 EHLLLYGSIKVpHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRS 1198
Cdd:PRK13647 98 WDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881501 1199 IWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK13647 177 LMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1936-2153 |
2.38e-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: 103.10 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1936 VQLYCLTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslghvdshssLV 2015
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR------------DV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 GYCPQED----------ALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALA 2085
Cdd:cd03301 65 TDLPPKDrdiamvfqnyALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2086 LIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGKFQCIG 2153
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1032-1243 |
3.20e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIY--GS---KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI---KTDLHTVRKNMG 1103
Cdd:PRK13637 7 NLTHIYmeGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VCMQHDVLFSYLTTKEHLLLYGSIKVpHWTKKQLHEEVKRTLKDTGL-YS-HRHKRVGTLSGGMKRKLSISIALIGGSRV 1181
Cdd:PRK13637 87 LVFQYPEYQLFEETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLdYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1182 VILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1949-2154 |
3.43e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1949 HKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSL---GhvdshsslVGYCPqedald 2025
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALlelG--------AGFHP------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 DLvTVEEHLYFYARVHGIPEKDIKETVHK------LLRRLHlMPFKdratsMCSYGTKRKLSTALALIGKPSILLLDEPS 2099
Cdd:COG1134 102 EL-TGRENIYLNGRLLGLSRKEIDEKFDEivefaeLGDFID-QPVK-----TYSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2100 SGMDP----KSKRHlwkiISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGS 2154
Cdd:COG1134 175 AVGDAafqkKCLAR----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1032-1235 |
4.00e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.92 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIK--TDLHTVRKNMGVCMQHD 1109
Cdd:PRK11300 10 GLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRTFQHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHLL-----------LYGSIKVPHWTKKQlHEEVKRT---LKDTGLYSHRHKRVGTLSGGMKRKLSISIAL 1175
Cdd:PRK11300 90 RLFREMTVIENLLvaqhqqlktglFSGLLKTPAFRRAE-SEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1176 IGGSRVVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1043-1235 |
5.29e-24 |
|
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: 102.93 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1043 VDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKnmgVCMQHDVLFSYLTTKEHLL 1122
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1123 LYGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDV 1202
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 27881501 1203 ISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:TIGR01184 157 LMQiwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1949-2148 |
5.58e-24 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 102.51 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1949 HKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHSSL---VGYCPQEDALD 2025
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR--DITGLPPHERAragIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 DLVTVEEHL--YFYARVHGIPEKDIKEtVHKLLRRLHLMpFKDRATSMcSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:cd03224 88 PELTVEENLllGAYARRRAKRKARLER-VYELFPRLKER-RKQLAGTL-SGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881501 2104 PKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03224 165 PKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1017-1237 |
8.29e-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: 101.09 E-value: 8.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1017 IEPEPKDLTVGVAlHGVTKiyGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGL--FGASAGTIFVYGKDIktD 1094
Cdd:cd03213 2 VTLSFRNLTVTVK-SSPSK--SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL--D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1095 LHTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVphwtkkqlheevkrtlkdtglyshrhkrvgtLSGGMKRKLSISIA 1174
Cdd:cd03213 77 KRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLRG-------------------------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1175 LIGGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHL-DEAEVLSDRIAFLEQGGL 1237
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1028-1235 |
8.53e-24 |
|
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: 102.57 E-value: 8.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSK----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNM 1102
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1103 GVCMQHDvlfsylttkehlllYGSIKvPHWT-KKQLHE------------EVKRTLKDTGLY-SHRHKRVGTLSGGMKRK 1168
Cdd:COG1124 82 QMVFQDP--------------YASLH-PRHTvDRILAEplrihglpdreeRIAELLEQVGLPpSFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1169 LSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTAR--TIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1941-2148 |
8.71e-24 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 101.80 E-value: 8.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI----------------RNKTgs 2004
Cdd:cd03255 6 LSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdgtdisklsekelaafRRRH-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2005 lghvdshsslVGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLmpfKDRATSMC---SYGTKRKLS 2081
Cdd:cd03255 84 ----------IGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGL---GDRLNHYPselSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2082 TALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNK-CSVILTSHSMEEcEALCTRLAIMVNGK 2148
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1028-1235 |
8.75e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.05 E-value: 8.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTVRKNM 1102
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1103 GVCMQhDV-LFSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRV 1181
Cdd:COG2884 82 GVVFQ-DFrLLPDRTVYENVAL--PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1182 VILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1954-2148 |
1.04e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghVDShsSLVGYCPQEDALDDLVTVEEH 2033
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-----IDY--SRKGLMKLRESVGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARVH----------GIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:PRK13636 94 QLFSASVYqdvsfgavnlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 2104 PKSKRHLWKIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1028-1223 |
1.55e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 109.06 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVR-------- 1099
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpriaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 -----KNmgvcmqhdvLFSYLTTKEHLL----LYGsikvpHwTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLS 1170
Cdd:NF033858 82 pqglgKN---------LYPTLSVFENLDffgrLFG-----Q-DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 1171 ISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTAR---TIILSTHHLDEAE 1223
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAE 202
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1028-1235 |
2.31e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 103.62 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSK----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTVR 1099
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 KNMGVCMQHDVLFSYLTTkehlllYGSI----KVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIAL 1175
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTV------AENValplEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1176 IGGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTAR-TIILSTHhldEAEV---LSDRIAFLEQG 1235
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDiNRELGlTIVLITH---EMDVvrrICDRVAVLENG 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1030-1243 |
2.35e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 101.70 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNMGVCMQH 1108
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYLTTKEhLLLYGsiKVPHwTKKQL----HEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:COG4604 84 NHINSRLTVRE-LVAFG--RFPY-SKGRLtaedREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1185 DEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRlaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1252 |
3.08e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI---KTDLHTVRKNMGVCMQH--DVLFSYLT 1116
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEhlLLYG--SIKVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPC 1194
Cdd:PRK13636 101 YQD--VSFGavNLKLP---EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1195 SRRSIWDVI--SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEAFGD 1252
Cdd:PRK13636 176 GVSEIMKLLveMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP---KEVFAE 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1028-1243 |
3.87e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.87 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI------KTDLHTVrkn 1101
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaeNRHVNTV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1102 mgvcMQHDVLFSYLTTKEHlLLYG--SIKVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGS 1179
Cdd:PRK09452 92 ----FQSYALFPHMTVFEN-VAFGlrMQKTP---AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 1180 RVVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1042-1237 |
4.40e-23 |
|
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: 99.97 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFsYLTTKEH 1120
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1121 LLLygsiKVPHWTKkqlhEEVKRTLKDTGL--YSHRHKR-----VG----TLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:cd03245 98 ITL----GAPLADD----ERILRAAELAGVtdFVNKHPNgldlqIGergrGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1190 GVDPCSRRSIWDVISKNKTARTIILSTHH---LDeaevLSDRIAFLEQGGL 1237
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDKTLIIITHRpslLD----LVDRIIVMDSGRI 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1033-1243 |
5.09e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 100.35 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1033 VTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHT-VRKNMGVCMQHDV 1110
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlPLHArARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1111 LFSYLTTKEHLLLYGSIKvPHWTKKQLHEEVKRTLKDTGLySHRHKRVG-TLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIR-DDLSAEQREDRANELMEEFHI-EHLRDSMGqSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1190 GVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK10895 167 GVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1028-1243 |
7.46e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 99.78 E-value: 7.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYG---KDIKTDLHTVRKNMGV 1104
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHDVLFSYLTTKEHlLLYGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:PRK09493 82 VFQQFYLFPHLTALEN-VMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1185 DEPSTGVDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1935-2158 |
1.16e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.33 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1935 LVQLYCLTKTYQliHKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgsLGHVDSHSSL 2014
Cdd:PRK09452 14 LVELRGISKSFD--GKEVI--SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILL 2094
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2095 LDEPSSGMDPKskrhLWKIISEEV---QNKCSV--ILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:PRK09452 168 LDESLSALDYK----LRKQMQNELkalQRKLGItfVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1028-1243 |
2.17e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 101.33 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKtdlHTVRKNMGVCM- 1106
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQRDICMv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 -QHDVLFSYLTTKEHlLLYGsIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:PRK11432 84 fQSYALFPHMSLGEN-VGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1186 EPSTGVDPCSRRSIWDVISKNKTARTI--ILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1033-1235 |
2.26e-22 |
|
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: 97.48 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1033 VTKIYGSKV-AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHT-----VRKNMGVCM 1106
Cdd:cd03292 6 VTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGraipyLRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLySHRHKRVGT-LSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:cd03292 85 QDFRLLPDRNVYENVAF--ALEVTGVPPREIRKRVPAALELVGL-SHKHRALPAeLSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1186 EPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1952-2160 |
2.66e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1952 IIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK--TGSLGHVDSHSSLVGYCPQEDALDDLVT 2029
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhiEGLPGHQIARMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2030 VE-----EHLYFYARV-HGI--------PEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLL 2095
Cdd:PRK11300 98 IEnllvaQHQQLKTGLfSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2096 DEPSSGMDPKSKRHLWKIISE-EVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKS 2160
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAElRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1955-2148 |
3.17e-22 |
|
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: 96.47 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPS--SGNILIRNKTGSLghvDSHSSLVGYCPQEDALDDLVTVEE 2032
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFYARVHGIpekdiketvhkllrrlhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:cd03213 102 TLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 27881501 2113 IISEEVQNKCSVILTSHSM-EECEALCTRLAIMVNGK 2148
Cdd:cd03213 153 LLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGR 189
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1040-1235 |
3.93e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.78 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1040 KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCM-QHDVLFSYLTTK 1118
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1119 EHLLLYGSI-KVPHWTKKQLHEEVKRTLKDTGLYshrHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRR 1197
Cdd:COG4586 115 DSFRLLKAIyRIPDAEYKKRLDELVELLDLGELL---DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27881501 1198 SIWDVISK-NKTAR-TIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:COG4586 192 AIREFLKEyNRERGtTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1948-2153 |
4.42e-22 |
|
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: 96.60 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1948 IHKKIIAVN-NISIGIPaGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI--------RNKTgslgHVDSHSSLVGYC 2018
Cdd:cd03297 6 IEKRLPDFTlKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsRKKI----NLPPQQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2019 PQEDALDDLVTVEEHLYFYARVHgiPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEP 2098
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRK--RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2099 SSGMDPKSKRHLWKIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGKFQCIG 2153
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1037-1237 |
4.91e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTT---TISMLTGLFG--ASAGTIFVYGKDI---KTDLHTVRKNMGVCMQH 1108
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSyLTTKEHLLlYG----SIKvphwTKKQLHEEVKRTLKDTGLYS----HRHKRVGTLSGGMKRKLSISIALIGGSR 1180
Cdd:PRK14239 95 PNPFP-MSIYENVV-YGlrlkGIK----DKQVLDEAVEKSLKGASIWDevkdRLHDSALGLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1181 VVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:PRK14239 169 IILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1028-1229 |
7.58e-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: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKtdLHTVR--KNMGVC 1105
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRdaQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 M--QHDVLFSYLTTKEHLLL------YGSIKvphwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIG 1177
Cdd:COG1129 83 IihQELNLVPNLSVAENIFLgreprrGGLID-----WRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1178 GSRVVILDEPSTGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRI 1229
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRV 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1950-2148 |
1.01e-21 |
|
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: 96.19 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1950 KKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPS---SGNILIRNKTGSLGHVDSHsslVGYCPQEDALDD 2026
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC---VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2027 LVTVEEHLYFYARVHGiPEK-----DIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSG 2101
Cdd:cd03234 95 GLTVRETLTYTAILRL-PRKssdaiRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 2102 MDPKSKRHLWKIISEEVQNKCSVILTSHS-MEECEALCTRLAIMVNGK 2148
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGE 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1951-2148 |
1.04e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.20 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1951 KIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHSSL---VGYCPQEDAL-DD 2026
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE--DITGLPPHRIArlgIGYVPEGRRIfPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2027 LvTVEEHLY--FYARVHGIPEKDIKETVHKLLRRLHLMpFKDRATSMcSYGTKRKLSTALALIGKPSILLLDEPSSGMDP 2104
Cdd:COG0410 93 L-TVEENLLlgAYARRDRAEVRADLERVYELFPRLKER-RRQRAGTL-SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881501 2105 KSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG0410 170 LIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1046-1235 |
1.12e-21 |
|
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: 95.64 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1046 LNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQHDVLFSYLTTKEHLLLyG 1125
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGL-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1126 SIKVPHWTKKQlHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK 1205
Cdd:cd03298 95 LSPGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|..
gi 27881501 1206 --NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03298 174 lhAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1037-1237 |
1.26e-21 |
|
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: 96.25 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCM-QHDVLFSYL 1115
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1116 TTKEHLLLYGSI-KVPHWTKKQLHEEVKRTLKDTGLYshrHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPC 1194
Cdd:cd03267 111 PVIDSFYLLAAIyDLPPARFKKRLDELSELLDLEELL---DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881501 1195 SRRSIWDVISK-NK-TARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:cd03267 188 AQENIRNFLKEyNReRGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1037-1235 |
1.33e-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: 95.76 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKV-AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSY 1114
Cdd:cd03254 12 YDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 lTTKEHLLLYGSI----KVPHWTK-KQLHEEVKRtLKDtGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:cd03254 92 -TIMENIRLGRPNatdeEVIEAAKeAGAHDFIMK-LPN-GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 1190 GVDPCSRRSIWDVISKNKTARTIILSTHHLDEAeVLSDRIAFLEQG 1235
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKGRTSIIIAHRLSTI-KNADKILVLDDG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1954-2148 |
1.56e-21 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 102.22 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHS--SLVGYCPQEDAL-DDlvTV 2030
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI--DLRQIDPASlrRQIGVVLQDVFLfSG--TI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEHLYFYARvhGIPEKDIKET-----VHKLLRRLHL---MPFKDRATSMcSYGTKRKLSTALALIGKPSILLLDEPSSGM 2102
Cdd:COG2274 566 RENITLGDP--DATDEEIIEAarlagLHDFIEALPMgydTVVGEGGSNL-SGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 2103 DPKSKRHLWKIISEEVQNkCSVILTSHSMeECEALCTRLAIMVNGK 2148
Cdd:COG2274 643 DAETEAIILENLRRLLKG-RTVIIIAHRL-STIRLADRIIVLDKGR 686
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1039-1264 |
1.62e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.60 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1039 SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTD-LHTVRKNMGVCMQH-DVLFSYLT 1116
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGIIFQNpDNQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEHlLLYG--SIKVPHWTKKQLHEEVKrtlKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPC 1194
Cdd:PRK13632 101 VEDD-IAFGleNKKVPPKKMKDIIDDLA---KKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1195 SRRSIWDVIS--KNKTARTIILSTHHLDEAeVLSDRIAFLEQGGLRCCGSPfylKEAFGDGYHLTLTKKKSP 1264
Cdd:PRK13632 177 GKREIKKIMVdlRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKP---KEILNNKEILEKAKIDSP 244
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1039-1250 |
1.77e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.70 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1039 SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHT--VRKNMGVCMQH-------- 1108
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdIRNKAGMVFQNpdnqivat 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 ----DVLFSylttKEHLllygsiKVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:PRK13633 102 iveeDVAFG----PENL------GIP---PEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1185 DEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAeVLSDRIAFLEQGGLRCCGSPfylKEAF 1250
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP---KEIF 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1037-1243 |
2.04e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.85 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTdlHTVR---KNMGVCMQHDVLFS 1113
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM--LSSRqlaRRLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1114 YLTTKEhLLLYG-SIKVPHWTK--KQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTG 1190
Cdd:PRK11231 90 GITVRE-LVAYGrSPWLSLWGRlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1191 VDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK11231 169 LDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1941-2144 |
2.04e-21 |
|
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: 95.19 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIH---KKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGS--LGHVDSHSSL- 2014
Cdd:COG4778 10 LSKTFTLHLqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdLAQASPREILa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 -----VGYC-------PQEDALDdlvTVEEHLyfyaRVHGIPEKDIKETVHKLLRRL-------HLMPfkdrATSmcSYG 2075
Cdd:COG4778 90 lrrrtIGYVsqflrviPRVSALD---VVAEPL----LERGVDREEARARARELLARLnlperlwDLPP----ATF--SGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2076 TKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIM 2144
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1954-2148 |
2.05e-21 |
|
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: 93.22 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHS--SLVGYCPQEDAL-DDlvTV 2030
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV--DLRDLDLESlrKNIAYVPQDPFLfSG--TI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEHLYfyarvhgipekdiketvhkllrrlhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHL 2110
Cdd:cd03228 93 RENIL-------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881501 2111 WKIISEEVQNKcSVILTSHSMEECEaLCTRLAIMVNGK 2148
Cdd:cd03228 136 LEALRALAKGK-TVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1257 |
2.69e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.97 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQ------------H 1108
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLRKHIGIVFQnpdnqfvgsivkY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYlttKEHLllygsikVPHwtkKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:PRK13648 104 DVAFGL---ENHA-------VPY---DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1189 TGVDPCSRRSIWDVISKNKTAR--TIILSTHHLDEAeVLSDRIAFLEQGGLRCCGSPfylKEAFGDGYHLT 1257
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTP---TEIFDHAEELT 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1955-2165 |
2.96e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQeDALDDLV--TVEE 2032
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ-NPDNQFVgaTVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 2113 IISE-EVQNKCSVILTSHSMEECeALCTRLAIMVNGKFQCIGSLQHIksrFGRG 2165
Cdd:PRK13650 182 TIKGiRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL---FSRG 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1037-1237 |
3.44e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.49 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF----GASA-GTIFVYGKDI---KTDLHTVRKNMGVCMQH 1108
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipGARVeGEILLDGEDIydpDVDVVELRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLF--------SYLttkehLLLYGsIKvphwTKKQLHEEVKRTLKDTGLY---SHR-HKRVGTLSGGMKRKLSISIALI 1176
Cdd:COG1117 101 PNPFpksiydnvAYG-----LRLHG-IK----SKSELDEIVEESLRKAALWdevKDRlKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1177 GGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1033-1235 |
4.34e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.46 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1033 VTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF---GASAGTIFVYGKDIKT------DLHTVRKNMG 1103
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlarDIRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VCMQHDVLFSYLTTKEHLLLYGSIKVPHWT------KKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIG 1177
Cdd:PRK09984 90 YIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1178 GSRVVILDEPSTGVDPCSRRSIWDVISK-NKT-ARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDiNQNdGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1935-2158 |
4.90e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.47 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1935 LVQLYCLTKTYQLIHkkiiAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGS-LGHVDSHSS 2013
Cdd:PRK09700 5 YISMAGIGKSFGPVH----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2014 LVGYCPQEDALDDLVTVEEHLYF----YARVHGIPEKDIKETVHK---LLRRLHLMPFKDRATSMCSYGTKRKLSTALAL 2086
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIIDWREMRVRaamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2087 IGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1038-1278 |
6.16e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1038 GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNMGVCMQH--DVLFSy 1114
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQNpdDQIFS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 lTTKEHLLLYGSIKVPHWTKKQLHEeVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPC 1194
Cdd:PRK13652 94 -PTVEQDIAFGPINLGLDEETVAHR-VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1195 SRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP--FYLKEAFGDGYHLTL--TKKKSPNLNA 1268
Cdd:PRK13652 172 GVKELIDFLNDlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDLpsLPKLIRSLQA 251
|
250
....*....|
gi 27881501 1269 NAVCDTMAVT 1278
Cdd:PRK13652 252 QGIAIDMAYT 261
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1951-2170 |
6.91e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 96.73 E-value: 6.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1951 KIIAVNNISIGIPAGECFGLLGVNGAG--KTTIFKMLTGdiiPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDLV 2028
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2029 TVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKR 2108
Cdd:NF000106 102 SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2109 HLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKSRFGrGFTVKV 2170
Cdd:NF000106 182 EVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQI 242
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
993-1235 |
1.18e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 98.70 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 993 LMFTNIMMQNTNPSAS--------PEYMFSSNIEPEPKDLTVGVALHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNG 1063
Cdd:COG1132 297 LANVLNQLQRALASAErifelldePPEIPDPPGAVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1064 AGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSyLTTKEHlLLYGSIKVPhwtkkqlHEEVK 1142
Cdd:COG1132 377 SGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFS-GTIREN-IRYGRPDAT-------DEEVE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1143 RTLKDTGL----------YSHrhkRVG----TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKT 1208
Cdd:COG1132 448 EAAKAAQAhefiealpdgYDT---VVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK 524
|
250 260
....*....|....*....|....*..
gi 27881501 1209 ARTIILSTHHLDEAEvLSDRIAFLEQG 1235
Cdd:COG1132 525 GRTTIVIAHRLSTIR-NADRILVLDDG 550
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1950-2148 |
1.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 94.00 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1950 KKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRN----KTGSLGHVDSHSSLVGYCPQedalD 2025
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsDEENLWDIRNKAGMVFQNPD----N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 DLVT--VEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:PRK13633 97 QIVAtiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 2104 PKSKRHLWKIISEevQNK---CSVILTSHSMEECeALCTRLAIMVNGK 2148
Cdd:PRK13633 177 PSGRREVVNTIKE--LNKkygITIILITHYMEEA-VEADRIIVMDSGK 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1030-1235 |
1.96e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.51 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAvdNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQHD 1109
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEHLLLyG---SIKVphwTKKQlHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:COG3840 81 NLFPHLTVAQNIGL-GlrpGLKL---TAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1187 PSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:COG3840 156 PFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1954-2161 |
3.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDalDDLV---TV 2030
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNP--DDQIfspTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHL 2110
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2111 WKIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKSR 2161
Cdd:PRK13652 177 IDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1028-1235 |
3.38e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.06 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYG--SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVC 1105
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 MQHDVLFsylttkehlllygsikvphwtkkqlheevkrtlkDTGLYSHRHKRvgtLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:cd03247 81 NQRPYLF----------------------------------DTTLRNNLGRR---FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881501 1186 EPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLsDRIAFLEQG 1235
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENG 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1037-1237 |
7.22e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.44 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF-----GASAGTIFVYGKDI---KTDLHTVRKNMGVCMQH 1108
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIyspDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYLTTKEHLLLYGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRV----GTLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLndypSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1185 DEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1956-2162 |
7.78e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1956 NNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIliRNKTGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHLY 2035
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI--RFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2036 FYARVhgIPEKD------IKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRH 2109
Cdd:PRK10851 97 FGLTV--LPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2110 L--W-KIISEEVqnKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI----KSRF 2162
Cdd:PRK10851 175 LrrWlRQLHEEL--KFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepATRF 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1941-2098 |
1.02e-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: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQliHKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGslghvdshsslVGYCPQ 2020
Cdd:COG0488 4 LSKSFG--GRPLL--DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTV----------------------------EEHLYFYARVHGIPEK----DIKETVHKLLRRLHLMPFK-DR 2067
Cdd:COG0488 69 EPPLDDDLTVldtvldgdaelraleaeleeleaklaepDEDLERLAELQEEFEAlggwEAEARAEEILSGLGFPEEDlDR 148
|
170 180 190
....*....|....*....|....*....|.
gi 27881501 2068 ATSMCSYGTKRKLSTALALIGKPSILLLDEP 2098
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1040-1242 |
1.11e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1040 KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFG------ASAGTIFVYGKDI-KTDLHTVRKNMGVCMQHDVLF 1112
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1113 SylttkeHLLLYGSIKVPHWT-----KKQLHEEVKRTLKDTGLYSHRHKRVGT----LSGGMKRKLSISIALIGGSRVVI 1183
Cdd:PRK14246 103 P------HLSIYDNIAYPLKShgikeKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGS 1242
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1045-1238 |
1.49e-19 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 89.28 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1045 NLNLNF-YEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGK-----DIKTDLHTVRKNMGVCMQHDVLFSYLTTK 1118
Cdd:cd03297 14 TLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1119 EHLLlYGSIKVPHWTKKQLHEEVKRTLkdtGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRS 1198
Cdd:cd03297 94 ENLA-FGLKRKRNREDRISVDELLDLL---GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27881501 1199 IWDVISKNKTARTI--ILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:cd03297 170 LLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1042-1243 |
1.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIK--TDLHTVRKNMGVCMQHDVLFSYLTTKE 1119
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIVFQNPETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1120 HLLLYG--SIKVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRR 1197
Cdd:PRK13644 97 EDLAFGpeNLCLP---PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881501 1198 SIWDVISK-NKTARTIILSTHHLDEAEVlSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK13644 174 AVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEP 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1954-2148 |
2.14e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.52 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKT-----GSLGHVDSHSSLVGYCPqedalDDLV 2028
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkKSLLEVRKTVGIVFQNP-----DDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2029 ---TVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPK 2105
Cdd:PRK13639 92 fapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881501 2106 SKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1941-2148 |
2.77e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.79 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI--RNKTG-----------SLGH 2007
Cdd:PRK11153 7 ISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgQDLTAlsekelrkarrQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2008 VDSH----SSLvgycpqedalddlvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTA 2083
Cdd:PRK11153 87 IFQHfnllSSR--------------TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2084 LALIGKPSILLLDEPSSGMDPKSKR---HLWKIISEEVqnKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRsilELLKDINREL--GLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1954-2158 |
2.81e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.05 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQE-DALDDLVTVEE 2032
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNpDNQFIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:PRK13632 104 DIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 2113 IISE--EVQNKCsVILTSHSMEECeALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:PRK13632 184 IMVDlrKTRKKT-LISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1942-2148 |
3.91e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 88.23 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1942 TKTYQlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL---VGYC 2018
Cdd:cd03292 7 TKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2019 PQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEP 2098
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881501 2099 SSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1029-1190 |
4.40e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 89.02 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1029 ALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVrKNMGVC-- 1105
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLtGLDEHEI-ARLGIGrk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 MQHDVLFSYLTTKEHLLL--------YGSIKvpHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIG 1177
Cdd:COG4674 91 FQKPTVFEELTVFENLELalkgdrgvFASLF--ARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQ 168
|
170
....*....|...
gi 27881501 1178 GSRVVILDEPSTG 1190
Cdd:COG4674 169 DPKLLLLDEPVAG 181
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1023-1266 |
4.47e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.07 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1023 DLTVGVALHGVTKIYGSKV-----AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHT 1097
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1098 V------RKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVPHwTKKQLHEEVKRTLKDTGLYSHRHKRVG-TLSGGMKRKLS 1170
Cdd:PRK13645 82 IkevkrlRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGE-NKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1171 ISIALIGGSRVVILDEPSTGVDPCSRR---SIWDVISKNKTARtIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFylk 1247
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKR-IIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF--- 236
|
250
....*....|....*....
gi 27881501 1248 EAFGDGYHLTLTKKKSPNL 1266
Cdd:PRK13645 237 EIFSNQELLTKIEIDPPKL 255
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1957-2129 |
4.63e-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: 87.41 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVgYCPQEDALDDLVTVEEHLYF 2036
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIL-YLGHLPGLKPELSALENLHF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 YARVHGipekDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISE 2116
Cdd:TIGR01189 97 WAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
170
....*....|...
gi 27881501 2117 EVQNKCSVILTSH 2129
Cdd:TIGR01189 173 HLARGGIVLLTTH 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1050-1255 |
5.32e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.57 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1050 FYEGHITSLLGPNGAGKTTTISML-----TGLFGAsaGTIFVYGKDIktDLHTVRKNMGVCMQHDVLFSYLTTKEHLLLY 1124
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALafrspKGVKGS--GSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1125 GSIKVP-HWTKKQLHEEVKRTLKDTGLYSHRHKRVGT------LSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRR 1197
Cdd:TIGR00955 124 AHLRMPrRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1198 SIWDVISKNKTARTIILSTHHLDEAEV--LSDRIAFLEQGGLRCCGSPFYLKEAFGDGYH 1255
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSPDQAVPFFSDLGH 263
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1954-2149 |
5.83e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHV-DSHSSLVGYCPQEDAL-DDLvTVE 2031
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLvPNL-SVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 EHLYF--YARVHG-IPEKDIKETVHKLLRRLHLM--PfkDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2106
Cdd:COG1129 98 ENIFLgrEPRRGGlIDWRAMRRRARELLARLGLDidP--DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTERE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881501 2107 KRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:COG1129 176 VERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1917-2158 |
6.90e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.94 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1917 EDVRAERlRVESGAaefDLVQLYCLTKTYQLIHKKII-AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGN 1995
Cdd:TIGR03269 265 SEVEKEC-EVEVGE---PIIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1996 ILIR--------NKTGSLGHvDSHSSLVGYCPQEDALDDLVTVEEHL-----------------YFYARVHGIPEKDIKE 2050
Cdd:TIGR03269 341 VNVRvgdewvdmTKPGPDGR-GRAKRYIGILHQEYDLYPHRTVLDNLteaiglelpdelarmkaVITLKMVGFDEEKAEE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2051 TVHKLlrrlhlmpfkdraTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKII--SEEVQNKCSVILtS 2128
Cdd:TIGR03269 420 ILDKY-------------PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIV-S 485
|
250 260 270
....*....|....*....|....*....|
gi 27881501 2129 HSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:TIGR03269 486 HDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1954-2189 |
7.45e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.92 E-value: 7.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQE-DalDDLV--TV 2030
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNpD--NQFVgaTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHL 2110
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2111 WKIISEEVQNK-CSVILTSHSMEECeALCTRLAIMVNGKFQCIGSLQHIksrFGRG-----------FTVK--------- 2169
Cdd:PRK13635 180 LETVRQLKEQKgITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI---FKSGhmlqeigldvpFSVKlkellkrng 255
|
250 260
....*....|....*....|.
gi 27881501 2170 VHLKNNKVTMETLTKFM-QLH 2189
Cdd:PRK13635 256 ILLPNTYLTMESLVDELwTLH 276
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1037-1261 |
8.11e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF-----GASAGTIFVYGKDI-KTDLHTVRKNMGVCMQHDV 1110
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1111 LFSYLTTKEHLLLYGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRV----GTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1187 PSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSpfyLKEAFGDGYHlTLTKK 1261
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP---TREVFTNPRH-ELTEK 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1037-1243 |
9.30e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 9.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSYL 1115
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1116 TTKEhllLYGSIKVPH------WtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:PRK10253 97 TVQE---LVARGRYPHqplftrW-RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 1190 GVDPCSRRSIWDVISK-NKT-ARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK10253 173 WLDISHQIDLLELLSElNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1019-1219 |
1.39e-18 |
|
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: 92.04 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1019 PEPKDLTVGVA---LHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTD 1094
Cdd:TIGR02868 323 PAAGAVGLGKPtleLRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1095 LHT-VRKNMGVCMQHDVLFSyLTTKEHLLLyGSIKVPHwtkkqlhEEVKRTLKDTGLYSH-------RHKRVG----TLS 1162
Cdd:TIGR02868 403 DQDeVRRRVSVCAQDAHLFD-TTVRENLRL-ARPDATD-------EELWAALERVGLADWlralpdgLDTVLGeggaRLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1163 GGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHL 1219
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1038-1243 |
1.74e-18 |
|
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: 86.39 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1038 GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSylt 1116
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFS--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 tkehlllyGSIKV---PHwtkkQLH--EEVKRTLKDTGLYSH----------RHKRVGT-LSGGMKRKLSISIALIGGSR 1180
Cdd:cd03244 92 --------GTIRSnldPF----GEYsdEELWQALERVGLKEFveslpggldtVVEEGGEnLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1181 VVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDeaEVL-SDRIAFLEQGGLRCCGSP 1243
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLD--TIIdSDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1954-2148 |
1.78e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDalDDLV---TV 2030
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDP--DDQVfssTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHL 2110
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881501 2111 WKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13647 178 MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1030-1235 |
1.89e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.09 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSK----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHTVRKN 1101
Cdd:PRK11153 4 LKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1102 MGVCMQHdvlFSYLTTKEhllLYGSIKVP----HWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIG 1177
Cdd:PRK11153 84 IGMIFQH---FNLLSSRT---VFDNVALPlelaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1178 GSRVVILDEPSTGVDPCSRRSIWDVISK-NKTAR-TIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDiNRELGlTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1027-1237 |
2.40e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1027 GVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGK--DIKTDLHT-----VR 1099
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairlLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 KNMGVCMQHDVLFSYLTTKEHLLlYGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGS 1179
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLI-EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1180 RVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRElSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1951-2148 |
3.05e-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: 85.72 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1951 KIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALddlvtv 2030
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTL------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 eehlyFYARVH-----GIPEKDIKE--------TVHKLLRRLHL---MPFKDRATSMcSYGTKRKLSTALALIGKPSILL 2094
Cdd:cd03245 90 -----FYGTLRdnitlGAPLADDERilraaelaGVTDFVNKHPNgldLQIGERGRGL-SGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2095 LDEPSSGMDPKSKRHLWKIISEEVQNKcSVILTSH--SMEEceaLCTRLAIMVNGK 2148
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHrpSLLD---LVDRIIVMDSGR 215
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1595-1856 |
3.23e-18 |
|
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: 88.60 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1595 FDITGVPANRTLAKVWYDPEGYHSLPAYLNSLNNFLLRVNMSKyDAARHGIIMYSHPYPGVQDQEQATISSLIDILVALS 1674
Cdd:pfam12698 89 FSKDLLKGESATVTVYINSSNLLVSKLILNALQSLLQQLNASA-LVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1675 ILMGYSVTTASFVTYVVREHQTKAKQLQHISGIGVTCYWVTNFIYDMVFYLVPVAFSIGIIAIFKLPAfyseNNLGAVSL 1754
Cdd:pfam12698 168 LMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPF----GNLGLLLL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1755 LLLLFGYATFSWMYLLAGLFHETGMAFITYVCVNLFFGINSIVSLsvvyflskekpndpTLELISETLKRIFLIFPQFCF 1834
Cdd:pfam12698 244 LFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLF--------------PLEDPPSFLQWIFSIIPFFSP 309
|
250 260
....*....|....*....|..
gi 27881501 1835 GYGLIELSQQQSVLDFLKAYGV 1856
Cdd:pfam12698 310 IDGLLRLIYGDSLWEIAPSLII 331
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1038-1238 |
3.43e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.84 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1038 GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT---DlhtvRknmGVCMQHDVLFSY 1114
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgaD----R---GVVFQKDALLPW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTTKEH----LLLYGsikVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTG 1190
Cdd:COG4525 91 LNVLDNvafgLRLRG---VP---KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1191 VDPCSRRS-------IWdviskNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:COG4525 165 LDALTREQmqellldVW-----QRTGKGVFLITHSVEEALFLATRLVVMSPGPGR 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1044-1243 |
4.54e-18 |
|
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: 85.74 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1044 DNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSylTTKEHLL 1122
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFN--DTIGYNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1123 LYGSIKVphwTKKQ---------LHEEVKRTLK--DT-----GLYshrhkrvgtLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:cd03253 96 RYGRPDA---TDEEvieaakaaqIHDKIMRFPDgyDTivgerGLK---------LSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1187 PSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAeVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTH 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1028-1236 |
4.74e-18 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 85.75 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKV--AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGV 1104
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHDVLFSylTTKEHLLLYGSIKVPhwtkkqlHEEVKRTLK-----------DTGLYSHRHKRVGTLSGGMKRKLSISI 1173
Cdd:cd03251 81 VSQDVFLFN--DTVAENIAYGRPGAT-------REEVEEAARaanahefimelPEGYDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1174 ALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVlSDRIAFLEQGG 1236
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1235 |
5.00e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.06 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1033 VTKIYGSKV-----AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTI-FVYgKDIKTDLHT--------- 1097
Cdd:PRK13651 8 IVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIF-KDEKNKKKTkekekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1098 ----------------VRKNMGVCMQHDVLFSYLTTKEHLLLYG--SIKVPhwtKKQLHEEVKRTLKDTGL-YSHRHKRV 1158
Cdd:PRK13651 87 lviqktrfkkikkikeIRRRVGVVFQFAEYQLFEQTIEKDIIFGpvSMGVS---KEEAKKRAAKYIELVGLdESYLQRSP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1159 GTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1012-1243 |
6.09e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1012 MFSSNIEPEPKDLTVGVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI 1091
Cdd:PRK10070 13 IFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1092 ----KTDLHTVR-KNMGVCMQHDVLFSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMK 1166
Cdd:PRK10070 93 akisDAELREVRrKKIAMVFQSFALMPHMTVLDNTAF--GMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMR 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1167 RKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK10070 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKlqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1045-1256 |
7.40e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.55 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1045 NLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKNMGVCMQHDVLFSylTTKEHLLL 1123
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvQYDHHYLHRQVALVGQEPVLFS--GSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1124 YGSIKVPhwtKKQLHEEVKRTLKD---TGLYSHRHKRVGT----LSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSR 1196
Cdd:TIGR00958 577 YGLTDTP---DEEIMAAAKAANAHdfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1197 RSIWDviSKNKTARTIILSTHHLDEAEVlSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHL 1256
Cdd:TIGR00958 654 QLLQE--SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1941-2148 |
9.36e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.06 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK-TGSLghvdSHSSL----- 2014
Cdd:COG1135 7 LSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdLTAL----SERELraarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 -VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLmpfKDRATsmcSY------GTKRKLSTALALI 2087
Cdd:COG1135 83 kIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGL---SDKAD---AYpsqlsgGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 2088 GKPSILLLDEPSSGMDPKSKR---HLWKIISEEVqnKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRsilDLLKDINREL--GLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1954-2148 |
1.03e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL------VGYCPQEDALDDL 2027
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIrelrrnVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 VTVEEHLyFYA--RVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPK 2105
Cdd:PRK11124 97 LTVQQNL-IEApcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881501 2106 SKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK11124 176 ITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1042-1243 |
1.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGT-----IFVYGKDIKTDLHTVRKNMGVCMQ--HDVLFSY 1114
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTTKEHLLLYGSIKVphwTKKQLHEEVKRTLKDTGLYSH-RHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDP 1193
Cdd:PRK13643 101 TVLKDVAFGPQNFGI---PKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1194 CSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK13643 178 KARIEMMQLFeSIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1040-1260 |
1.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.60 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1040 KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI--KTD---LHTVRKNMGVCMQHDVLFSY 1114
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKdkyIRPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTTKEHLLLYGsikvPHWTKKQLhEEVK----RTLKDTGLYSH-RHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:PRK13646 100 EDTVEREIIFG----PKNFKMNL-DEVKnyahRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1190 GVDPCSRRSIWDVISKNKTA--RTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEAFGDG-----YHLTLTK 1260
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP---KELFKDKkkladWHIGLPE 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1037-1238 |
1.60e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.83 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTI---SMLTGLF-GASA-GTIFVYGKDI---KTDLHTVRKNMGVCMQH 1108
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIpGFRVeGKVTFHGKNLyapDVDPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYlTTKEHlLLYGSiKVPHWtKKQLHEEVKRTLKDTGLYSH---RHKRVG-TLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:PRK14243 100 PNPFPK-SIYDN-IAYGA-RINGY-KGDMDELVERSLRQAALWDEvkdKLKQSGlSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1185 DEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAF----LEQGGLR 1238
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFfnveLTEGGGR 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1958-2129 |
1.99e-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: 82.93 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1958 ISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrNKTGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHLYFY 2037
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL-NGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2038 ARVHGipekdiKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEE 2117
Cdd:cd03231 98 HADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|..
gi 27881501 2118 VQNKCSVILTSH 2129
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1028-1229 |
2.11e-17 |
|
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: 88.11 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVC 1105
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 MQHDVLFsYLTTKEHLLLYgsikvphwTKKQLHEEVKRTLKDTGLYS-------HRHKRVGT----LSGGMKRKLSISIA 1174
Cdd:TIGR02857 402 PQHPFLF-AGTIAENIRLA--------RPDASDAEIREALERAGLDEfvaalpqGLDTPIGEggagLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1175 LIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEvLSDRI 1229
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA-LADRI 526
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1954-2149 |
2.45e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 82.09 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL-VGYCPqEDALDDLVtvee 2032
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP-EDRKREGL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 hlyfyarvhgIPEKDIKETVhkLLRRLhLmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:cd03215 90 ----------VLDLSVAENI--ALSSL-L-----------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 27881501 2113 IISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:cd03215 146 LIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1046-1243 |
2.74e-17 |
|
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: 85.93 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1046 LNLNF-YEGH-ITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-----KTDLHTVRKNMGVCMQHDVLFSYLTTK 1118
Cdd:TIGR02142 14 LDADFtLPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkGIFLPPEKRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1119 EHLLlYGSIKVPHWTKKQLHEEVKRTLkdtGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRS 1198
Cdd:TIGR02142 94 GNLR-YGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 1199 IWDVIsKNKTART---IILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:TIGR02142 170 ILPYL-ERLHAEFgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1037-1241 |
3.10e-17 |
|
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: 82.97 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKdIKTDLhtvrkNMGVCMQHDvlfsyLT 1116
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLL-----GLGGGFNPE-----LT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEHLLLYGSIKvpHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSR 1196
Cdd:cd03220 101 GRENIYLNGRLL--GLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 1197 RSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCG 1241
Cdd:cd03220 179 EKCQRRLrELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1891-2148 |
3.72e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1891 ESLIKKLRLFFRKFNSSHVRET-----IDEDEDVRAERLRVESGAAEF----------DLVQLYCLTKTYQliHKKIIav 1955
Cdd:COG0488 256 QKKIAKEEEFIRRFRAKARKAKqaqsrIKALEKLEREEPPRRDKTVEIrfppperlgkKVLELEGLSKSYG--DKTLL-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1956 NNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirnKTGSlgHVDshsslVGYCPQE-DALDDLVTVEEHL 2034
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGE--TVK-----IGYFDQHqEELDPDKTVLDEL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2035 YFYArvhgipEKDIKETVHKLLRRlhlMPFK-DRA---TSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHL 2110
Cdd:COG0488 401 RDGA------PGGTEQEVRGYLGR---FLFSgDDAfkpVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 27881501 2111 wkiisEEV-QN-KCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG0488 472 -----EEAlDDfPGTVLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1926-2158 |
3.76e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1926 VESGAAEFDLvqlYCLTKTYQLIHKKIIaVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSL 2005
Cdd:PRK14246 1 MEAGKSAEDV---FNISRLYLYINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2006 G----HVDSHS--SLVGYCPQEDALDDLVTVEEHLYFYARVHGIPEK-DIKETVHKLLRRLHLMP-FKDR---ATSMCSY 2074
Cdd:PRK14246 77 GkdifQIDAIKlrKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKeVYDRlnsPASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2075 GTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISeEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGS 2154
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT-ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
....
gi 27881501 2155 LQHI 2158
Cdd:PRK14246 236 SNEI 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1030-1235 |
4.04e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTI------FVYGKDIKT-DLHTVRKNM 1102
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhFDFSKTPSDkAIRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1103 GVCMQHDVLFSYLTTKEHlLLYGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVV 1182
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQN-LIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1183 ILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1955-2148 |
4.26e-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: 81.11 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALddlvtveehl 2034
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDEL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2035 yfyarvhgipekdiketvhkllrrlhlmpFKDR-ATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKI 2113
Cdd:cd03246 88 -----------------------------FSGSiAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*
gi 27881501 2114 ISEEVQNKCSVILTSHSMEECEAlCTRLAIMVNGK 2148
Cdd:cd03246 139 IAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1028-1242 |
5.70e-17 |
|
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: 82.53 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYG--SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGV 1104
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHDVLFS-------YLT----TKEHLLLYGSIKVPHWTKKQLHEEVKRTLKDTGlyshrhkrVGtLSGGMKRKLSISI 1173
Cdd:cd03252 81 VLQENVLFNrsirdniALAdpgmSMERVIEAAKLAGAHDFISELPEGYDTIVGEQG--------AG-LSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1174 ALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVlSDRIAFLEQGGLRCCGS 1242
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1037-1235 |
5.83e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.83 E-value: 5.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDlhtvRKNMGVCMQHDVLFSYLT 1116
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP----GAERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEH----LLLYGsikVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVD 1192
Cdd:PRK11248 87 VQDNvafgLQLAG---VE---KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881501 1193 PCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11248 161 AFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1021-1237 |
6.96e-17 |
|
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: 82.13 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1021 PKDLTVGVALHGVTKIYGSKVAV---DNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHT 1097
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTlvlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1098 -VRKNMGVCMQHDVLFSYLTTKEhlLLYGSIKVPHWTKKQL----HEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSIS 1172
Cdd:cd03248 85 yLHSKVSLVGQEPVLFARSLQDN--IAYGLQSCSFECVKEAaqkaHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1173 IALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEvLSDRIAFLEQGGL 1237
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1934-2162 |
7.34e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.77 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1934 DLVQLYCLTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRnktgslGHVDSHSS 2013
Cdd:PRK11432 5 NFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID------GEDVTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2014 LvgycPQED--------ALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALA 2085
Cdd:PRK11432 75 I----QQRDicmvfqsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2086 LIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQ--NKCSVILTsHSMEECEALCTRLAIMVNGKFQCIGSLQ----HIK 2159
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVT-HDQSEAFAVSDTVIVMNKGKIMQIGSPQelyrQPA 229
|
...
gi 27881501 2160 SRF 2162
Cdd:PRK11432 230 SRF 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1954-2160 |
8.32e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRN-KTGSLGHVDSHSSLVGYCPQEDALDDL-VTVE 2031
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVGIVFQNPETQFVgRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 EHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLW 2111
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2112 KIISEEVQNKCSVILTSHSMEECEAlCTRLAIMVNGKFQCIGSLQHIKS 2160
Cdd:PRK13644 177 ERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1264 |
1.38e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSK-----VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTI----FVYGKDIKTDLHT- 1097
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELIt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1098 ------------VRKNMGVCMQHDVLFSYLTTKEHLLLYGSI--KVPhwtKKQLHEEVKRTLKDTGL-YSHRHKRVGTLS 1162
Cdd:PRK13631 102 npyskkiknfkeLRRRVSMVFQFPEYQLFKDTIEKDIMFGPValGVK---KSEAKKLAKFYLNKMGLdDSYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1163 GGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNK-TARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCG 1241
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250 260
....*....|....*....|...
gi 27881501 1242 SPFylkEAFGDGYHLTLTKKKSP 1264
Cdd:PRK13631 259 TPY---EIFTDQHIINSTSIQVP 278
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1019-1235 |
1.41e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.78 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1019 PEPKDLTVGVALHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLH 1096
Cdd:PRK13657 326 IDLGRVKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1097 TVRKNMGVCMQHDVLFSYlTTKEHLllygSIKVPHWTKKQLHEEVKRT-------LKDTGLYSHRHKRVGTLSGGMKRKL 1169
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNR-SIEDNI----RVGRPDATDEEMRAAAERAqahdfieRKPDGYDTVVGERGRQLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1170 SISIALIGGSRVVILDEPSTGVDPCSRRSI---WDVISKNKTARTII--LSThhLDEAevlsDRIAFLEQG 1235
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVkaaLDELMKGRTTFIIAhrLST--VRNA----DRILVFDNG 545
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1035-1266 |
1.43e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1035 KIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI--------------KTDLHTVRK 1100
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1101 NMGVCMQHDVLFSYLTTKEHlLLYGSIKVPHWTKKQLHEEVKRTLKDTGL-YSHRHKRVGTLSGGMKRKLSISIALIGGS 1179
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLEN-VMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1180 RVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEAFGDgyhltl 1258
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP---EQLFGN------ 242
|
....*...
gi 27881501 1259 tkKKSPNL 1266
Cdd:PRK10619 243 --PQSPRL 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1029-1235 |
1.43e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.44 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1029 ALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI--KTDLHTVRKNMGVCM 1106
Cdd:PRK10762 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSSQEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSYLTTKEHLLL-------YGSIKvphWtkKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGS 1179
Cdd:PRK10762 86 QELNLIPQLTIAENIFLgrefvnrFGRID---W--KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1180 RVVILDEPSTGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1028-1241 |
1.51e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCM- 1106
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 -QHDVLFSYLTTKEHLLL-------YGSIKVPHWTKKQLHEEVkrTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGG 1178
Cdd:PRK09700 86 yQELSVIDELTVLENLYIgrhltkkVCGVNIIDWREMRVRAAM--MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1179 SRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCG 1241
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1954-2151 |
1.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGN-----ILIRNKTGS--LGHVDSHSSLVGYCPQEDALDD 2026
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTvtvddITITHKTKDkyIRPVRKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2027 lvTVEEHLYFYARVHGIPEKDIKETVHKLLRRL-------HLMPFKdratsmCSYGTKRKLSTALALIGKPSILLLDEPS 2099
Cdd:PRK13646 102 --TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLgfsrdvmSQSPFQ------MSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2100 SGMDPKSKRHLWKIISE--EVQNKcSVILTSHSMEECEALCTRLAIMVNGK--FQC 2151
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSlqTDENK-TIILVSHDMNEVARYADEVIVMKEGSivSQT 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1021-1243 |
1.79e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.73 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1021 PKDLTVGVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRK 1100
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1101 NMGVCMQHDVLFSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSR 1180
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAF--GLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1181 VVILDEPSTGVDPCSRR----SIWDVISknKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDrmqlEVVDILE--RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1037-1222 |
2.15e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.59 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI------KTDLH-----TVRK--NMG 1103
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqRSEVPdslplTVRDlvAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VcMQHDVLFSYLTTKEHLllygsikvphwtkkqlheEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:NF040873 82 R-WARRGLWRRLTRDDRA------------------AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEA 1222
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELV 182
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1940-2148 |
2.24e-16 |
|
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: 80.69 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1940 CLTKTYQLIHKkiiAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIR-NKTGSLGHVD--SHSSLVG 2016
Cdd:cd03256 5 NLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgTDINKLKGKAlrQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2017 YCPQEDALDDLVTVEE---------HLYFYARVHGIPEKDIKETVHkLLRRLHLmpfKDRATSMCSY---GTKRKLSTAL 2084
Cdd:cd03256 82 MIFQQFNLIERLSVLEnvlsgrlgrRSTWRSLFGLFPKEEKQRALA-ALERVGL---LDKAYQRADQlsgGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 2085 ALIGKPSILLLDEPSSGMDPKSKR---HLWKIISEEVQnkCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRqvmDLLKRINREEG--ITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1028-1226 |
2.25e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.74 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHTVRKNMG 1103
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VCMQHDVLFSYLTtkehllLYGSIKVPHWTKKQLHEEVKRT-----LKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGG 1178
Cdd:PRK11831 88 MLFQSGALFTDMN------VFDNVAYPLREHTQLPAPLLHStvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881501 1179 SRVVILDEPSTGVDPCSRRSIWDVISKNKTAR--TIILSTHhlDEAEVLS 1226
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSH--DVPEVLS 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1957-2130 |
2.48e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRnktGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHLYF 2036
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD---GGDIDDPDVAEACHYLGHRNAMKPALTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 YARVHGIPEKDIKETvhklLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISE 2116
Cdd:PRK13539 97 WAAFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
170
....*....|....
gi 27881501 2117 EVQNKCSVILTSHS 2130
Cdd:PRK13539 173 HLAQGGIVIAATHI 186
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1042-1230 |
3.80e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 82.02 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGL---FGASAGTIFVYGKDI----KTDLHTVR-KNMGVCMQhDVLFS 1113
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLlklsEKELRKIRgREIQMIFQ-DPMTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1114 ---YLTTKEH----LLLYGSIkvphwTKKQLHEEVKRTLKDTGL---------YSHRhkrvgtLSGGMKRKLSISIALIG 1177
Cdd:COG0444 99 lnpVMTVGDQiaepLRIHGGL-----SKAEARERAIELLERVGLpdperrldrYPHE------LSGGMRQRVMIARALAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1178 GSRVVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIA 1230
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQILNLLKdlQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1037-1243 |
4.00e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIK-TDLHTVRKNMGVCMQhDVLFSYL 1115
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQ-DTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1116 TTKEHLLLYGsiKVPHWTKKQLHEE-----VKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTG 1190
Cdd:PRK09536 92 FDVRQVVEMG--RTPHRSRFDTWTEtdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1191 VDPCSR-RSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK09536 170 LDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1042-1243 |
4.04e-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: 84.08 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHT--------VRKNMGVCMQHDVLFS 1113
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKpgpdgrgrAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1114 YLTTKEHLLLYGSIKVPhwtkkqlhEEVKR-----TLKDTGLYSHRHKRV-----GTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:TIGR03269 379 HRTVLDNLTEAIGLELP--------DELARmkaviTLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVI--SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1954-2132 |
4.23e-16 |
|
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: 84.04 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHS--SLVGYCPQEDAL-DDlvTV 2030
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV--DLSDLDPASwrRQIAWVPQNPYLfAG--TI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEHLYFYArvhgiPEKDiKETVHKLLRRLHLMPF------------KDRATSMcSYGTKRKLSTALALIGKPSILLLDEP 2098
Cdd:COG4988 428 RENLRLGR-----PDAS-DEELEAALEAAGLDEFvaalpdgldtplGEGGRGL-SGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190
....*....|....*....|....*....|....
gi 27881501 2099 SSGMDPKSKRHLWKIISEEVQNKCsVILTSHSME 2132
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAKGRT-VILITHRLA 533
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1954-2133 |
4.77e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.57 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK---TGSLGHVDSHSSLVGYCPQEDALDDlvTV 2030
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitDDNFEKLRKHIGIVFQNPDNQFVGS--IV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHL 2110
Cdd:PRK13648 102 KYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180
....*....|....*....|....
gi 27881501 2111 WKIISEEVQNK-CSVILTSHSMEE 2133
Cdd:PRK13648 182 LDLVRKVKSEHnITIISITHDLSE 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1027-1251 |
4.90e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.09 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1027 GVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTiSMLTGLFGASAGT----IFVYGKDIKTDLHTVRKNM 1102
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrF*TWCANRRALRRTIG*HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1103 GVCMQHDVLFSyltTKEHLLLYGsiKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVV 1182
Cdd:NF000106 92 PVR*GRRESFS---GRENLYMIG--R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1183 ILDEPSTGVDPCSRRSIWD-VISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFG 1251
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDeVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1944-2149 |
5.19e-16 |
|
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: 78.12 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1944 TYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRnktgslghvDSHSSLVgycpqEDA 2023
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD---------GVPVSDL-----EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2024 LDDLVTV---EEHLYfyarvhgipEKDIKETVHkllRRLhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:cd03247 73 LSSLISVlnqRPYLF---------DTTLRNNLG---RRF-------------SGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSH--SMEECEALCtrlaIMVNGKF 2149
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWITHHltGIEHMDKIL----FLENGKI 174
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1044-1236 |
5.35e-16 |
|
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: 79.51 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1044 DNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSyLTTKEHlL 1122
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFD-GTIAEN-I 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1123 LYGSIKVPhwtkkqlHEEVKRTLKDTGLYS------HR-HKRVG----TLSGGMKRKLSISIALIGGSRVVILDEPSTGV 1191
Cdd:cd03249 98 RYGKPDAT-------DEEVEEAAKKANIHDfimslpDGyDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881501 1192 DPCSRRSIWDVISKNKTARTIILSTHHLDEAEVlSDRIAFLEQGG 1236
Cdd:cd03249 171 DAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1027-1255 |
6.63e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1027 GVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCM 1106
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSYLTTKEH----LLLYGSIKVphwTKKQLHEEVKRTLKDTGLYSHRHKrvgTLSGGMKRKLSISIALIGGSRVV 1182
Cdd:PRK11000 82 QSYALYPHLSVAENmsfgLKLAGAKKE---EINQRVNQVAEVLQLAHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1183 ILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLkeafgdgYH 1255
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRlhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1959-2148 |
6.67e-16 |
|
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: 78.69 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1959 SIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHSSLVGYCPQEDALDDLVTVEEH--LYF 2036
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV--DVTAAPPADRPVSMLFQENNLFAHLTVEQNvgLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 YARVHGIPEKdiKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISE 2116
Cdd:cd03298 96 SPGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|...
gi 27881501 2117 -EVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03298 174 lHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1941-2148 |
6.72e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKT---GS--------LGHVD 2009
Cdd:COG3845 11 ITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvriRSprdaialgIGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2010 SHSSLVgycpqeDALddlvTVEEHLYFYA---RVHGIPEKDIKETVHKLLRRLHL-MPFKDRATSMcSYGTKRKLSTALA 2085
Cdd:COG3845 87 QHFMLV------PNL----TVAENIVLGLeptKGGRLDRKAARARIRELSERYGLdVDPDAKVEDL-SVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2086 LIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1941-2147 |
7.12e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 7.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKkiiAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrnktgsLGHVDSHS---SLVGY 2017
Cdd:PRK15056 12 VTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI------LGQPTRQAlqkNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2018 CPQEDALD--------DLVTVEE--HLYFYARvhgiPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALI 2087
Cdd:PRK15056 83 VPQSEEVDwsfpvlveDVVMMGRygHMGWLRR----AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2088 GKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTrLAIMVNG 2147
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1055-1243 |
7.18e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 81.69 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1055 ITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGK-----DIKTDLHTVRKNMGVCMQHDVLFSYLTTKEHLLlYGSIKV 1129
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPPHRRRIGYVFQEARLFPHLSVRGNLL-YGRKRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1130 PHWTKKQLHEEVKRTLkdtGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NK 1207
Cdd:COG4148 106 PRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERlrDE 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 27881501 1208 TARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG4148 183 LDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPL 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1027-1219 |
8.66e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.93 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1027 GVALHGVTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLhtvRKNM--G 1103
Cdd:PRK15056 6 GIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvaY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1104 VCMQHDVLFSYLTTKEHLLL---YGSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSR 1180
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDVVMmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27881501 1181 VVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHL 1219
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNL 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1040-1243 |
9.77e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1040 KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF---GASAGTIFVYGKDIKTD-LHTVRKNMGVCMQH-DVLFSY 1114
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKtVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTTKEHLLlYG--SIKVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVD 1192
Cdd:PRK13640 100 ATVGDDVA-FGleNRAVP---RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1193 PCSRRSIWDVISK--NKTARTIILSTHHLDEAEvLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK13640 176 PAGKEQILKLIRKlkKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1037-1243 |
1.12e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI---KTDLHTVRKNMGVCMQHDVLFS 1113
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1114 YLTTKEHLLLYgSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDP 1193
Cdd:PRK13638 91 FYTDIDSDIAF-SLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1194 CSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK13638 170 AGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1039-1256 |
1.14e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1039 SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGkdIKTDLHTV---RKNMGVCMQH-DVLFSY 1114
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG--MVLSEETVwdvRRQVGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 lTTKEHLLLYG--SIKVPHwtkKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVD 1192
Cdd:PRK13635 97 -ATVQDDVAFGleNIGVPR---EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 1193 PCSRRSIWDVIS--KNKTARTIILSTHHLDEAeVLSDRIAFLEQGGLRCCGSPfylKEAFGDGYHL 1256
Cdd:PRK13635 173 PRGRREVLETVRqlKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP---EEIFKSGHML 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1043-1256 |
1.24e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.78 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1043 VDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGK--------DIKTDLHTVRKN-----MGVCMQHD 1109
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRHKIGMVFQNpdnqfVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSyLTTKehlllygsiKVPHwtkKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:PRK13650 103 VAFG-LENK---------GIPH---EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1190 GVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAeVLSDRIAFLEQGGLRCCGSPfylKEAFGDGYHL 1256
Cdd:PRK13650 170 MLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTP---RELFSRGNDL 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1953-2158 |
1.35e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 81.62 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRN----KTGSLGHVDSHSSLVGYCPQEDALDDLV 2028
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKISDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2029 TVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKR 2108
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2109 HLW-KIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:PRK10070 202 EMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1037-1302 |
1.39e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.37 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLN---LNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTD-LHTVRKNMGVCMQH-DVL 1111
Cdd:PRK13642 14 YEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1112 FSYLTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGV 1191
Cdd:PRK13642 94 FVGATVEDDVAF--GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1192 DPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVlSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKKKSPNLNAN 1269
Cdd:PRK13642 172 DPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKD 250
|
250 260 270
....*....|....*....|....*....|...
gi 27881501 1270 AVCDTMavtamiqsHLPEAYLKEDiggELVYVL 1302
Cdd:PRK13642 251 LRKNGF--------DLPEKYLSED---ELVELL 272
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1969-2132 |
1.44e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.28 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1969 GLLGVNGAGKTTIFKMLTGDIIPSSGNILIR------NKTGSLGhVDSHSSLVGYCPQEDALddLVTVEEHLYFYARVHG 2042
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkpldySKRGLLA-LRQQVATVFQDPEQQIF--YTDIDSDIAFSLRNLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2043 IPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKC 2122
Cdd:PRK13638 108 VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN 187
|
170
....*....|
gi 27881501 2123 SVILTSHSME 2132
Cdd:PRK13638 188 HVIISSHDID 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1951-2163 |
1.47e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.25 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1951 KIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIL-----IRNKtgslGHVDSHSSLVGYCPQedALD 2025
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADA----RHRRAVCPRIAYMPQ--GLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 -----DLvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:NF033858 87 knlypTL-SVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2101 GMDPKSKRHLWKIISE--EVQNKCSVILTSHSMEECEAlCTRLAIMVNGKFQCIGSLQHIKSRFG 2163
Cdd:NF033858 166 GVDPLSRRQFWELIDRirAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1037-1237 |
1.66e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 82.87 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVaVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSYl 1115
Cdd:TIGR01193 485 YGSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1116 TTKEHLLLYGSIKVPHWTKKQLHE--EVKRTLKD--TGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGV 1191
Cdd:TIGR01193 563 SILENLLLGAKENVSQDEIWAACEiaEIKDDIENmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 1192 DPCSRRSIWDVISkNKTARTIILSTHHLDEAEvLSDRIAFLEQGGL 1237
Cdd:TIGR01193 643 DTITEKKIVNNLL-NLQDKTIIFVAHRLSVAK-QSDKIIVLDHGKI 686
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1007-1242 |
1.79e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.18 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1007 ASPEYMFSSNIEPEPKdlTVGVALHGVTKIY--GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTI 1084
Cdd:PRK11160 320 QKPEVTFPTTSTAAAD--QVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1085 FVYGKDIKT-DLHTVRKNMGVCMQHDVLFSYlTTKEHLLLygsiKVPHWTKKQLHEevkrTLKDTGLYSHRHKRVG---- 1159
Cdd:PRK11160 398 LLNGQPIADySEAALRQAISVVSQRVHLFSA-TLRDNLLL----AAPNASDEALIE----VLQQVGLEKLLEDDKGlnaw 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1160 ------TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLsDRIAFLE 1233
Cdd:PRK11160 469 lgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMD 547
|
....*....
gi 27881501 1234 QGGLRCCGS 1242
Cdd:PRK11160 548 NGQIIEQGT 556
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1040-1252 |
1.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.10 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1040 KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTD-----LHTVRKNMGVCMQ--HDVLF 1112
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1113 SYLTTKEhlLLYGSIKVpHWTKKQLHEEVKRTLKDTGLYSH-RHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGV 1191
Cdd:PRK13641 100 ENTVLKD--VEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1192 DPCSRRSIWDV-ISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEAFGD 1252
Cdd:PRK13641 177 DPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP---KEIFSD 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1957-2129 |
1.94e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVgYCPQEDALDDLVTVEEHLYF 2036
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL-YLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 YARVHGIPEKDikeTVHKLLRRLHLMPFKDRATSMCSYGTKRKlsTALA--LIGKPSILLLDEPSSGMDPKSKRHLWKII 2114
Cdd:PRK13538 98 YQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*
gi 27881501 2115 SEEVQNKCSVILTSH 2129
Cdd:PRK13538 173 AQHAEQGGMVILTTH 187
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1040-1257 |
2.24e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1040 KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTI------FVYGKDIKtDLHTVRKNMGVCMQ---HDv 1110
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKKNK-KLKPLRKKVGIVFQfpeHQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1111 LFSylTTKEHLLLYGSIK--VPhwtKKQLHEEVKRTLKDTGL-YSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:PRK13634 98 LFE--ETVEKDICFGPMNfgVS---EEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1188 STGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEAFGDGYHLT 1257
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP---REIFADPDELE 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1037-1233 |
2.33e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.54 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASA-----GTIFVYGKDI---KTDLHTVRKNMGVCMQH 1108
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLNRLRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYLTTKEhlLLYGsIKVPHWTKK-QLHEEVKRTLKDTGLY---SHR-HKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:PRK14258 97 PNLFPMSVYDN--VAYG-VKIVGWRPKlEIDDIVESALKDADLWdeiKHKiHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISKN--KTARTIILSTHHLDEAEVLSDRIAFLE 1233
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1019-1235 |
2.33e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.18 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1019 PEPKDLTVG--VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVyGKdikTDLH 1096
Cdd:PRK11247 2 MNTARLNQGtpLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GT---APLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1097 TVRKNMGVCMQHDVLFSYLTTKEH--LLLYGsikvpHWTKKQLheevkRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIA 1174
Cdd:PRK11247 78 EAREDTRLMFQDARLLPWKKVIDNvgLGLKG-----QWRDAAL-----QALAAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1175 LIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1954-2149 |
2.85e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHV-DSHSSLVGYCPQEDALDDLVTVEE 2032
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLY---FYARVHGIPEKDIKETVHKLLRRLHL-----MPFKDratsmCSYGTKRKLSTALALIGKPSILLLDEPSSGMDP 2104
Cdd:PRK11288 99 NLYlgqLPHKGGIVNRRLLNYEAREQLEHLGVdidpdTPLKY-----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27881501 2105 KSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:PRK11288 174 REIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1047-1225 |
3.87e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1047 NLNFY--EGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIktDLHTVRKNMGVCMQHDVLFSYLTTKEHLLLY 1124
Cdd:PRK13539 20 GLSFTlaAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1125 GSIKVPHWTkkqlheEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVIS 1204
Cdd:PRK13539 98 AAFLGGEEL------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
170 180
....*....|....*....|....*
gi 27881501 1205 KN-KTARTIILSTHH---LDEAEVL 1225
Cdd:PRK13539 172 AHlAQGGIVIAATHIplgLPGAREL 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1951-2148 |
4.46e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1951 KIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRN-----KTGSLGHVDSHS------------- 2012
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdKKNNHELITNPYskkiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2013 -SLVGYCPQEDALDDlvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHL-MPFKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:PRK13631 118 vSMVFQFPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1028-1243 |
5.13e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.97 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDLHTVRKNMGVCMQ 1107
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHlLLYGSIKVPHW---TKKQLHEEVKRTLKDTGLySHRHKRVGT-LSGGMKRKLSISIALIGGSRVVI 1183
Cdd:PRK10851 82 HYALFRHMTVFDN-IAFGLTVLPRRerpNAAAIKAKVTQLLEMVQL-AHLADRYPAqLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1184 LDEPSTGVDPCSRRSI--WDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK10851 160 LDEPFGALDAQVRKELrrWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1031-1243 |
5.98e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.08 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1031 HGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTVRknmGVCM 1106
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwELARRR---AVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVL-FSYlTTKEHLLLyGSIkvPH-WTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALI-------G 1177
Cdd:COG4559 82 QHSSLaFPF-TVEEVVAL-GRA--PHgSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1178 GSRVVILDEPSTGVDPCSRRSIWDvISKNKTARTI----ILstHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLR-LARQLARRGGgvvaVL--HDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1030-1187 |
6.82e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVyGKDIK----------TDLHTVR 1099
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLRigylpqepplDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 KNmgVCMQHDVLFSYLTTKEHLLLYGSIKVPHWTK-KQLHEE------------VKRTLKDTGLYSHRH-KRVGTLSGGM 1165
Cdd:COG0488 80 DT--VLDGDAELRALEAELEELEAKLAEPDEDLERlAELQEEfealggweaearAEEILSGLGFPEEDLdRPVSELSGGW 157
|
170 180
....*....|....*....|..
gi 27881501 1166 KRKLSISIALIGGSRVVILDEP 1187
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEP 179
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1029-1226 |
8.20e-15 |
|
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: 75.09 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1029 ALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQH 1108
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYLTTKEHLLLYGSIKVPHwtKKQLHEevkrTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:TIGR01189 82 PGLKPELSALENLHFWAAIHGGA--QRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881501 1189 TGVDPCSRRSIWDVISKNkTAR--TIILSTHH---LDEAEVLS 1226
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAH-LARggIVLLTTHQdlgLVEARELR 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1027-1252 |
9.48e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.09 E-value: 9.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1027 GVALHGVTKIYGSKV-----AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-----DLH 1096
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1097 TVRKNMGVCMQ--HDVLFSYLTTKEHLLLYGSIKVPHWTKKQLHEEvkrTLKDTGLY-SHRHKRVGTLSGGMKRKLSISI 1173
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALARE---KLALVGISeSLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1174 ALIGGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPfylKEAFGD 1252
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP---KDIFQD 235
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1954-2160 |
1.01e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.31 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslghvdshsSLVGYCPQEDA---------- 2023
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-----------DLTGLDEHEIArlgigrkfqk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2024 ---LDDLvTVEEHLYF-YARVHGI-------PEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSI 2092
Cdd:COG4674 94 ptvFEEL-TVFENLELaLKGDRGVfaslfarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2093 LLLDEPSSGMDPKSKRHLWKIIsEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKS 2160
Cdd:COG4674 173 LLLDEPVAGMTDAETERTAELL-KSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQA 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1956-2106 |
1.09e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 74.59 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1956 NNISIGIPAGECFGLLGVNGAGKTTIFKML----TGDIIpsSGNILIRNKTGslghVDSHSSLVGYCPQEDALDDLVTVE 2031
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLagrkTAGVI--TGEILINGRPL----DKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2032 EHLYFYArvhgipekdiketvhkLLRRLhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2106
Cdd:cd03232 98 EALRFSA----------------LLRGL-------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1953-2148 |
1.18e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.79 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK-----TGS--LGHVDSHSSLVGYCPQEDALD 2025
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpeTGNknLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 DlvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHL-------MPFKdratsmCSYGTKRKLSTALALIGKPSILLLDEP 2098
Cdd:PRK13641 101 N--TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsedliskSPFE------LSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881501 2099 SSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1028-1187 |
1.23e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIfVYGkdiktdlHTVRknMGVCMQ 1107
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLG-------ETVK--IGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 H-DVLFSYLTTKEHLLLYGsikvPHWTKKqlheEVKRTLKDTGLYSHR-HKRVGTLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:COG0488 386 HqEELDPDKTVLDELRDGA----PGGTEQ----EVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
..
gi 27881501 1186 EP 1187
Cdd:COG0488 458 EP 459
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1954-2135 |
1.29e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIP-----SSGNIL-----------IRNKTGSLGHvDSHSSLVGy 2017
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVDgitltaktvwdIREKVGIVFQ-NPDNQFVG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2018 cpqedalddlVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDE 2097
Cdd:PRK13640 100 ----------ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 27881501 2098 PSSGMDPKSKRHLWKIISE-EVQNKCSVILTSHSMEECE 2135
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEAN 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1944-2154 |
1.35e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.96 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1944 TYQLIHKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSH--SSLVGYCPQE 2021
Cdd:PRK13548 9 SVRLGGRTLL--DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR--PLADWSPAelARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2022 DALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRK--LSTALALI----GKPSILLL 2095
Cdd:PRK13548 85 SSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRvqLARVLAQLwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2096 DEPSSGMDPKSKRHLWKIISE-EVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGS 2154
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1031-1243 |
1.79e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1031 HGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIK----TDLHTVRknmGVCM 1106
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspAELARRR---AVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVL-FSYlTTKEHLLLYGSikvPH-WTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALI------GG 1178
Cdd:PRK13548 83 QHSSLsFPF-TVEEVVAMGRA---PHgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1179 SRVVILDEPSTGVDPCSRRSIWDvISKNKTART-----IILstHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLR-LARQLAHERglaviVVL--HDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1022-1254 |
1.82e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.10 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1022 KDLTVGValhgvtkiyGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFG--ASAGTIFVYGKDIkTDLHT-- 1097
Cdd:cd03217 4 KDLHVSV---------GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDI-TDLPPee 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1098 -VRKNMGVCMQHDVLFSYLTTKEHLllygsikvphwtkkqlheevkrtlkdtglyshRHKRVGtLSGGMKRKLSISIALI 1176
Cdd:cd03217 74 rARLGIFLAFQYPPEIPGVKNADFL--------------------------------RYVNEG-FSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1177 GGSRVVILDEPSTGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAE-VLSDRIAFLEQGGLRCCGSPFYLKEAFGDGY 1254
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEgKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1030-1237 |
2.50e-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: 73.02 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYG--SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCM 1106
Cdd:cd03246 3 VENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 QHDVLFSylttkehlllyGSIkvphwtkkqlheevkrtlkdtglyshrhkRVGTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:cd03246 83 QDDELFS-----------GSI-----------------------------AENILSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1187 PSTGVDPCSRRSIWDVISKNKTAR-TIILSTHHLdeaEVLS--DRIAFLEQGGL 1237
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGaTRIVIAHRP---ETLAsaDRILVLEDGRV 173
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
986-1235 |
4.32e-14 |
|
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: 77.83 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 986 KPEKSngLMFTNIMMQNTNPSAspEYMFSS-NIEPEPKDLTVG-------VALHGVTKIYG--SKVAVDNLNLNFYEGHI 1055
Cdd:TIGR02203 285 RPLKS--LTNVNAPMQRGLAAA--ESLFTLlDSPPEKDTGTRAierargdVEFRNVTFRYPgrDRPALDSISLVIEPGET 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1056 TSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSylTTKEHLLLYGSikvphwTK 1134
Cdd:TIGR02203 361 VALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDVVLFN--DTIANNIAYGR------TE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1135 KQLHEEVKRTLKDTGLYSH-------RHKRVGT----LSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVI 1203
Cdd:TIGR02203 433 QADRAEIERALAAAYAQDFvdklplgLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL 512
|
250 260 270
....*....|....*....|....*....|..
gi 27881501 1204 SKNKTARTIILSTHHLDEAEVlSDRIAFLEQG 1235
Cdd:TIGR02203 513 ERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDG 543
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1951-2148 |
4.34e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.15 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1951 KIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK------TGSLGHVDshsslVGYCPQEDAL 2024
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqTAKIMREA-----VAIVPEGRRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2025 DDLVTVEEHLY---FYARVHGIPEKdiKETVHKLLRRLHLMPFKdRATSMcSYGTKRKLSTALALIGKPSILLLDEPSSG 2101
Cdd:PRK11614 92 FSRMTVEENLAmggFFAERDQFQER--IKWVYELFPRLHERRIQ-RAGTM-SGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881501 2102 MDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1953-2148 |
4.48e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK----------TGSLGHV--DShssLVGYCPq 2020
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeykrAKYIGRVfqDP---MMGTAP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 edaldDLvTVEEHLYF-YARVH------GIPEKDIKEtVHKLLRRLHLmPFKDR---ATSMCSYGTKRKLSTALALIGKP 2090
Cdd:COG1101 96 -----SM-TIEENLALaYRRGKrrglrrGLTKKRREL-FRELLATLGL-GLENRldtKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLW----KIISEevqNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLelteKIVEE---NNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1954-2132 |
7.15e-14 |
|
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: 76.94 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDlVTVEEH 2033
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFA-GTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARvhGIPEKDIKETVHK---------LLRRLHLMpfKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDP 2104
Cdd:TIGR02857 416 IRLARP--DASDAEIREALERagldefvaaLPQGLDTP--IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180
....*....|....*....|....*...
gi 27881501 2105 KSKRHLWKIISEEVQNKcSVILTSHSME 2132
Cdd:TIGR02857 492 ETEAEVLEALRALAQGR-TVLLVTHRLA 518
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1935-2167 |
7.75e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.79 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1935 LVQLYCLTKTYqlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGdIIPS---SGNILIRNKTGSLGHV-DS 2010
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIrDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2011 HSSLVGYCPQEDALDDLVTVEEHLYFYARV-HGIPEKDIKETV---HKLLRRLHLMPFKD-RATSMCSYGTKRKLSTALA 2085
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELSVAENIFLGNEItLPGGRMAYNAMYlraKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2086 LIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGkfqcigslQHIKSRFGRG 2165
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--------QHVATKDMST 227
|
..
gi 27881501 2166 FT 2167
Cdd:TIGR02633 228 MS 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1941-2148 |
8.13e-14 |
|
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: 70.56 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYqliHKKIIaVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGnILIRNKTGSLGHVdshsslvgycpq 2020
Cdd:cd03221 6 LSKTY---GGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVKIGYF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 edalddlvtveEHLyfyarvhgipekdiketvhkllrrlhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:cd03221 69 -----------EQL--------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2101 GMDPKSKRHLwkiiSEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03221 100 HLDLESIEAL----EEALKEyPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1042-1235 |
9.22e-14 |
|
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: 71.69 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCM-----QHDVLFSYLT 1116
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEHLLLygsikvphwtkKQLheevkrtlkdtglyshrhkrvgtLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSR 1196
Cdd:cd03215 95 VAENIAL-----------SSL-----------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27881501 1197 RSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:cd03215 141 AEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1952-2167 |
9.63e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1952 IIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGdIIPS---SGNILIRNKTGSLGHV-DSHSSLVGYCPQEDALDDL 2027
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 VTVEEHLYFYARV--HGIPEKD-IKETVHKLLRRLHLmpFKDRATSMCSYGT-KRKL-STALALIGKPSILLLDEPSSGM 2102
Cdd:PRK13549 97 LSVLENIFLGNEItpGGIMDYDaMYLRAQKLLAQLKL--DINPATPVGNLGLgQQQLvEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2103 DPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKfqcigslqHIKSRFGRGFT 2167
Cdd:PRK13549 175 TESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--------HIGTRPAAGMT 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1030-1235 |
1.02e-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: 76.40 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF--GASAGTIFVYGKDIKTD--LHTVRKNMGVC 1105
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASniRDTERAGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 MQHDVLFSYLTTKEHLLLYGSIKVP----HWTKKQLH-EEVKRTLKDTGLYSHRhkRVGTLSGGMKRKLSISIALIGGSR 1180
Cdd:TIGR02633 84 HQELTLVPELSVAENIFLGNEITLPggrmAYNAMYLRaKNLLRELQLDADNVTR--PVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1181 VVILDEPSTGVDPCSRRSIWDVIsKNKTARTI--ILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDII-RDLKAHGVacVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1950-2158 |
1.19e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 73.31 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1950 KKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirNKTGSLGHVDSHSSLVGYcpqedalddlVT 2029
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAISAGLSGQ----------LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2030 VEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEP-SSGMDPKSKR 2108
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881501 2109 HLWKIISEEVQNKcSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:PRK13546 182 CLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1954-2148 |
1.33e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHV-DSHSSLVGYCPQEDALDDLV---T 2029
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPEDRKGEGLVldlS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2030 VEEHLYF-----YARVHGIPEKDIKETVHKLLRRLHLmpfkdRATSMcsyGTK-RKLS------TALA--LIGKPSILLL 2095
Cdd:COG1129 347 IRENITLasldrLSRGGLLDRRRERALAEEYIKRLRI-----KTPSP---EQPvGNLSggnqqkVVLAkwLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2096 DEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1955-2148 |
1.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQE-DALDDLVTVEEH 2033
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKI 2113
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 27881501 2114 IsEEVQNK--CSVILTSHSMEECeALCTRLAIMVNGK 2148
Cdd:PRK13642 183 I-HEIKEKyqLTVLSITHDLDEA-ASSDRILVMKAGE 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1957-2148 |
1.87e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.09 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSH----SSLVgycpQEDALDDLVTVEE 2032
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ--DLTALPPAerpvSMLF----QENNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFyarvhGI-----PEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSK 2107
Cdd:COG3840 91 NIGL-----GLrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881501 2108 R---HLWKIISEEVQNkcSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:COG3840 166 QemlDLVDELCRERGL--TVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1954-2167 |
2.00e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghVDSHSSLVGYCPQEDALDDLVTVEEH 2033
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRH---- 2109
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQmqtl 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2110 LWKIISEEVQnkcSVILTSHSMEECEALCTRLAIMVNGKFQCigsLQHIKSRFGRGFT 2167
Cdd:PRK11248 171 LLKLWQETGK---QVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRFV 222
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
1042-1246 |
2.56e-13 |
|
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: 71.63 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGA----SAGTIFVYGKDIkTDLHTVRKNMGVCMQH--DVLFSYL 1115
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL-LPLSIRGRHIATIMQNprTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1116 TTKEH----LLLYGSI-KVPhwTKKQLH-------EEVKRTLKdtgLYSHRhkrvgtLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:TIGR02770 80 TMGNHaietLRSLGKLsKQA--RALILEaleavglPDPEEVLK---KYPFQ------LSGGMLQRVMIALALLLEPPFLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYL 1246
Cdd:TIGR02770 149 ADEPTTDLDVVNQARVLKLLRElrQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1038-1218 |
3.10e-13 |
|
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: 70.60 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1038 GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHDVLFSYLTT 1117
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1118 KEHLLLYGSIkvpHWTkkqlhEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRR 1197
Cdd:cd03231 91 LENLRFWHAD---HSD-----EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|...
gi 27881501 1198 SIWDVISKNkTAR--TIILSTHH 1218
Cdd:cd03231 163 RFAEAMAGH-CARggMVVLTTHQ 184
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1941-2162 |
3.12e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQliHKKiiAVNNISIGIPAGECFGLLGVNGAGKTTIFK----MLTGDIIPSSGNILIRN---KTGSL-GHVDSHS 2012
Cdd:PRK09984 10 LAKTFN--QHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRtvqREGRLaRDIRKSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2013 SLVGYCPQEDALDDLVTVEEHLY--------FYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTAL 2084
Cdd:PRK09984 86 ANTGYIFQQFNLVNRLSVLENVLigalgstpFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2085 ALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNK-CSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKS-RF 2162
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNeRF 245
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1950-2125 |
3.79e-13 |
|
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: 71.10 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1950 KKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDAL--Ddl 2027
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLfsG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 vTVEEHLYFyarvhGIPEKDiKETVHKLLRRLHLMPF-----KDRATSM------CSYGTKRKLSTALALIGKPSILLLD 2096
Cdd:cd03254 92 -TIMENIRL-----GRPNAT-DEEVIEAAKEAGAHDFimklpNGYDTVLgenggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180
....*....|....*....|....*....
gi 27881501 2097 EPSSGMDPKSKRHLWKIISEEVQNKCSVI 2125
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMKGRTSII 193
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1949-2127 |
4.05e-13 |
|
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: 71.11 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1949 HKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDAL-DDl 2027
Cdd:cd03253 13 GRPVL--KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLfND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 vTVEEHLYfYARVHGIPEKDIKET----VHKLLRRlhlMPFK------DRATsMCSYGTKRKLSTALALIGKPSILLLDE 2097
Cdd:cd03253 90 -TIGYNIR-YGRPDATDEEVIEAAkaaqIHDKIMR---FPDGydtivgERGL-KLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190
....*....|....*....|....*....|
gi 27881501 2098 PSSGMDPKSKRHLWKIISEEVQNKCSVILT 2127
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSKGRTTIVIA 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1029-1235 |
4.16e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1029 ALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQH 1108
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVL--FSYLTTKEHLLL------YGSIKvphwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSR 1180
Cdd:PRK11288 86 QELhlVPEMTVAENLYLgqlphkGGIVN-----RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1181 VVILDEPSTGVdpcSRRSI---WDVISKNKT-ARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11288 161 VIAFDEPTSSL---SAREIeqlFRVIRELRAeGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1953-2195 |
4.36e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.36 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI---------RNKtgSLGHVDSHSSLVGYCPQEDA 2023
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkKNK--KLKPLRKKVGIVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2024 LDDlvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMP-FKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGM 2102
Cdd:PRK13634 99 FEE--TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2103 DPKSKRHLWKIISEEVQNK-CSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIksrfgrgFTVKVHLKNNKVTMET 2181
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKgLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI-------FADPDELEAIGLDLPE 249
|
250 260
....*....|....*....|.
gi 27881501 2182 LTKFMQ-------LHFPKTYL 2195
Cdd:PRK13634 250 TVKFKRaleekfgISFPKPCL 270
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1032-1235 |
4.44e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF--GASAGTIFVYGKDIK--TDLHTVRKNMGVCMQ 1107
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQasNIRDTERAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTTKEHLLLyGSIKVPH----WTKkqLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:PRK13549 90 ELALVKELSVLENIFL-GNEITPGgimdYDA--MYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVIS--KNKTARTIILStHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRdlKAHGIACIYIS-HKLNEVKAISDTICVIRDG 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1037-1237 |
4.81e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAG-----TIFVYGKDI--KTDLHTVRKNMGVCMQHD 1109
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSyLTTKEHLL--LYGSIKVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGT----LSGGMKRKLSISIALIGGSRVVI 1183
Cdd:PRK14271 111 NPFP-MSIMDNVLagVRAHKLVP---RKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1956-2129 |
7.70e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.93 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1956 NNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPS---SGNILIRnktgslGHV---DSHSSLVGYCPQEDALDDLVT 2029
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLN------GMPidaKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2030 VEEHLYFYARVH---GIPEKDIKETVHKLLRRLHLMPFKD-------RATSMcSYGTKRKLSTALALIGKPSILLLDEPS 2099
Cdd:TIGR00955 116 VREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtrigvpgRVKGL-SGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190
....*....|....*....|....*....|
gi 27881501 2100 SGMDPKSKRHLWKIISEEVQNKCSVILTSH 2129
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
708-952 |
8.18e-13 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 72.04 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 708 DSIERAIIELQTGrNSQEIAVQVQAIPYPCFMKDNFLTSVSYSL-PIVLMVAWVVFIAAFVKKLVYEKDLRLHEYMKMMG 786
Cdd:pfam12698 121 QSLLQQLNASALV-LLLEALSTSAPIPVESTPLFNPQSGYAYYLvGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 787 VNSCSHFFAWLIeSVGFLLVTIVILIIILKFGNILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYI 866
Cdd:pfam12698 200 VSPLQYWLGKIL-GDFLVGLLQLLIILLLLFGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVIL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 867 IAFFPFIVLVTVENeLSYVLKVFMSLLSPTAFsyasqyiaryeeqGIGLQWENMYTSPVQdDTTSFGWLCCLILadsfIY 946
Cdd:pfam12698 279 LLSGFFGGLFPLED-PPSFLQWIFSIIPFFSP-------------IDGLLRLIYGDSLWE-IAPSLIILLLFAV----VL 339
|
....*.
gi 27881501 947 FLIAWY 952
Cdd:pfam12698 340 LLLALL 345
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1045-1235 |
1.05e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1045 NLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCM-----QHDVLF--SYLTT 1117
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYlpedrQSSGLYldAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1118 KEHLLLYGsiKVPHWTK-KQLHEEVKRTLKDTGL-YSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCS 1195
Cdd:PRK15439 361 NVCALTHN--RRGFWIKpARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881501 1196 RRSIWDVI---SKNKTArtIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK15439 439 RNDIYQLIrsiAAQNVA--VLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1028-1235 |
1.21e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.16 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTD---------LHTV 1098
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1099 RKNMGVCMQHDVLFSYLTTKEHLllygsIKVPHWTKKQLHEEV----KRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIA 1174
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENI-----IEGPVIVKGEPKEEAtaraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1175 LIGGSRVVILDEPSTGVDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIrQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1955-2148 |
1.65e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghvdshssLVGYCPQeDAL---------- 2024
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE-----------VVTRSPQ-DGLangivyised 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2025 ---DDLV---TVEEHL------YFYARVHGIPEKDIKETVHKLLRRLHL-MPFKDRATSMCSYGTKRKLSTALALIGKPS 2091
Cdd:PRK10762 336 rkrDGLVlgmSVKENMsltalrYFSRAGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 2092 ILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1941-2148 |
1.70e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.66 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQlihKKIIaVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSH--SSLVGYC 2018
Cdd:PRK11231 8 LTVGYG---TKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK--PISMLSSRqlARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2019 PQEDALDDLVTVEE--------HLYFYARvhgIPEKDiKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:PRK11231 82 PQHHLTPEGITVRElvaygrspWLSLWGR---LSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1954-2149 |
2.07e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSL-GHVDSHSSLVGYCPQEDALDDLVTVEE 2032
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFnGPKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLY----FYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKR 2108
Cdd:PRK10762 99 NIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27881501 2109 HLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:PRK10762 179 SLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1030-1235 |
2.54e-12 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 69.09 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTV---------R 1099
Cdd:TIGR02323 6 VSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAElELYQLseaerrrlmR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 KNMGVCMQH--DVLFSYLTT----KEHLLL-----YGSIKVP--HWTKKQlheEVKRTLKDtglyshrhKRVGTLSGGMK 1166
Cdd:TIGR02323 86 TEWGFVHQNprDGLRMRVSAganiGERLMAigarhYGNIRATaqDWLEEV---EIDPTRID--------DLPRAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1167 RKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGlvRDLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1954-2148 |
2.93e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.39 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI-------RNKTGSLGHVDSHSSLVGYCPQEDALDD 2026
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitsTSKNKDIKQIRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2027 lvTVEEHLYFYARVHGIPekdiKETVHKLLR-RLHLM----PFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSG 2101
Cdd:PRK13649 102 --TVLKDVAFGPQNFGVS----QEEAEALAReKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881501 2102 MDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1953-2110 |
3.37e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 71.62 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDlVTVEE 2032
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFD-TTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFyarvhGIPEKDiKETVHKLLRRLHLMPFKDR-----ATSM------CSYGTKRKLSTALALIGKPSILLLDEPSSG 2101
Cdd:TIGR02868 428 NLRL-----ARPDAT-DEELWAALERVGLADWLRAlpdglDTVLgeggarLSGGERQRLALARALLADAPILLLDEPTEH 501
|
....*....
gi 27881501 2102 MDPKSKRHL 2110
Cdd:TIGR02868 502 LDAETADEL 510
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1037-1243 |
3.42e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.57 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKdIKTDLhtvrkNMGVCMQHDvlfsyLT 1116
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSALL-----ELGAGFHPE-----LT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEHLLLYGSIkvphwtkkqL---HEEVKRTLKD----TGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP-S 1188
Cdd:COG1134 105 GRENIYLNGRL---------LglsRKEIDEKFDEivefAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1189 TGvDP-----CSRRsIWDVISKnktARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:COG1134 176 VG-DAafqkkCLAR-IRELRES---GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1962-2141 |
4.35e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.57 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1962 IPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDAldDLVTVeEHLYFYARVH 2041
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKA--DLSTL-ENLHFLCGLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2042 GipeKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNK 2121
Cdd:PRK13543 111 G---RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
170 180
....*....|....*....|
gi 27881501 2122 CSVILTSHSMEECEALCTRL 2141
Cdd:PRK13543 188 GAALVTTHGAYAAPPVRTRM 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1956-2148 |
4.70e-12 |
|
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: 67.11 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1956 NNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirnktgslghvdSHSSLVGYCPQE----DAlddlvTVE 2031
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAYVSQEpwiqNG-----TIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 EHLYFyarvhGIP--EKDIKETVHK--LLRRLHLMPFKD------RATSMcSYGTKRKLSTALALIGKPSILLLDEPSSG 2101
Cdd:cd03250 84 ENILF-----GKPfdEERYEKVIKAcaLEPDLEILPDGDlteigeKGINL-SGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2102 MDPKSKRHLWK--IISEEVQNKCsVILTSHSMEECEAlCTRLAIMVNGK 2148
Cdd:cd03250 158 VDAHVGRHIFEncILGLLLNNKT-RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1042-1230 |
6.85e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKtdLHTV--------------RKNMGVCMQ 1107
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPrdairagiayvpedRKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLF-SYLTTKEHLLLYGSIKvphwtKKQLHEEVKRTLKDTGL-YSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:COG1129 345 LSIREnITLASLDRLSRGGLLD-----RRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 1186 EPSTGVDPCSRRSIWDVIskNKTAR---TIILSTHHLDEAEVLSDRIA 1230
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLI--RELAAegkAVIVISSELPELLGLSDRIL 465
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1058-1230 |
7.43e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 7.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1058 LLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDiktdlHT----VRKNMGVCMQHDVLFSYLTTKEH--LLLYGSIKVPH 1131
Cdd:PRK10771 30 ILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTttppSRRPVSMLFQENNLFSHLTVAQNigLGLNPGLKLNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1132 WTKKQLHEEVKRtlkdTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTAR- 1210
Cdd:PRK10771 105 AQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERq 180
|
170 180
....*....|....*....|.
gi 27881501 1211 -TIILSTHHLDEAEvlsdRIA 1230
Cdd:PRK10771 181 lTLLMVSHSLEDAA----RIA 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1955-2131 |
8.24e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirnktgslghVDSHSSLVGYCPQEDALDDL--VTVEE 2032
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLDTTlpLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLyfyaRVH-GIPEKDIKETvhklLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLW 2111
Cdd:PRK09544 89 FL----RLRpGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180
....*....|....*....|..
gi 27881501 2112 KIIsEEVQNK--CSVILTSHSM 2131
Cdd:PRK09544 161 DLI-DQLRREldCAVLMVSHDL 181
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1954-2133 |
1.06e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI-------RNKTGSLGHVDSHSSLVGYCPQEDALDD 2026
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2027 lvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHL-MPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPK 2105
Cdd:PRK13643 101 --TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180
....*....|....*....|....*...
gi 27881501 2106 SKRHLWKIISEEVQNKCSVILTSHSMEE 2133
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDD 206
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1954-2185 |
1.50e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.53 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRnktGSlghvdshSSLVGYcpqEDALDDLVTVEEH 2033
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK---GS-------AALIAI---SSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKI 2113
Cdd:PRK13545 106 IELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2114 ISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKSRFGRgftvkvHLKN-NKVTMETLTKF 2185
Cdd:PRK13545 186 MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE------FLKKyNQMSVEERKDF 252
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1058-1243 |
1.74e-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: 65.90 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1058 LLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSYlTTKEHLLLYGsikvpHWTKKQ 1136
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQDPTLFSG-TIRSNLDPFD-----EYSDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1137 LHEEVKrtLKDTGLyshrhkrvgTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILST 1216
Cdd:cd03369 113 IYGALR--VSEGGL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIA 181
|
170 180
....*....|....*....|....*..
gi 27881501 1217 HHLdEAEVLSDRIAFLEQGGLRCCGSP 1243
Cdd:cd03369 182 HRL-RTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1037-1218 |
1.81e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1037 YGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHDVLFSYLT 1116
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEHLLLYgsikvPHWTKKQLH-EEVKRTLKdtgLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDpcs 1195
Cdd:PRK13540 91 LRENCLYD-----IHFSPGAVGiTELCRLFS---LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD--- 159
|
170 180
....*....|....*....|....*..
gi 27881501 1196 RRSIWDVISKNKTAR----TIILSTHH 1218
Cdd:PRK13540 160 ELSLLTIITKIQEHRakggAVLLTSHQ 186
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1965-2114 |
1.87e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.66 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1965 GECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghvdshsslVGYCPQEDALDDLVTVEEHLYFYARVHGIP 2044
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKPQYIKADYEGTVRDLLSSITKDFYTH 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2045 EKDIKEtvhkLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKII 2114
Cdd:cd03237 93 PYFKTE----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1955-2153 |
2.26e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.33 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDLVTVEE-- 2032
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 ------HLyfyARVHGIPEKDiKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2106
Cdd:PRK09536 99 emgrtpHR---SRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881501 2107 KRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIG 2153
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1043-1249 |
2.36e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1043 VDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDL------------------------HTV 1098
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglangivyisedrkrdglvlgMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1099 RKNMGVC-MQHdvlFSYLttkehlllYGSIKvphwtkkqlHEEVKRTLKD-TGLYS----HRHKRVGTLSGGMKRKLSIS 1172
Cdd:PRK10762 348 KENMSLTaLRY---FSRA--------GGSLK---------HADEQQAVSDfIRLFNiktpSMEQAIGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1173 IALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKT-ARTIILSTHHLDEAEVLSDRIAFLEQGglRCCGSpFYLKEA 1249
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGMSDRILVMHEG--RISGE-FTREQA 482
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1030-1236 |
2.43e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 63.62 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVyGKDIKtdlhtvrknmgvcmqhd 1109
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 vlFSYLTtkehlllygsikvphwtkkQlheevkrtlkdtglyshrhkrvgtLSGGMKRKLSISIALIGGSRVVILDEPST 1189
Cdd:cd03221 65 --IGYFE-------------------Q------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881501 1190 GVDPCSRRSIWDVIskNKTARTIILSTH---HLDEaevLSDRIAFLEQGG 1236
Cdd:cd03221 100 HLDLESIEALEEAL--KEYPGTVILVSHdryFLDQ---VATKIIELEDGK 144
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1870-2129 |
2.68e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.65 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1870 AMFVALVSQgtMFFSLRLLINE-SLIKKLRLFFRKfnsshVRETIDEDEDVR----AERLRVESGAAEFDLVqlyclTKT 1944
Cdd:COG1132 281 VAFILYLLR--LFGPLRQLANVlNQLQRALASAER-----IFELLDEPPEIPdppgAVPLPPVRGEIEFENV-----SFS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1945 YQlihKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrnktgslGHVD----SHSSL---VGY 2017
Cdd:COG1132 349 YP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-------DGVDirdlTLESLrrqIGV 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2018 CPQEDAL-DDlvTVEEHLyFYARvHGIPEKDIKETvhklLRRLHLMPF------------KDRATSMcSYGTKRKLSTAL 2084
Cdd:COG1132 419 VPQDTFLfSG--TIRENI-RYGR-PDATDEEVEEA----AKAAQAHEFiealpdgydtvvGERGVNL-SGGQRQRIAIAR 489
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27881501 2085 ALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKcSVILTSH 2129
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGR-TTIVIAH 533
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1033-1237 |
2.72e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.67 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1033 VTKIY-GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHTVRKNMGVCMQ 1107
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 hdvlfsylttKEHLLL----YGSIKVPHWTKKQLHEEVKR----TLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGS 1179
Cdd:PRK10908 87 ----------DHHLLMdrtvYDNVAIPLIIAGASGDDIRRrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1180 RVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1942-2147 |
2.90e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1942 TKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLT--GDIIPssgNILIrnkTGSLGHvDSHSSlvgYCP 2019
Cdd:PRK14239 8 VSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNP---EVTI---TGSIVY-NGHNI---YSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2020 QEDALD-----DLV---------TVEEHLYFYARVHGIPEKDI-KETVHKLLR----------RLHlmpfkDRATSMcSY 2074
Cdd:PRK14239 78 RTDTVDlrkeiGMVfqqpnpfpmSIYENVVYGLRLKGIKDKQVlDEAVEKSLKgasiwdevkdRLH-----DSALGL-SG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2075 GTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISeEVQNKCSVILTSHSMEECEALCTRLAIMVNG 2147
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLL-GLKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1954-2125 |
3.49e-11 |
|
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: 65.33 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRnktgslGH------VDSHSSLVGYCPQEDAL-DD 2026
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID------GHdvrdytLASLRRQIGLVSQDVFLfND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2027 lvTVEEHLYfYARvHGIPEKDIKETvhklLRRLHLMPF------------KDRATSMcSYGTKRKLSTALALIGKPSILL 2094
Cdd:cd03251 91 --TVAENIA-YGR-PGATREEVEEA----ARAANAHEFimelpegydtviGERGVKL-SGGQRQRIAIARALLKDPPILI 161
|
170 180 190
....*....|....*....|....*....|.
gi 27881501 2095 LDEPSSGMDPKSKRHLWKIISEEVQNKCSVI 2125
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFV 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1038-1236 |
3.76e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1038 GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSYlt 1116
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 tkehlLLYGSIKVPhWTKKQLHEEVKRTLKDT---GLYSHR-HKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVD 1192
Cdd:PRK10247 96 -----TVYDNLIFP-WQIRNQQPDPAIFLDDLerfALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 1193 PCSRRSIWDVISKNKTARTI--ILSTHHLDEAEVLSDRIAFLEQGG 1236
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIavLWVTHDKDEINHADKVITLQPHAG 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1954-2148 |
4.21e-11 |
|
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: 64.86 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK--TGSLGHVDSHSSLVGYCPQEDALDDLVTVE 2031
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLklTDDKKNINELRQKVGMVFQQFNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 EHLYFYAR-VHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHL 2110
Cdd:cd03262 95 ENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEV 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881501 2111 WKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:cd03262 175 LDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1030-1217 |
4.37e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.21 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYGS---KVAV-DNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTVRK- 1100
Cdd:PRK10535 7 LKDIRRSYPSgeeQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLRRe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1101 NMGVCMQHDVLFSYLTTKEhlllygSIKVPH----WTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALI 1176
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQ------NVEVPAvyagLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27881501 1177 GGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTH 1217
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTH 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1043-1238 |
5.47e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1043 VDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF-GASAGTIFVYGK--DIKTDLHTVRKnmGVCM-----QHDVLFSY 1114
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKpvKIRNPQQAIAQ--GIAMvpedrKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTTKEHLLLYGSIKVPHWTK-------KQLHEEVKRTLKDTglySHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1187
Cdd:PRK13549 356 MGVGKNITLAALDRFTGGSRiddaaelKTILESIQRLKVKT---ASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1188 STGVDPCSRRSIWDVIskNKTAR---TIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:PRK13549 433 TRGIDVGAKYEIYKLI--NQLVQqgvAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1043-1238 |
5.60e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.54 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1043 VDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF-GASAGTIFVYGK--DIKTDLHTVRKnmGVCM-----QHDVLFSY 1114
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKpvDIRNPAQAIRA--GIAMvpedrKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTTKEHLLLygSIKVPHWTKKQLHEEVKRTLKDTGLY------SHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:TIGR02633 354 LGVGKNITL--SVLKSFCFKMRIDAAAELQIIGSAIQrlkvktASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1189 TGVDPCSRRSIWDVIskNKTAR---TIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:TIGR02633 432 RGVDVGAKYEIYKLI--NQLAQegvAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1954-2164 |
6.67e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 64.81 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgSLGHVDSHS--SLVGYCPQEDAL------D 2025
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGH--DLALADPAWlrRQVGVVLQENVLfnrsirD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 DLVTVEEhlyfyarvhGIPEKDIKET-----VHKLLRRLHL---MPFKDRATSMcSYGTKRKLSTALALIGKPSILLLDE 2097
Cdd:cd03252 95 NIALADP---------GMSMERVIEAaklagAHDFISELPEgydTIVGEQGAGL-SGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2098 PSSGMDPKSKRhlwkIISEEVQNKC---SVILTSHSMEECEAlCTRLAIMVNGKFQCIGSLQHIKSRFGR 2164
Cdd:cd03252 165 ATSALDYESEH----AIMRNMHDICagrTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1948-2147 |
7.49e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1948 IHKKIIAVN---NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRnktgslGHVDSHSS----------L 2014
Cdd:PRK15439 17 ISKQYSGVEvlkGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG------GNPCARLTpakahqlgiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 VgycPQEDALDDLVTVEEHLYFyarvhGIPEK-DIKETVHKLLRRL--HLMPfkDRATSMCSYGTKRKLSTALALIGKPS 2091
Cdd:PRK15439 91 V---PQEPLLFPNLSVKENILF-----GLPKRqASMQKMKQLLAALgcQLDL--DSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2092 ILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNG 2147
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1955-2129 |
7.80e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI--RNKTGSLGHVDSHSSLVGYcpqEDALDDLVTVEE 2032
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerQSIKKDLCTYQKQLCFVGH---RSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFyarvhGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:PRK13540 94 NCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170
....*....|....*..
gi 27881501 2113 IISEEVQNKCSVILTSH 2129
Cdd:PRK13540 169 KIQEHRAKGGAVLLTSH 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1958-2103 |
7.88e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1958 ISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDLVTVEEhLYFY 2037
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE-LVAI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2038 ARV--HG----IPEKDiKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:PRK10575 109 GRYpwHGalgrFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1053-1218 |
1.08e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1053 GHITSLLGPNGAGKTTTISMLTGLFGAS--AGTIFVYGKDIKTDlhtVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVP 1130
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ---ILKRTGFVTQDDILYPHLTVRETLVFCSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1131 HWTKKQLHEEVKRT-LKDTGLYSHRHKRVGT-----LSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSR-RSIWDVI 1203
Cdd:PLN03211 171 KSLTKQEKILVAESvISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLG 250
|
170
....*....|....*
gi 27881501 1204 SKNKTARTIILSTHH 1218
Cdd:PLN03211 251 SLAQKGKTIVTSMHQ 265
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1032-1235 |
1.24e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIktDLHTVRKNM--GVCMQHD 1109
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFKSSKEALenGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYL--TTKEHLLL--YgSIKVPHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:PRK10982 81 ELNLVLqrSVMDNMWLgrY-PTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1186 EPSTGVDPCSRRSIWDVISKNKTART-IILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1954-2148 |
1.27e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.11 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNI--LIRNKtgslgHVDSHSSLVgycpqEDALDDLV--- 2028
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDE-----KNKKKTKEK-----EKVLEKLViqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2029 ------------------------------TVEEHLYFYARVHGIPEKDIKETVHKLLRRLHL-MPFKDRATSMCSYGTK 2077
Cdd:PRK13651 92 trfkkikkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2078 RKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1028-1243 |
1.41e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIfvygkdiktdLHTVRKNMGVCMQ 1107
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSY--LTTKEHLLLYGSIKvphwtKKQLHEEVKRTLKDTGLYSHRHKrvgtLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:PRK09544 75 KLYLDTTlpLTVNRFLRLRPGTK-----KEDILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1186 EPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIAFLEQgGLRCCGSP 1243
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTP 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1049-1243 |
1.43e-10 |
|
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: 63.97 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1049 NFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGtifvygkDIKTDLHTVRKNmgvcmQHDVLFSYLTTKEHLLLygSIK 1128
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELDTVSYK-----PQYIKADYEGTVRDLLS--SIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1129 VPHWTKKQLHEEVKRTLKDTGLYShrhKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVI----- 1203
Cdd:cd03237 87 KDFYTHPYFKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIrrfae 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27881501 1204 SKNKTARTIilsTHHLDEAEVLSDR-IAFLEQGGLRCCGSP 1243
Cdd:cd03237 164 NNEKTAFVV---EHDIIMIDYLADRlIVFEGEPSVNGVANP 201
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1954-2207 |
1.48e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.64 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRN--------KTGSLGHVDSHSSLVGYCPQEDALD 2025
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkKIKEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 DlvTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHL-MPFKDRATSMCSYGTKRKLSTA--LALIGKpsILLLDEPSSGM 2102
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAgiIAMDGN--TLVLDEPTGGL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2103 DPKSKRHLWKIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHIKSrfgrgftvkvhlknnkvTMET 2181
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS-----------------NQEL 244
|
250 260 270
....*....|....*....|....*....|.
gi 27881501 2182 LTKfMQLHFPKTY-----LKDQHLSMLEYHV 2207
Cdd:PRK13645 245 LTK-IEIDPPKLYqlmykLKNKGIDLLNKNI 274
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1951-2133 |
1.75e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.03 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1951 KIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKML--TGDIIPS---SGNILIRNKTGSLGHVD-----SHSSLVGYCPQ 2020
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPDVDpvevrRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDAlddlVTVEEHLYFYARVHGIpEKDIKETVHKLLRRLHLM-----PFKDRATSMcSYGTKRKLSTALALIGKPSILLL 2095
Cdd:PRK14243 102 PFP----KSIYDNIAYGARINGY-KGDMDELVERSLRQAALWdevkdKLKQSGLSL-SGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881501 2096 DEPSSGMDPKSKRHLWKIISEEVQNKCSVILTsHSMEE 2133
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVT-HNMQQ 212
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1031-1235 |
2.21e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 63.67 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1031 HGVTKIY---------GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHT 1097
Cdd:TIGR02769 6 RDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQRRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1098 VRKNMGVCMQHdvlfSYLTTKEHLLLYGSIKVP--HWTKKQLHEEVKRT---LKDTGLYS-HRHKRVGTLSGGMKRKLSI 1171
Cdd:TIGR02769 86 FRRDVQLVFQD----SPSAVNPRMTVRQIIGEPlrHLTSLDESEQKARIaelLDMVGLRSeDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 1172 SIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTI--ILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
998-1237 |
2.52e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 998 IMMQNTNPSASPEYMFSSN--IEPEPKDLTVgVALHGvtkiygsKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTG 1075
Cdd:PRK11174 327 FLETPLAHPQQGEKELASNdpVTIEAEDLEI-LSPDG-------KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1076 lFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFsYLTTKEHLLLyGSikvPHWTKKQLHEEVKRT-------LKD 1147
Cdd:PRK11174 399 -FLPYQGSLKINGIELRElDPESWRKHLSWVGQNPQLP-HGTLRDNVLL-GN---PDASDEQLQQALENAwvseflpLLP 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1148 TGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLsD 1227
Cdd:PRK11174 473 QGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-D 551
|
250
....*....|
gi 27881501 1228 RIAFLEQGGL 1237
Cdd:PRK11174 552 QIWVMQDGQI 561
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1039-1235 |
2.84e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 62.10 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1039 SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKdiktdlhtvrknMGVCMQHDVLFSyLTTK 1118
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWIQN-GTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1119 EHLLlygsikvphWTKKQLHEEVKRTLKDTGLyshrhKR------------VG----TLSGGMKRKLSISIALIGGSRVV 1182
Cdd:cd03250 84 ENIL---------FGKPFDEERYEKVIKACAL-----EPdleilpdgdlteIGekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1183 ILDEPSTGVDPCSRRSIWD-VISKN-KTARTIILSTHHLdeaEVLS--DRIAFLEQG 1235
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFEnCILGLlLNNKTRILVTHQL---QLLPhaDQIVVLDNG 203
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1038-1236 |
2.89e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.88 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1038 GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTG--LFGASAGTIFVYGKDIKTDLhtvRKNMGVCMQHDVLFSYL 1115
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1116 TTKEHLLLYGSIKvphwtkkqlheevkrtlkdtglyshrhkrvgTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPcs 1195
Cdd:cd03232 95 TVREALRFSALLR-------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS-- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 1196 rRSIWDVISK-NKTART--IILSTHHLDEAEVLS--DRIAFLEQGG 1236
Cdd:cd03232 142 -QAAYNIVRFlKKLADSgqAILCTIHQPSASIFEkfDRLLLLKRGG 186
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1970-2129 |
4.89e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 65.25 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1970 LLGVNGAGKTTIFKML----TGDIIpsSGNILIrnkTGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHLYFYARVHgIPE 2045
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLagrkTGGYI--EGDIRI---SGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLR-LPK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2046 KDIKET----VHKLLRRLHLMPFKDRATSM-----CSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISE 2116
Cdd:PLN03140 985 EVSKEEkmmfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
170
....*....|...
gi 27881501 2117 EVQNKCSVILTSH 2129
Cdd:PLN03140 1065 TVDTGRTVVCTIH 1077
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1954-2184 |
5.28e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTG--DIIPSSGNILIR-NKTGSLGHVDSHSSLVGYCP-------QEDA 2023
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvALCEKCGYVERPSKVGEPCPvcggtlePEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2024 ----LDDLVTVEEH------------LYFYARV-----HGIPEKDI--KETVHKLLRRLHLMPFKDRATSMC---SYGTK 2077
Cdd:TIGR03269 95 dfwnLSDKLRRRIRkriaimlqrtfaLYGDDTVldnvlEALEEIGYegKEAVGRAVDLIEMVQLSHRITHIArdlSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2078 RKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNK-CSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQ 2156
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPD 254
|
250 260 270
....*....|....*....|....*....|...
gi 27881501 2157 HIKSRFGRGFTV-----KVHLKNNKVTMETLTK 2184
Cdd:TIGR03269 255 EVVAVFMEGVSEvekecEVEVGEPIIKVRNVSK 287
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1031-1192 |
5.87e-10 |
|
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: 64.57 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1031 HGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIfVYGKdiktdlhTVRknMG-VCMQHD 1109
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-EIGE-------TVK--LAyVDQSRD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSYLTTKEH------LLLYGSIKVPhwtkkqlheevkrtlkdTGLYSHR--------HKRVGTLSGGMKRKLSISIAL 1175
Cdd:TIGR03719 396 ALDPNKTVWEEisggldIIKLGKREIP-----------------SRAYVGRfnfkgsdqQKKVGQLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 27881501 1176 IGGSRVVILDEPSTGVD 1192
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1922-2149 |
6.46e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.42 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1922 ERLRVESGAAEFDLVQLYCLTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLT--GDIIPS---SGNI 1996
Cdd:PRK14271 4 ERLGGQSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmNDKVSGyrySGDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1997 LIRNKT-GSLGHVDSHSSLVGYCPQEDALDDLvTVEEHLYFYARVHG-IPEKDIKETVHKLLRRLHLM-PFKDRATS--- 2070
Cdd:PRK14271 84 LLGGRSiFNYRDVLEFRRRVGMLFQRPNPFPM-SIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWdAVKDRLSDspf 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2071 MCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIIsEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI-RSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1941-2148 |
6.98e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.00 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQliHKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILirnktgslghvdshsslVGYCPQ 2020
Cdd:PRK11247 18 VSKRYG--ERTVL--NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----------------AGTAPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLvtveeHLYFY-ARVhgIPEKDIKETV---------HKLLRRLHLMPFKDRAT---SMCSYGTKRKLSTALALI 2087
Cdd:PRK11247 77 AEAREDT-----RLMFQdARL--LPWKKVIDNVglglkgqwrDAALQALAAVGLADRANewpAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2088 GKPSILLLDEPSSGMDPKSK-------RHLWKiiseevQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRiemqdliESLWQ------QHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1042-1192 |
7.04e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.19 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHTVRKNMGVCMQhDVLFSY--- 1114
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQ-DPLASLnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTT----KEHLLLYgsikVPHWTKKQLHEEVKRTLKDTGL-------YSHRhkrvgtLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:PRK15079 115 MTIgeiiAEPLRTY----HPKLSRQEVKDRVKAMMLKVGLlpnlinrYPHE------FSGGQCQRIGIARALILEPKLII 184
|
....*....
gi 27881501 1184 LDEPSTGVD 1192
Cdd:PRK15079 185 CDEPVSALD 193
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1952-2106 |
7.93e-10 |
|
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: 61.40 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1952 IIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDlVTVE 2031
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 EHLYFyarvhGIPEKDIKETV--------HKLLRRLhlmPFK------DRATSMcSYGTKRKLSTALALIGKPSILLLDE 2097
Cdd:cd03249 95 ENIRY-----GKPDATDEEVEeaakkaniHDFIMSL---PDGydtlvgERGSQL-SGGQKQRIAIARALLRNPKILLLDE 165
|
....*....
gi 27881501 2098 PSSGMDPKS 2106
Cdd:cd03249 166 ATSALDAES 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1935-2103 |
9.05e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.73 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1935 LVQLYCLTKTYQ----LIHKKII-AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVD 2009
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgWFRRQTVeAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2010 SHSSLVGYCPQEDA------------LDDLVTVEEHLYFYARvhgipEKDIKETvhklLRRLHLMPfkDRAT---SMCSY 2074
Cdd:PRK15112 84 YRSQRIRMIFQDPStslnprqrisqiLDFPLRLNTDLEPEQR-----EKQIIET----LRQVGLLP--DHASyypHMLAP 152
|
170 180
....*....|....*....|....*....
gi 27881501 2075 GTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1039-1237 |
1.26e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1039 SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSYlTT 1117
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1118 KEHLLLyGSikvPHWTKKQL---------HEEVKRTLKdtGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1188
Cdd:PRK10789 406 ANNIAL-GR---PDATQQEIehvarlasvHDDILRLPQ--GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 1189 TGVDPCSRRSIWDVISKNKTARTIILSTHHLdEAEVLSDRIAFLEQGGL 1237
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHI 527
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1941-2148 |
1.27e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.75 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKKIiavnniSIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslgHVDSHSSL--VGYC 2018
Cdd:PRK10771 7 ITWLYHHLPMRF------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPSRrpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2019 PQEDALDDLVTVEEHLYFyarvhGI-P----EKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSIL 2093
Cdd:PRK10771 77 FQENNLFSHLTVAQNIGL-----GLnPglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2094 LLDEPSSGMDPKSKRHLWKIISEEVQNK-CSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERqLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1941-2114 |
1.35e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKML----TGDIIpSSGNILIrnktGSLGHVDSHSSLVG 2016
Cdd:TIGR00956 765 LTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervTTGVI-TGGDRLV----NGRPLDSSFQRSIG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2017 YCPQEDALDDLVTVEEHLYFYARVH---GIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYG----TKRKLSTALALIGK 2089
Cdd:TIGR00956 840 YVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAK 919
|
170 180
....*....|....*....|....*.
gi 27881501 2090 PSILL-LDEPSSGMDPKSKrhlWKII 2114
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTA---WSIC 942
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1945-2150 |
1.35e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1945 YQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGdIIPS--SGNILIRNKTGSLGH-VDSHSSLVGYCPQE 2021
Cdd:TIGR02633 266 WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKPVDIRNpAQAIRAGIAMVPED 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2022 DALDDLV-----------TVEEHLYFYARVHGIPEKDIketVHKLLRRLHLMPFK-DRATSMCSYGTKRKLSTALALIGK 2089
Cdd:TIGR02633 345 RKRHGIVpilgvgknitlSVLKSFCFKMRIDAAAELQI---IGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2090 PSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQ 2150
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1022-1236 |
1.53e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1022 KDLTVGVALHGvtkiyGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISML-----TGLFgaSAGTIFVYGKDIKTdlh 1096
Cdd:TIGR00956 763 RNLTYEVKIKK-----EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDS--- 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1097 TVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVP-HWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGM----KRKLSI 1171
Cdd:TIGR00956 833 SFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTI 912
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1172 SIALIGGSRVVI-LDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLS--DRIAFLEQGG 1236
Cdd:TIGR00956 913 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEefDRLLLLQKGG 980
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1043-1237 |
1.78e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1043 VDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI--KTDLHTVRKNMGVCMQH---DVLFSYLTT 1117
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrdNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1118 KEHLLLYGSIKVPHW----------TKKQLHEEVKrtlKDTGLYSHR-HKRVGTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:PRK09700 359 AQNMAISRSLKDGGYkgamglfhevDEQRTAENQR---ELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1187 PSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1956-2140 |
1.97e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1956 NNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirnKTgslghvdSHSSLVGYCPQ--EDALDDLVTVEEH 2033
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KW-------SENANIGYYAQdhAYDFENDLTLFDW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARvhgipEKDIKETVHKLLRRLhLMPFKD--RATSMCSYGTK-RKLSTALALiGKPSILLLDEPSSGMDPKSkrhl 2110
Cdd:PRK15064 405 MSQWRQ-----EGDDEQAVRGTLGRL-LFSQDDikKSVKVLSGGEKgRMLFGKLMM-QKPNVLVMDEPTNHMDMES---- 473
|
170 180 190
....*....|....*....|....*....|....*
gi 27881501 2111 wkIisEEVQN-----KCSVILTSHSMEECEALCTR 2140
Cdd:PRK15064 474 --I--ESLNMalekyEGTLIFVSHDREFVSSLATR 504
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1954-2149 |
2.00e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslgHVDSHSSL------VGYCPQEDALDDL 2027
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-----EIDFKSSKealengISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 VTVEEHLYF--YARV-----HGIPEKDIKETVHKLlrRLHLMPFKDRATsmCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:PRK10982 88 RSVMDNMWLgrYPTKgmfvdQDKMYRDTKAIFDEL--DIDIDPRAKVAT--LSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQW 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1012-1237 |
2.97e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1012 MFSSNIEPEPKdltvgVALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI 1091
Cdd:PRK15439 1 MQTSDTTAPPL-----LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1092 KTDLHTVRKNMGVCM--QHDVLFSYLTTKEHLLLygsiKVPhwtKKQLHEE-VKRTLKDTGLYSHRHKRVGTLSGGMKRK 1168
Cdd:PRK15439 76 ARLTPAKAHQLGIYLvpQEPLLFPNLSVKENILF----GLP---KRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1169 LSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1237
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRElLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1956-2148 |
3.13e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.72 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1956 NNISIGIPAGECFGLLGVNGAGKTTIFKML-------TGDII--------PSSGNILIRNKTGSlghVDSHSSLVgycPQ 2020
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIvdglkvndPKVDERLIRQEAGM---VFQQFYLF---PH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLvtveehLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:PRK09493 92 LTALENV------MFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1039-1251 |
3.15e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.85 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1039 SKVAVDN----LNLNFYEGHITSLLGPNGAGKTTTISMLTGLFgASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVL-- 1111
Cdd:COG4138 4 NDVAVAGrlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELARHRAYLSQQQSPpf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1112 ----FSYLTtkehllLYGSIKVPHWTKKQLHEEVKRTLKDTGLYshrHKRVGTLSGGMKRK-------LSISIALIGGSR 1180
Cdd:COG4138 83 ampvFQYLA------LHQPAGASSEAVEQLLAQLAEALGLEDKL---SRPLTQLSGGEWQRvrlaavlLQVWPTINPEGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1181 VVILDEPSTGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGS------PFYLKEAFG 1251
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGEtaevmtPENLSEVFG 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1935-2150 |
3.17e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.83 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1935 LVQLYCLTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIR----NKTGSLGHVDS 2010
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2011 HSSLVGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISE-EVQNKCSVILTSHSMEECEALCTRLAiMVNGKFQ 2150
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLT 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1955-2114 |
3.61e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.81 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPS---SGNILIRNKTGSLGHVDSHSSLVgYCPQEDALDDLVTVE 2031
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEII-YVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 EHLYFYARVHGipekdiketvHKLLRRLhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLW 2111
Cdd:cd03233 102 ETLDFALRCKG----------NEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
...
gi 27881501 2112 KII 2114
Cdd:cd03233 159 KCI 161
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1041-1251 |
3.65e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1041 VAVDN----LNLNFYEGHITSLLGPNGAGKTTTISMLTGLFgASAGTIFVYGKDIKT----DLHTVRKNMgvCMQHDVLF 1112
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYL--SQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1113 S-----YLTtkehllLYGSIKVPHWTKKQLHEEVKRTLKDTGLYsHRHkrVGTLSGGMKRK-------LSISIALIGGSR 1180
Cdd:PRK03695 83 AmpvfqYLT------LHQPDKTRTEAVASALNEVAEALGLDDKL-GRS--VNQLSGGEWQRvrlaavvLQVWPDINPAGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1181 VVILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGS------PFYLKEAFG 1251
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSElCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRrdevltPENLAQVFG 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1945-2133 |
3.93e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1945 YQLIHKKIiaVNNISIGIPAGEcFGLL-GVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDA 2023
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2024 L--DdlvTVEEHLYFYARVHGI-PEKDiketvhKLLRrlHLMPFK------DRATSMCSYGTKRKLSTALALIGKPSILL 2094
Cdd:PRK10247 92 LfgD---TVYDNLIFPWQIRNQqPDPA------IFLD--DLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27881501 2095 LDEPSSGMDPKSKRHLWKIISEEVQNK-CSVILTSHSMEE 2133
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQnIAVLWVTHDKDE 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1957-2116 |
4.06e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKT------GSLGHVDSHSSLVGycpQEDALDDLVTV 2030
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsrSRLYTVRKRMSMLF---QSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEHLYFYARVHG-IPEKDIKETV-HKL----LR-RLHLMPfkdratSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:PRK11831 102 FDNVAYPLREHTqLPAPLLHSTVmMKLeavgLRgAAKLMP------SELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170
....*....|...
gi 27881501 2104 PKSKRHLWKIISE 2116
Cdd:PRK11831 176 PITMGVLVKLISE 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1954-2172 |
4.67e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.38 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslghvdshsSLVGYCpqEDALDDLVTVEEH 2033
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ-----------PIADYS--EAALRQAISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 lyfyaRVH------------GIPEKDiKETVHKLLRRLHLMPFKDRATSM----------CSYGTKRKLSTALALIGKPS 2091
Cdd:PRK11160 422 -----RVHlfsatlrdnlllAAPNAS-DEALIEVLQQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2092 ILLLDEPSSGMDPKSKRHLWKIISEEVQNKcSVILTSH---SMEECEALCtrlaIMVNGKFQCIGSLQHIKSRFGRGFTV 2168
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQELLAQQGRYYQL 570
|
....
gi 27881501 2169 KVHL 2172
Cdd:PRK11160 571 KQRL 574
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1954-2129 |
4.99e-09 |
|
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: 58.66 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTI----FKMLTgdiiPSSGNILIRNK-TGSLGHVDSHSSLvGYCPQE------- 2021
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLVE----LSSGSILIDGVdISKIGLHDLRSRI-SIIPQDpvlfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2022 --DALDDLvtvEEHlyfyarvhgiPEKDIKETVHK--LLRRLHLMPFKDRAT-----SMCSYGTKRKLSTALALIGKPSI 2092
Cdd:cd03244 94 irSNLDPF---GEY----------SDEELWQALERvgLKEFVESLPGGLDTVveeggENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 27881501 2093 LLLDEPSSGMDPKSKRHLWKIISEEVQNkCSVILTSH 2129
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKD-CTVLTIAH 196
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1954-2148 |
5.56e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTG------------------DIIPSSGniliRNKTGSLGHvdsHSSLV 2015
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddiDLLRLSP----RERRKLVGH---NVSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 GYCPQEdALDDLVTVEEHLyfyarVHGIPEKDIK----ETVHKLLRR----LHLMPFKDRATSMCSY------GTKRKLS 2081
Cdd:PRK15093 95 FQEPQS-CLDPSERVGRQL-----MQNIPGWTYKgrwwQRFGWRKRRaielLHRVGIKDHKDAMRSFpyelteGECQKVM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2082 TALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVI-LTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1033-1235 |
6.22e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.19 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1033 VTKIYGSK--VAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHD 1109
Cdd:PRK11176 347 VTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1110 VLFSylTTKEHLLLYGSikvphwTKKQLHEEVKRTLK-----------DTGLyshrHKRVG----TLSGGMKRKLSISIA 1174
Cdd:PRK11176 427 HLFN--DTIANNIAYAR------TEQYSREQIEEAARmayamdfinkmDNGL----DTVIGengvLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1175 LIGGSRVVILDEPSTGVDPCSRRSIW---DVISKNKTARTIilsTHHLDEAEVlSDRIAFLEQG 1235
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQaalDELQKNRTSLVI---AHRLSTIEK-ADEILVVEDG 554
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1957-2155 |
6.54e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.27 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgsLghVDSHSSL--------VGYCPQEDALDDLV 2028
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV--L--FDAEKGIclppekrrIGYVFQDARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2029 TVEEHLYFyarvhGIPEKDiKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKR 2108
Cdd:PRK11144 92 KVRGNLRY-----GMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27881501 2109 HLW---KIISEEVqnKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSL 2155
Cdd:PRK11144 166 ELLpylERLAREI--NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1962-2103 |
7.15e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1962 IPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslghvdshsslVGYCPQEDALDDLVTVEEHLyfyarvh 2041
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISYKPQYIKPDYDGTVEDLL------- 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2042 gipeKDIKETV------HKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:PRK13409 422 ----RSITDDLgssyykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2073-2132 |
8.13e-09 |
|
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: 59.33 E-value: 8.13e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2073 SYGTKRKLSTALALI---GKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSME 2132
Cdd:pfam13304 238 SDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1965-2103 |
9.10e-09 |
|
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: 60.57 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1965 GECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslghvdshsslVGYCPQEDALDDLVTVEEHLYfyarvhgip 2044
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------ISYKPQYISPDYDGTVEEFLR--------- 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2045 eKDIKETV------HKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:COG1245 424 -SANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1045-1226 |
9.25e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.29 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1045 NLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVR-----KNMGVCMQ-HDVL--FSYLT 1116
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQfHHLLpdFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEHLLLYGSIKvphwtKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSR 1196
Cdd:PRK11629 107 NVAMPLLIGKKK-----PAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|..
gi 27881501 1197 RSIWDVISK-NKTARTIIL-STHHLDEAEVLS 1226
Cdd:PRK11629 182 DSIFQLLGElNRLQGTAFLvVTHDLQLAKRMS 213
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1965-2129 |
1.32e-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: 58.15 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1965 GECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirNKTGSLGHVDSH---SSLVGYCPQ--EDALDDLVTVEEHLYFYAR 2039
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---DDPPDWDEILDEfrgSELQNYFTKllEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2040 VHG-----IPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKII 2114
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170
....*....|....*
gi 27881501 2115 SEEVQNKCSVILTSH 2129
Cdd:cd03236 183 RELAEDDNYVLVVEH 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1953-2103 |
1.45e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.18 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrNKTGSLGHVDSHSslvgycpqedaLDDLVTVEE 2032
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYFAQHQ-----------LEFLRADES 393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2033 HLYFYARVhgIPekdiKETVHKLLRRLHLMPFK-DRATSMC---SYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:PRK10636 394 PLQHLARL--AP----QELEQKLRDYLGGFGFQgDKVTEETrrfSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1031-1235 |
1.69e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1031 HGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKD-IKTDLHT---------VRK 1100
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYAlseaerrrlLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1101 NMGVCMQH--DVLFSYLTT----KEHLLL-----YGSI--KVPHWTKKQlheEVKRTLKDtglyshrhKRVGTLSGGMKR 1167
Cdd:PRK11701 90 EWGFVHQHprDGLRMQVSAggniGERLMAvgarhYGDIraTAGDWLERV---EIDAARID--------DLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1168 KLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVIsKNKTAR---TIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLL-RGLVRElglAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1057-1217 |
1.73e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1057 SLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVR-----KNMGVCMQHDVLFSYLTTKEHL----LLYGSi 1127
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALENVelpaLLRGE- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1128 kvphwTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVI-SKN 1206
Cdd:PRK10584 119 -----SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfSLN 193
|
170
....*....|..
gi 27881501 1207 KT-ARTIILSTH 1217
Cdd:PRK10584 194 REhGTTLILVTH 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1040-1236 |
2.27e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1040 KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTG--LFGASAGTIFVYGKDIKTDLHTVrknmgvcmqhdvlfsyltt 1117
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGREASLI------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1118 kEHLLLYGSIKvphwtkkqlheEVKRTLKDTGL---YSHRhKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDpc 1194
Cdd:COG2401 104 -DAIGRKGDFK-----------DAVELLNAVGLsdaVLWL-RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD-- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 1195 srRSIWDVISKN------KTARTIILSTHHLDEAEVLS-DRIAFLEQGG 1236
Cdd:COG2401 169 --RQTAKRVARNlqklarRAGITLVVATHHYDVIDDLQpDLLIFVGYGG 215
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1019-1236 |
2.91e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1019 PEPKDLTVGVAL----------HGVTKiYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTG-----------LF 1077
Cdd:PRK10938 243 PEPDEPSARHALpaneprivlnNGVVS-YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLF 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1078 G---ASAGTIFvygkDIKtdlhtvrKNMGvcmqhdvlfsYLTTKEHL-----------LLYG---SIKVPHWTKKQLHEE 1140
Cdd:PRK10938 322 GrrrGSGETIW----DIK-------KHIG----------YVSSSLHLdyrvstsvrnvILSGffdSIGIYQAVSDRQQKL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1141 VKRTLKDTGLyshrHKRVG-----TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSR---RSIWDVISKNKTARTI 1212
Cdd:PRK10938 381 AQQWLDILGI----DKRTAdapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLISEGETQLL 456
|
250 260
....*....|....*....|....
gi 27881501 1213 ILSTHHLDEAEVLSDRIAFLEQGG 1236
Cdd:PRK10938 457 FVSHHAEDAPACITHRLEFVPDGD 480
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1950-2158 |
3.08e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1950 KKIIAvNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKtgslgHVDSHSS-----LVGYCPQEDAL 2024
Cdd:PRK10253 19 KYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-----HIQHYASkevarRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2025 DDLVTVEEhLYFYARVHGIP-----EKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPS 2099
Cdd:PRK10253 93 PGDITVQE-LVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2100 SGMDPKSKRHLWKIISEEVQNK-CSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1972-2130 |
3.45e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1972 GVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSlghvDSHSSLVGYCPQEDALDDLVTVEEHLYFYARVHgipekDIKET 2051
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN----NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAET 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2052 VHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHS 2130
Cdd:PRK13541 104 LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1957-2149 |
3.47e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKT-GSLGHVDS-HSSLVgYCPqEDALDDLVTVEEHL 2034
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEiNALSTAQRlARGLV-YLP-EDRQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2035 YF--YARVHGIP--------EKDIKETVHKLL--RRLHLmpfkDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGM 2102
Cdd:PRK15439 359 AWnvCALTHNRRgfwikparENAVLERYRRALniKFNHA----EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27881501 2103 DPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKF 2149
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1962-2103 |
3.63e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1962 IPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI--------------RNKTGS--------LGHVDSH-------S 2012
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqqdppRNVEGTvydfvaegIEEQAEYlkryhdiS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2013 SLVGYCPQEDALDDLVTVEEHLyfyaRVHGIPEKDIKetVHKLLRRLHLMPfkDRATSMCSYGTKRKLSTALALIGKPSI 2092
Cdd:PRK11147 106 HLVETDPSEKNLNELAKLQEQL----DHHNLWQLENR--INEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDV 177
|
170
....*....|.
gi 27881501 2093 LLLDEPSSGMD 2103
Cdd:PRK11147 178 LLLDEPTNHLD 188
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1958-2150 |
3.83e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.90 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1958 ISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNI--------LIRNKTGSLGHVDSH------SSLVGYCPQEDA 2023
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinLVRDKDGQLKVADKNqlrllrTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2024 LDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMP-FKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGM 2102
Cdd:PRK10619 104 WSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27881501 2103 DPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQ 2150
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1954-2154 |
4.57e-08 |
|
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: 55.88 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK-TGSLGHVDSHSSLvGYCPQEDALDDlVTVEE 2032
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdISTIPLEDLRSSL-TIIPQDPTLFS-GTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2033 HLYFYARVhgiPEKDIKETVHKLLRRLHLmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWK 2112
Cdd:cd03369 101 NLDPFDEY---SDEEIYGALRVSEGGLNL-----------SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27881501 2113 IISEEVQNkcSVILT-SHSMEECeALCTRLAIMVNGKFQCIGS 2154
Cdd:cd03369 167 TIREEFTN--STILTiAHRLRTI-IDYDKILVMDAGEVKEYDH 206
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1042-1238 |
4.64e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.75 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGkdiktDLHTVRKNMGVCMQhdvlfsyLTTKEH- 1120
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ-------LTGIENi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1121 ---LLLYGsikvphWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP-STGVDPCSR 1196
Cdd:PRK13546 107 efkMLCMG------FKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27881501 1197 RSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1949-2148 |
4.65e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1949 HKKIiaVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGdIIP--SSGNILIRNKTGSLGH-VDSHSSLVGYCPQEDALD 2025
Cdd:PRK13549 274 HIKR--VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2026 DLVT---VEEH-----LYFYARVHGIPEKDIKETVHKLLRRLHL-MPFKDRATSMCSYGTKRKLSTALALIGKPSILLLD 2096
Cdd:PRK13549 351 GIVPvmgVGKNitlaaLDRFTGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2097 EPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1929-2126 |
4.97e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1929 GAAEFDLVqlyclTKTYQliHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTG--DIipSSGNILIrnktgslg 2006
Cdd:PRK11176 340 GDIEFRNV-----TFTYP--GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfyDI--DEGEILL-------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2007 hvDSH-------SSLVGYCPqedalddLVTVEEHLY--------FYARvhgiPEKDIKETVHKLLRRLHLMPFKDRATS- 2070
Cdd:PRK11176 403 --DGHdlrdytlASLRNQVA-------LVSQNVHLFndtianniAYAR----TEQYSREQIEEAARMAYAMDFINKMDNg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2071 ----------MCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVIL 2126
Cdd:PRK11176 470 ldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI 535
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1955-2032 |
5.51e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 5.51e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrNKTGSLGHVDSHsslvgycpqEDALDDLVTVEE 2032
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLAYVDQS---------RDALDPNKTVWE 407
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1952-2103 |
6.05e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1952 IIAVNNISIGIPAGEC------FGL--------LGVNGAGKTTIFKMLTGDIIPSSGNIL----IRNKTGSLGHVdshss 2013
Cdd:PLN03073 508 IISFSDASFGYPGGPLlfknlnFGIdldsriamVGPNGIGKSTILKLISGELQPSSGTVFrsakVRMAVFSQHHV----- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2014 lvgycpqeDALDdlVTVEEHLYFYARVHGIPEKDIketvhkllrRLHLMPF------KDRATSMCSYGTKRKLSTALALI 2087
Cdd:PLN03073 583 --------DGLD--LSSNPLLYMMRCFPGVPEQKL---------RAHLGSFgvtgnlALQPMYTLSGGQKSRVAFAKITF 643
|
170
....*....|....*.
gi 27881501 2088 GKPSILLLDEPSSGMD 2103
Cdd:PLN03073 644 KKPHILLLDEPSNHLD 659
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1950-2154 |
6.98e-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: 54.84 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1950 KKIiaVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTG--DIIPSSGNILIRNktgslghvdshsslvgycpqEDALDdl 2027
Cdd:cd03217 13 KEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKG--------------------EDITD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 VTVEEH------LYFY--ARVHGIpekdikeTVHKLLRRLHlMPFkdratsmcSYGTKRKLSTALALIGKPSILLLDEPS 2099
Cdd:cd03217 69 LPPEERarlgifLAFQypPEIPGV-------KNADFLRYVN-EGF--------SGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27881501 2100 SGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEAL-CTRLAIMVNGKFQCIGS 2154
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1047-1192 |
9.56e-08 |
|
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: 54.58 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1047 NLNFY--EGHITSLLGPNGAGKTT---TISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHDVLFSYLTtkehl 1121
Cdd:cd03233 25 DFSGVvkPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLT----- 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1122 llygsikvphwtkkqlheeVKRTLkDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVD 1192
Cdd:cd03233 100 -------------------VRETL-DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1894-2163 |
9.57e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1894 IKKLRLFFrkfnsSHvrETIDEDEdvrAERLRVESGAAEFDLVQlyclTKTYQLIHKKIIAVNNISIGIPAGECFGLLGV 1973
Cdd:TIGR00957 607 LKRLRIFL-----SH--EELEPDS---IERRTIKPGEGNSITVH----NATFTWARDLPPTLNGITFSIPEGALVAVVGQ 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1974 NGAGKTTIFKMLTGDIIPSSGNILIRnktGSlghvdshsslVGYCPQEDALDDlVTVEEHLYFYarvHGIPEKDIKETVH 2053
Cdd:TIGR00957 673 VGCGKSSLLSALLAEMDKVEGHVHMK---GS----------VAYVPQQAWIQN-DSLRENILFG---KALNEKYYQQVLE 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2054 K--LLRRLHLMPFKDRAT-----SMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLW-KIISEE--VQNKCS 2123
Cdd:TIGR00957 736 AcaLLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEgvLKNKTR 815
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 27881501 2124 VILTsHSMEECEALcTRLAIMVNGKFQCIGSLQHIKSRFG 2163
Cdd:TIGR00957 816 ILVT-HGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1941-2032 |
1.12e-07 |
|
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: 56.87 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQliHKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrNKTGSLGHVDShsslvgycpQ 2020
Cdd:TIGR03719 328 LTKAFG--DKLLI--DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQ---------S 393
|
90
....*....|..
gi 27881501 2021 EDALDDLVTVEE 2032
Cdd:TIGR03719 394 RDALDPNKTVWE 405
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1952-2132 |
1.14e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 54.64 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1952 IIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL----VGYCPQEDALDDl 2027
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 VTVEEHLYFYARVHGIPEKDIKETVhKLLRRLHLMPFKD------RATSMcSYGTKRKLSTALALIGKPSILLLDEPSSG 2101
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDAC-SLQPDIDLLPFGDqteigeRGINL-SGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190
....*....|....*....|....*....|...
gi 27881501 2102 MDPKSKRHLWK--IISEEVQNKCSVILTSHSME 2132
Cdd:cd03290 171 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1028-1235 |
1.19e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1028 VALHGVTKIYGS-KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNmGVCM 1106
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ-GVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1107 -QHD--VL----FSYLTTKEHLllyGSIKVphWT---KKQLHEEVkRTLKDtGLYSHRHKRVGTLSGGMKRKLSISIALI 1176
Cdd:PRK10790 420 vQQDpvVLadtfLANVTLGRDI---SEEQV--WQaleTVQLAELA-RSLPD-GLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1177 GGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAeVLSDRIAFLEQG 1235
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI-VEADTILVLHRG 550
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1030-1235 |
1.21e-07 |
|
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: 54.75 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LH--GVTKIygskVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHT--------VR 1099
Cdd:COG4778 16 LHlqGGKRL----PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQaspreilaLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1100 KN-MGVCMQH----------DVlfsyltTKEHLLLYGsikvphWTKKQLHEEVKRTLkdtglyshRHKRV---------G 1159
Cdd:COG4778 92 RRtIGYVSQFlrviprvsalDV------VAEPLLERG------VDREEARARARELL--------ARLNLperlwdlppA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1160 TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILS-THHLDEAEVLSDRIAFLEQG 1235
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGiFHDEEVREAVADRVVDVTPF 228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1957-2142 |
1.99e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRN--KTGSLGH----------VDS----HSSLVGYCPQ 2020
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPneRLGKLRQdqfafeeftvLDTvimgHTELWEVKQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDAL--------DDLVTVEEHLYFYARVHG---------------IPEKdiketvhkllrrLHLMPFKDRATsmcsyGTK 2077
Cdd:PRK15064 99 RDRIyalpemseEDGMKVADLEVKFAEMDGytaearagelllgvgIPEE------------QHYGLMSEVAP-----GWK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 2078 RKLSTALALIGKPSILLLDEPSSGMDPKSKRHLwkiisEEVQN--KCSVILTSHSMEECEALCTRLA 2142
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWL-----EDVLNerNSTMIIISHDRHFLNSVCTHMA 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1027-1242 |
2.18e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.32 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1027 GVALHGVTkIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGA----SAGTIFVYGKDIKtdLHTVR-KN 1101
Cdd:PRK10418 4 QIELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA--PCALRgRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1102 MGVCMQHD-VLFSYLTT-----KEHLLLYGSIKVPHWTKKQLH----EEVKRTLKdtgLYSHRhkrvgtLSGGMKRKLSI 1171
Cdd:PRK10418 81 IATIMQNPrSAFNPLHTmhthaRETCLALGKPADDATLTAALEavglENAARVLK---LYPFE------MSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1172 SIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGS 1242
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1031-1188 |
2.46e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1031 HGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVyGKdiktdlhTVRknmgvcmqhdv 1110
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE-------TVK----------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1111 lFSYL-TTKEHLLlygsikvphwTKKQLHEEV----------KRTLKDTGlYSHR--------HKRVGTLSGGMKRKLSI 1171
Cdd:PRK11819 389 -LAYVdQSRDALD----------PNKTVWEEIsggldiikvgNREIPSRA-YVGRfnfkggdqQKKVGVLSGGERNRLHL 456
|
170
....*....|....*..
gi 27881501 1172 SIALIGGSRVVILDEPS 1188
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPT 473
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1953-2158 |
2.87e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTifkmlTG----DIIPSSGNI---------LIRNKTGSLGH------VDSHSS 2013
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKST-----TGlallRLINSQGEIwfdgqplhnLNRRQLLPVRHriqvvfQDPNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2014 LvgyCPQedaLDDLVTVEEHLyfyaRVH--GIPEKDIKETVHKLLRRLHLMP-FKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:PRK15134 375 L---NPR---LNVLQIIEEGL----RVHqpTLSAAQREQQVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKII-SEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIGSLQHI 2158
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLkSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1030-1238 |
3.36e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1030 LHGVTKIYG-SKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI-KTDLHTVRKnmgvcmq 1107
Cdd:PRK10522 325 LRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRK------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 hdvLFSYLTTKEHL---LLYGSIKVPhwtKKQLHEEVKRTLKDTGLYSHRHKRVGT--LSGGMKRKLSISIALIGGSRVV 1182
Cdd:PRK10522 398 ---LFSAVFTDFHLfdqLLGPEGKPA---NPALVEKWLERLKMAHKLELEDGRISNlkLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1183 ILDEPSTGVDPCSRRSIWDVI-----SKNKTARTIILSTHHLDEAevlsDRIAFLEQGGLR 1238
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLlpllqEMGKTIFAISHDDHYFIHA----DRLLEMRNGQLS 528
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1035-1192 |
3.68e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1035 KIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFgASAGTIFVYGKDIKT----DLHTVRKNMGVCMQ--H 1108
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNlnrrQLLPVRHRIQVVFQdpN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYLTTKEhlLLYGSIKV--PHWTKKQLHEEVKRTLKDTGL-YSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:PRK15134 373 SSLNPRLNVLQ--IIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
....*..
gi 27881501 1186 EPSTGVD 1192
Cdd:PRK15134 451 EPTSSLD 457
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1953-2148 |
3.69e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.24 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGdIIPSSGNILIRN---KTGSLGHVDSHSSLVGYCPQ--EDALDDL 2027
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGielRELDPESWRKHLSWVGQNPQlpHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 VTVEEHLYFYARVHGIPEK-DIKETVHKLLRRLHLmPFKDRATSMcSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2106
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENaWVSEFLPLLPQGLDT-PIGDQAAGL-SVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27881501 2107 KRHLWKIISEEVQNKCSVILTsHSMEECEAlCTRLAIMVNGK 2148
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVT-HQLEDLAQ-WDQIWVMQDGQ 560
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1046-1249 |
3.82e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1046 LNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSYLTTKEhLLLY 1124
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRE-LVAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1125 GsiKVP-HWTKKQL----HEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSI 1199
Cdd:PRK10575 109 G--RYPwHGALGRFgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1200 WDVISKNKTAR--TIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEA 1249
Cdd:PRK10575 187 LALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1935-2129 |
4.38e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1935 LVQLYCLTKTYQLIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL 2014
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 ----VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:PRK10535 84 rrehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSH 2129
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1943-2129 |
5.21e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1943 KTYQLIHKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDI--IPSSGNILIRNktgslGHVDSHSSLVgycpq 2020
Cdd:COG2401 36 VELRVVERYVL--RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD-----NQFGREASLI----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 eDALDDLVTVEEHLYFYARVhGIPEKdiketvhKLLRRlhlmPFKDratsmCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:COG2401 104 -DAIGRKGDFKDAVELLNAV-GLSDA-------VLWLR----RFKE-----LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|
gi 27881501 2101 GMDPKSKRHLWKIISEEVQ-NKCSVILTSH 2129
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARrAGITLVVATH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1958-2148 |
5.26e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1958 ISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHV-DSHSSLVGYCPQEDALDDLV---TVEEH 2033
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRAGIMLCPEDRKAEGIIpvhSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARVHGIPEKDI------KETVHKLLRRLHL-MPFKDRATSMCSYGTKRK--LSTALALIGKpsILLLDEPSSGMDP 2104
Cdd:PRK11288 352 INISARRHHLRAGCLinnrweAENADRFIRSLNIkTPSREQLIMNLSGGNQQKaiLGRWLSEDMK--VILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881501 2105 KSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1955-2148 |
5.95e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.22 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirnKTGSLgHVDSHSSL-------------VGYC--- 2018
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI----RVGDI-TIDTARSLsqqkglirqlrqhVGFVfqn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2019 ----PQEDALDDLVtvEEHLYfyarVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILL 2094
Cdd:PRK11264 94 fnlfPHRTVLENII--EGPVI----VKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27881501 2095 LDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1955-2153 |
7.43e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLtgdiipssgNILIrnKTGSLGHVDSHSSLVG---YCPQEDALDDLVTVE 2031
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTF---------NRLL--ELNEEARVEGEVRLFGrniYSPDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2032 ---------EHLYFYARVH-GI-------PEKDIKETVHKLLRRLHLM-PFKDRAT---SMCSYGTKRKLSTALALIGKP 2090
Cdd:PRK14267 89 mvfqypnpfPHLTIYDNVAiGVklnglvkSKKELDERVEWALKKAALWdEVKDRLNdypSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISeEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCIG 2153
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLF-ELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1954-2131 |
8.56e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.18 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI------RNKTGSLGHVDSHsslVGYCPQEDALDDL 2027
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghditRLKNREVPFLRRQ---IGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2028 VTVEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMpfkDRATSM---CSYGTKRKLSTALALIGKPSILLLDEPSSGMDP 2104
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLL---DKAKNFpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180
....*....|....*....|....*..
gi 27881501 2105 KSKRHLWKIISEEVQNKCSVILTSHSM 2131
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1961-2129 |
8.85e-07 |
|
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: 54.02 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1961 GIPA---GECFGLLGVNGAGKTTIFKMLTGDIIPSsgnilirnktgsLGHVDSHSSlvgycpQEDALDDLVTVEEHLYFY 2037
Cdd:COG1245 92 GLPVpkkGKVTGILGPNGIGKSTALKILSGELKPN------------LGDYDEEPS------WDEVLKRFRGTELQDYFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2038 A-------------RVHGIPeKDIKETVHKLLRR-------------LHLMPFKDRATSMCSYGTKRKLSTALALIGKPS 2091
Cdd:COG1245 154 KlangeikvahkpqYVDLIP-KVFKGTVRELLEKvdergkldelaekLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881501 2092 ILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSH 2129
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1053-1235 |
9.93e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1053 GHITSLLGPNGAGKTttiSMLTGLFGA---SAGTIFVYGK--------------------DIKTD----LHTVRKNMGVc 1105
Cdd:PRK11288 279 GEIVGLFGLVGAGRS---ELMKLLYGAtrrTAGQVYLDGKpidirsprdairagimlcpeDRKAEgiipVHSVADNINI- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1106 mqhdvlfsylTTKEHLLLYGSIKVPHWTKKQLHEEVKRTLKDTglySHRHKRVGTLSGGMKRKLSISIALIGGSRVVILD 1185
Cdd:PRK11288 355 ----------SARRHHLRAGCLINNRWEAENADRFIRSLNIKT---PSREQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1186 EPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1022-1238 |
1.24e-06 |
|
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: 52.55 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1022 KDLTVgvalhgvTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGaSAGTIFVYGKDIKT-DLHTVRK 1100
Cdd:cd03289 6 KDLTA-------KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1101 NMGVCMQHDVLFSYlTTKEHLLLYGSikvphWTKkqlhEEVKRTLKDTGLYSHRHKRVG-----------TLSGGMKRKL 1169
Cdd:cd03289 78 AFGVIPQKVFIFSG-TFRKNLDPYGK-----WSD----EEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLM 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1170 SISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLdEAEVLSDRIAFLEQGGLR 1238
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1050-1236 |
1.39e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1050 FYEGHITSLLGPNGAGKTTTISMLTG--LFGASAGTIFVYGKDIKTDlhTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSI 1127
Cdd:PLN03140 903 FRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISGFPKKQE--TFARISGYCEQNDIHSPQVTVRESLIYSAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1128 KVPHWTKK--------QLHEEVK-RTLKDT--GLYShrhkrVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCS- 1195
Cdd:PLN03140 981 RLPKEVSKeekmmfvdEVMELVElDNLKDAivGLPG-----VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAa 1055
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27881501 1196 ---RRSIWDVISknkTARTIILSTHH--LDEAEVLsDRIAFLEQGG 1236
Cdd:PLN03140 1056 aivMRTVRNTVD---TGRTVVCTIHQpsIDIFEAF-DELLLMKRGG 1097
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1954-2108 |
1.89e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSLVGycpqedalddlvTVEEH 2033
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS------------AVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARVHGiPEKDIKET--VHKLLRRL---HLMPFKDR--ATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2106
Cdd:PRK10522 406 FHLFDQLLG-PEGKPANPalVEKWLERLkmaHKLELEDGriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
..
gi 27881501 2107 KR 2108
Cdd:PRK10522 485 RR 486
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1033-1192 |
2.10e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1033 VTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVyGKDIKtdlhtvrknMGVCMQHDVlf 1112
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK---------LGYFAQHQL-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1113 SYLTTKEHLLLYGSIKVPHWTKKQLHEEVkrtlkdtGLYSHRHKRV----GTLSGGMKRKLsiSIALIGGSR--VVILDE 1186
Cdd:PRK10636 386 EFLRADESPLQHLARLAPQELEQKLRDYL-------GGFGFQGDKVteetRRFSGGEKARL--VLALIVWQRpnLLLLDE 456
|
....*.
gi 27881501 1187 PSTGVD 1192
Cdd:PRK10636 457 PTNHLD 462
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1957-2135 |
2.56e-06 |
|
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: 50.93 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSL-GHVDSHS--SLVGYCPQEDALddlvTVEEH 2033
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSkvSLVGQEPVLFAR----SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFyaRVHGIPEKDIKET-----VHKLLRRLHLMPFKD--RATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2106
Cdd:cd03248 108 IAY--GLQSCSFECVKEAaqkahAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180
....*....|....*....|....*....
gi 27881501 2107 KRHLWKIISEEVQNKcSVILTSHSMEECE 2135
Cdd:cd03248 186 EQQVQQALYDWPERR-TVLVIAHRLSTVE 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1953-2129 |
2.92e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.09 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1953 IAVNNISIG---------IPAGECFGLLGVNGAGKTTIFKMLTGdIIPSSGNILIRNKtgSLGHVdSHSSLV---GYCPQ 2020
Cdd:PRK03695 1 MQLNDVAVStrlgplsaeVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQ--PLEAW-SAAELArhrAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTVEEHLYFYaRVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGT-KRKLSTALALIGKPSI------L 2093
Cdd:PRK03695 77 QQTPPFAMPVFQYLTLH-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEwQRVRLAAVVLQVWPDInpagqlL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 27881501 2094 LLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSH 2129
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1032-1235 |
3.97e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1032 GVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGL--FGASAGTIFVYG-----KDIKTDLHtvrknMGV 1104
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGevcrfKDIRDSEA-----LGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1105 CMQHD--VLFSYLTTKEHLLL------YGSIkvpHWtkKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALI 1176
Cdd:NF040905 81 VIIHQelALIPYLSIAENIFLgnerakRGVI---DW--NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1177 GGSRVVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILStHHLDEAEVLSDRIAFLEQG 1235
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLelKAQGITSIIIS-HKLNEIRRVADSITVLRDG 215
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1044-1230 |
4.04e-06 |
|
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: 48.90 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1044 DNLNLNFYEGHITSLLGPNGAGKTTTI-SMLTGLFGASAGTifvygkdiktdlhtvRKNMGVCMQHDVLFSYLTtkehll 1122
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKSTILdAIGLALGGAQSAT---------------RRRSGVKAGCIVAAVSAE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1123 lygsikvphwtkkqlheevkrtlkdtgLYSHRHKrvgtLSGGMKRKLSISIAL----IGGSRVVILDEPSTGVDPCSRRS 1198
Cdd:cd03227 71 ---------------------------LIFTRLQ----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|....
gi 27881501 1199 IWDVISKN--KTARTIILSthHLDEAEVLSDRIA 1230
Cdd:cd03227 120 LAEAILEHlvKGAQVIVIT--HLPELAELADKLI 151
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1044-1192 |
4.09e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1044 DNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDLHTVRKNMGVCMQHDVLFSYLTTKEHLLL 1123
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 1124 YGSIKVPhwtkkQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVD 1192
Cdd:PRK13538 98 YQRLHGP-----GDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1954-2103 |
4.39e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 51.99 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGdIIPSSGNILIRNKtgSLGHVDSH-----------------SSL-- 2014
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQ--DLDGLSRRalrplrrrmqvvfqdpfGSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2015 ---VGycpQedalddlvTVEEHLyfyaRVHGIP--EKDIKETVHKLLRRLHLMP-FKDRATSMCSYGTKRKLSTALALIG 2088
Cdd:COG4172 378 rmtVG---Q--------IIAEGL----RVHGPGlsAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALIL 442
|
170
....*....|....*
gi 27881501 2089 KPSILLLDEPSSGMD 2103
Cdd:COG4172 443 EPKLLVLDEPTSALD 457
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1941-2110 |
4.47e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLiHKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrnktgslghvdSHSSLVGYCPQ 2020
Cdd:TIGR03719 10 VSKVVPP-KKEIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-----------QPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVTVEEH--------LYFYARVHGIPEK-------------------DIKETV--HKLLRRLHL------MPFK 2065
Cdd:TIGR03719 76 EPQLDPTKTVRENveegvaeiKDALDRFNEISAKyaepdadfdklaaeqaelqEIIDAAdaWDLDSQLEIamdalrCPPW 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2066 DRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS----KRHL 2110
Cdd:TIGR03719 156 DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHL 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1044-1218 |
4.92e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1044 DNLNLNFYEGhITSLLGPNGAGKTTTISMLT-GLFGASAGTifvyGKDIKTDLHTVRKNmGVCMQHDVLFS------YLT 1116
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTTIIEALKyALTGELPPN----SKGGAHDPKLIREG-EVRAQVKLAFEnangkkYTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1117 TKEHLLLYGSIKVPHwtkkqlhEEVKRTLKDTglyshrhkrVGTLSGGMKRKLSISIAL------IGGSRVVILDEPSTG 1190
Cdd:cd03240 88 TRSLAILENVIFCHQ-------GESNWPLLDM---------RGRCSGGEKVLASLIIRLalaetfGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|.
gi 27881501 1191 VDPCSRR-SIWDVIS--KNKTARTIILSTHH 1218
Cdd:cd03240 152 LDEENIEeSLAEIIEerKSQKNFQLIVITHD 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1042-1235 |
6.18e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKT----DLHTVRKNMGVCMQ---------H 1108
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpyasldprQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYLTT-KEHLLLYGsikvphwtkKQLHEEVKRTLKDTGLY-SHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:PRK10261 419 TVGDSIMEPlRVHGLLPG---------KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1187 PSTGVDPCSRRSIWDVISKNKTARTI--ILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLG 540
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1954-2148 |
6.21e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghVDSHSSLvgycpqeDALDD---LVTV 2030
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKK-----INNHNAN-------EAINHgfaLVTE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2031 EEH---------LYFYARVHGIPE----------KDIKETVHKLLRRLHL-MPFKDRATSMCSYGTKRKLSTALALIGKP 2090
Cdd:PRK10982 331 ERRstgiyayldIGFNSLISNIRNyknkvglldnSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 2091 SILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGK 2148
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1957-2135 |
9.69e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTgDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDlVTVEEHLYF 2036
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFS-GTFRKNLDP 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 YARvhgIPEKDIKETVHKLLRRLHLMPFKDR-------ATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRH 2109
Cdd:TIGR01271 1315 YEQ---WSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQI 1391
|
170 180
....*....|....*....|....*....
gi 27881501 2110 LWKIISEEVQNkCSVILTSHSME---ECE 2135
Cdd:TIGR01271 1392 IRKTLKQSFSN-CTVILSEHRVEallECQ 1419
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1945-2130 |
9.85e-06 |
|
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: 48.09 E-value: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1945 YQLIHKKIiavNNISIGIPAGECFGLLGVNGAGKTTIFKmltgDIIPSSGNILIRNKTGSLGH-----VDSHSSLV---- 2015
Cdd:cd03238 4 SGANVHNL---QNLDVSIPLNVLVVVTGVSGSGKSTLVN----EGLYASGKARLISFLPKFSRnklifIDQLQFLIdvgl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 GYCPQEDALDDLVTVEehlyfyarvhgipekdiketvhklLRRLHLMPFkdratsmcsygtkrklstaLALIGKPSILLL 2095
Cdd:cd03238 77 GYLTLGQKLSTLSGGE------------------------LQRVKLASE-------------------LFSEPPGTLFIL 113
|
170 180 190
....*....|....*....|....*....|....*
gi 27881501 2096 DEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHS 2130
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1954-2097 |
1.15e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.57 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1954 AVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghVDSHSSlvgycpqeDALDDLVTV--- 2030
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP-----VTADNR--------EAYRQLFSAvfs 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2031 EEHLyfYARVHGIPEKDIKETVHKLLRRLHL---MPFKDRATSmcsygtKRKLSTA----LALI-----GKPsILLLDE 2097
Cdd:COG4615 414 DFHL--FDRLLGLDGEADPARARELLERLELdhkVSVEDGRFS------TTDLSQGqrkrLALLvalleDRP-ILVFDE 483
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1055-1242 |
1.37e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1055 ITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGK---DI--KTDLHTVRKNMGVCMQHDVLFsylttkehlllygsikv 1129
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAekGICLPPEKRRIGYVFQDARLF----------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1130 PHWT-KKQLHEEVKRTLKD-----TGLYSHRH--KRV-GTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIW 1200
Cdd:PRK11144 89 PHYKvRGNLRYGMAKSMVAqfdkiVALLGIEPllDRYpGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27881501 1201 DVISK-NKTARTIIL-STHHLDEAEVLSDRIAFLEQGGLRCCGS 1242
Cdd:PRK11144 169 PYLERlAREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1053-1192 |
1.51e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1053 GHITSLLGPNGAGKTT---TISMLTGLFGASAGTIFVY----GKDIKTDLhtvRKNMGVCMQHDVLFSYLTTKEHLLLYG 1125
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTllkTIASNTDGFHIGVEGVITYdgitPEEIKKHY---RGDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27881501 1126 SIKVPHWTKKQLHEEVKR------TLKDTGLYSHRHKRVGT-----LSGGMKRKLSISIALIGGSRVVILDEPSTGVD 1192
Cdd:TIGR00956 164 RCKTPQNRPDGVSREEYAkhiadvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1965-2150 |
1.82e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.24 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1965 GECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSSL----VGYCPQEDALDDLVTVEEHLYFYARV 2040
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2041 HGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKII-SEEVQ 2119
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfSLNRE 195
|
170 180 190
....*....|....*....|....*....|.
gi 27881501 2120 NKCSVILTSHSmEECEALCTRLAIMVNGKFQ 2150
Cdd:PRK10584 196 HGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1045-1256 |
2.26e-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: 49.94 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1045 NLNLNFYEGHITSLLGPNGAGKTttiSMLTGLF---GASAGTIFVYGKDI-KTDLHTVRKNMGVCMQHDVLFSYlTTKEH 1120
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKS---SLTLGLFrinESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1121 LLLYGSIKVPH-WTKKQL-HEEVKRTLKDTGLySHRHKRVG-TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRR 1197
Cdd:TIGR00957 1380 LDPFSQYSDEEvWWALELaHLKTFVSALPDKL-DHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27881501 1198 SIWDVISKNKTARTIILSTHHLDeaeVLSD--RIAFLEQGGLRCCGSPFYLKEAFGDGYHL 1256
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLN---TIMDytRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1957-2185 |
2.27e-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: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirnktgslghvdSHSSLVGYCPQEDALDDlVTVEEHLYF 2036
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMP-GTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 yarvhGIPEKDIKET----VHKLLRRLHLMPFKDRATSM-----CSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSK 2107
Cdd:TIGR01271 510 -----GLSYDEYRYTsvikACQLEEDIALFPEKDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2108 RHLW-KIISEEVQNKCSVILTShSMEECEAlCTRLAIMVNGKFQCIGS---LQHIKSRFGRGFTVKVHLKN------NKV 2177
Cdd:TIGR01271 585 KEIFeSCLCKLMSNKTRILVTS-KLEHLKK-ADKILLLHEGVCYFYGTfseLQAKRPDFSSLLLGLEAFDNfsaerrNSI 662
|
....*...
gi 27881501 2178 TMETLTKF 2185
Cdd:TIGR01271 663 LTETLRRV 670
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1033-1250 |
2.44e-05 |
|
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: 49.42 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1033 VTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGL--FGASAGTIfVYG---------------------- 1088
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRI-IYHvalcekcgyverpskvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1089 -----KDIKTDL--------HTVRKNMGVCMQHDvlfsylttkehLLLYGSIKVPHWTKKQLHE-------EVKRTLK-- 1146
Cdd:TIGR03269 85 cggtlEPEEVDFwnlsdklrRRIRKRIAIMLQRT-----------FALYGDDTVLDNVLEALEEigyegkeAVGRAVDli 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1147 DTGLYSHRHKRVG-TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAE 1223
Cdd:TIGR03269 154 EMVQLSHRITHIArDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*..
gi 27881501 1224 VLSDRIAFLEQGGLRCCGSPFYLKEAF 1250
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1955-2129 |
2.72e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1955 VNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPS-SGNILIRnktGSlghvdshsslVGYCPQEDALDDlVTVEEH 2033
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIR---GS----------VAYVPQVSWIFN-ATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2034 LYFYARVHgiPEKDIKET-VHKLLRRLHLMPFKDRAT-----SMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSK 2107
Cdd:PLN03232 699 ILFGSDFE--SERYWRAIdVTALQHDLDLLPGRDLTEigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180
....*....|....*....|...
gi 27881501 2108 RHLW-KIISEEVQNKCSVILTSH 2129
Cdd:PLN03232 777 HQVFdSCMKDELKGKTRVLVTNQ 799
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1873-2103 |
2.85e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.19 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1873 VALVSQGTMFFSlRL-----LINESLIK--KLRLFFRKFNSshVRETIDEDEDVRAERLrveSGAAEFDLVqlycltkTY 1945
Cdd:PRK13657 276 VAFVGFATLLIG-RLdqvvaFINQVFMAapKLEEFFEVEDA--VPDVRDPPGAIDLGRV---KGAVEFDDV-------SF 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1946 QLIHKKIiAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI-----RNKT-GSLGHVdshsslVGYCP 2019
Cdd:PRK13657 343 SYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdiRTVTrASLRRN------IAVVF 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2020 QEDALDDLvTVEEHLyfyaRVhGIPEKDIKEtVHKLLRRLHLMPFKDRAT-----------SMCSYGTKRKLSTALALIG 2088
Cdd:PRK13657 416 QDAGLFNR-SIEDNI----RV-GRPDATDEE-MRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALLK 488
|
250
....*....|....*
gi 27881501 2089 KPSILLLDEPSSGMD 2103
Cdd:PRK13657 489 DPPILILDEATSALD 503
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1961-2129 |
3.06e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1961 GIPA---GECFGLLGVNGAGKTTIFKMLTGDIIPssgnilirnktgSLGHVDSHSSlvgycpQEDALDDLVTVEEHLYFY 2037
Cdd:PRK13409 92 GLPIpkeGKVTGILGPNGIGKTTAVKILSGELIP------------NLGDYEEEPS------WDEVLKRFRGTELQNYFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2038 A-------------RVHGIPeKDIKETVHKLLR-------------RLHLMPFKDRATSMCSYGTKRKLSTALALIGKPS 2091
Cdd:PRK13409 154 KlyngeikvvhkpqYVDLIP-KVFKGKVRELLKkvdergkldevveRLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881501 2092 ILLLDEPSSGMDPKSKRHLWKIISEEVQNKcSVILTSH 2129
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAEGK-YVLVVEH 269
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
984-1220 |
4.33e-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: 49.14 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 984 EVKPEKSNGLMFTNIMMQNTNPSASPEYmfssniePEPKDLTVgvalHGVTKIY--GSKVAVDNLNLNFYEGHITSLLGP 1061
Cdd:TIGR01271 1185 EPRPSGGGGKYQLSTVLVIENPHAQKCW-------PSGGQMDV----QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGR 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1062 NGAGKTTTISMLTGLFgASAGTIFVYGKDIKT-DLHTVRKNMGVCMQHDVLFSYlTTKEHLLLYgsikvPHWTKkqlhEE 1140
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGVIPQKVFIFSG-TFRKNLDPY-----EQWSD----EE 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1141 VKRTLKDTGLYSHRHKRVG-----------TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTA 1209
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN 1402
|
250
....*....|.
gi 27881501 1210 RTIILSTHHLD 1220
Cdd:TIGR01271 1403 CTVILSEHRVE 1413
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1941-2103 |
4.54e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQlihkKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTGSLGHVDSHSS-----LV 2015
Cdd:PRK11701 12 LTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEaerrrLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2016 ----GYCPQeDALDDL---VT----VEEHLYFY-ARVHGipekDIKETVHKLLRRLHLMPFK-DRATSMCSYGTKRKLST 2082
Cdd:PRK11701 88 rtewGFVHQ-HPRDGLrmqVSaggnIGERLMAVgARHYG----DIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQI 162
|
170 180
....*....|....*....|.
gi 27881501 2083 ALALIGKPSILLLDEPSSGMD 2103
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2073-2133 |
4.76e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.34 E-value: 4.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27881501 2073 SYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKII-SEEVQNKCSVILTSHSMEE 2133
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqSLRLRSELTMVIVSHNLHQ 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1948-2153 |
5.70e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1948 IHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI---RNKTGSLGHVDSHSSLVGYCPQED-- 2022
Cdd:PRK10261 333 VTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFngqRIDTLSPGKLQALRRDIQFIFQDPya 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2023 ALDDLVTVEEHLYFYARVHGI-PEKDIKETVHKLLRRLHLMPFKD-RATSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2100
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2101 GMDPKSKRHLWKIISeEVQNKCSV--ILTSHSMEECEALCTRLAIMVNGKFQCIG 2153
Cdd:PRK10261 493 ALDVSIRGQIINLLL-DLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1957-2127 |
5.85e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIP-SSGNILIRNKtgslghvdshsslVGYCPQEDALDDlVTVEEHLY 2035
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT-------------VAYVPQVSWIFN-ATVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2036 FyarvhGIP------EKDIKetVHKLLRRLHLMPFKD------RATSMcSYGTKRKLSTALALIGKPSILLLDEPSSGMD 2103
Cdd:PLN03130 701 F-----GSPfdperyERAID--VTALQHDLDLLPGGDlteigeRGVNI-SGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180
....*....|....*....|....*
gi 27881501 2104 PKSKRHLW-KIISEEVQNKCSVILT 2127
Cdd:PLN03130 773 AHVGRQVFdKCIKDELRGKTRVLVT 797
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1045-1220 |
6.30e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1045 NLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDI----KTDLHTVRKNMGVCMQhdvlfsyLTTKEH 1120
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniaKPYCTYIGHNLGLKLE-------MTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1121 LLLYGSIkvphwtkKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIW 1200
Cdd:PRK13541 91 LKFWSEI-------YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170 180
....*....|....*....|
gi 27881501 1201 DVISKNKTARTIILSTHHLD 1220
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSHLE 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1042-1235 |
1.21e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTdlHTV--------------RKNMGVCMQ 1107
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN--HNAneainhgfalvteeRRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1108 HDVLFSYLTT--KEHLLLYGSIKvphwtKKQLHEEVKRTLKDTGLYSHRHK-RVGTLSGGMKRKLSISIALIGGSRVVIL 1184
Cdd:PRK10982 341 LDIGFNSLISniRNYKNKVGLLD-----NSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27881501 1185 DEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1052-1188 |
1.21e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1052 EGHITSLLGPNGAGKTTTISMLTGL----FGAsagtifvYGKDIKTD--LHTVRKNmgvcmqhdVLFSYLTTkehllLY- 1124
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGElkpnLGD-------YDEEPSWDevLKRFRGT--------ELQDYFKK-----LAn 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1125 GSIKVPHwtKKQLHEEVKRTLKDT---------------------GLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:COG1245 158 GEIKVAH--KPQYVDLIPKVFKGTvrellekvdergkldelaeklGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
....*
gi 27881501 1184 LDEPS 1188
Cdd:COG1245 236 FDEPS 240
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1945-2129 |
1.85e-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: 44.27 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1945 YQLIHKKIIAVNNIsIGIPAGECFGLLGVNGAGKTTIFKMltgdiipssgnilirnktgslghvdshsslVGYcpqedal 2024
Cdd:cd03227 2 IVLGRFPSYFVPND-VTFGEGSLTIITGPNGSGKSTILDA------------------------------IGL------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2025 ddlvtveehLYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRatsmCSYGTKRKLSTALALIG---KPSIL-LLDEPSS 2100
Cdd:cd03227 44 ---------ALGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ----LSGGEKELSALALILALaslKPRPLyILDEIDR 110
|
170 180
....*....|....*....|....*....
gi 27881501 2101 GMDPKSKRHLWKIISEEVQNKCSVILTSH 2129
Cdd:cd03227 111 GLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1957-2156 |
1.93e-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: 45.62 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTgDIIPSSGNILIRNKTGSLGHVDSHSSLVGYCPQEDALDDlVTVEEHLYF 2036
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFS-GTFRKNLDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 YARVHgipEKDIKETVHKLLRRLHLMPFKDR-------ATSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRH 2109
Cdd:cd03289 100 YGKWS---DEEIWKVAEEVGLKSVIEQFPGQldfvlvdGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27881501 2110 LWKIISEEVQNkCSVILTSHSMeecEAL--CTRLAIMVNGKFQCIGSLQ 2156
Cdd:cd03289 177 IRKTLKQAFAD-CTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQ 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1947-2152 |
2.03e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1947 LIHKKIIAVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTG--------------DIIPSSGNILIRNktgSLGHVDSHS 2012
Cdd:PRK09700 271 VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkraggeirlngkDISPRSPLDAVKK---GMAYITESR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2013 SLVGYCP-----QEDALDDLVTVEEHLYFYARVHGIPEKDIKETVHKLLRrLHLMPFKDRATSMcSYGTKRKLSTALALI 2087
Cdd:PRK09700 348 RDNGFFPnfsiaQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLA-LKCHSVNQNITEL-SGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27881501 2088 GKPSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGKFQCI 2152
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1056-1229 |
3.90e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1056 TSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIKTDL---------------------------------HTVRKNM 1102
Cdd:PTZ00265 1197 TAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMtneqdyqgdeeqnvgmknvnefsltkeggsgedSTVFKNS 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1103 GVCMQHDV------------LFSyLTTKEHLLLYGSI--KVPHWTKKQLHEEVKRTLK----DTGLYSHRHK---RVG-- 1159
Cdd:PTZ00265 1277 GKILLDGVdicdynlkdlrnLFS-IVSQEPMLFNMSIyeNIKFGKEDATREDVKRACKfaaiDEFIESLPNKydtNVGpy 1355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 1160 --TLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEvLSDRI 1229
Cdd:PTZ00265 1356 gkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIK-RSDKI 1428
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1030-1076 |
4.30e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 4.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 27881501 1030 LHGVTKIYGS-KVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGL 1076
Cdd:PRK11819 9 MNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 56
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1007-1091 |
4.75e-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: 45.17 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1007 ASPEYMFSSNIEPEPKDLTVGVALHGVTKIY-----GSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASA 1081
Cdd:COG4615 307 AAAEPAAADAAAPPAPADFQTLELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPES 386
|
90
....*....|
gi 27881501 1082 GTIFVYGKDI 1091
Cdd:COG4615 387 GEILLDGQPV 396
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1920-1996 |
5.18e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1920 RAERLRVE------------SGAAEFDLVQLycltkTYQLIHKKIiaVNNISIGIPAGECFGLLGVNGAGKTTIFKMLTG 1987
Cdd:PRK11147 295 RSERREVMgtakmqveeasrSGKIVFEMENV-----NYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG 367
|
....*....
gi 27881501 1988 DIIPSSGNI 1996
Cdd:PRK11147 368 QLQADSGRI 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1962-2166 |
5.48e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1962 IPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKTgslghvdshsslVGYCPQEDALddlvtveehlyfyarvh 2041
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT------------PVYKPQYIDL----------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2042 gipekdiketvhkllrrlhlmpfkdratsmcSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWKIISE-EVQN 2120
Cdd:cd03222 73 -------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlSEEG 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27881501 2121 KCSVILTSHSMEECEALCTRLAIM-----VNGKFQCIGSLQHIKSRFGRGF 2166
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFegepgVYGIASQPKGTREGINRFLRGY 172
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2021-2132 |
6.41e-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: 44.61 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2021 EDALDDLVT-VEEHLYFYARVHGIPEKDIKETVHKLLRRLHLMpFKDRAT---SMCSYGTKRKLSTALALI-------GK 2089
Cdd:COG3593 109 KEALKALNElLSEYLKELLDGLDLELELSLDELEDLLKSLSLR-IEDGKElplDRLGSGFQRLILLALLSAlaelkraPA 187
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 27881501 2090 PSILLLDEPSSGMDPKSKRHLWKIISEEVQNKCSVILTSHSME 2132
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1941-2110 |
8.72e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1941 LTKTYQLiHKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKML-------TGDIIPSSGnilIRnktgslghvdshss 2013
Cdd:PRK11819 12 VSKVVPP-KKQIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkefEGEARPAPG---IK-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2014 lVGYCPQEDALDDLVTVEEHL---------------YFYARvHGIPEKDIKETV---------------HKLLRRLHL-M 2062
Cdd:PRK11819 72 -VGYLPQEPQLDPEKTVRENVeegvaevkaaldrfnEIYAA-YAEPDADFDALAaeqgelqeiidaadaWDLDSQLEIaM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27881501 2063 -----PFKDRATSMCSYGTKRKLstALA--LIGKPSILLLDEPSSGMDPKS----KRHL 2110
Cdd:PRK11819 150 dalrcPPWDAKVTKLSGGERRRV--ALCrlLLEKPDMLLLDEPTNHLDAESvawlEQFL 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1030-1076 |
1.03e-03 |
|
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: 44.16 E-value: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 27881501 1030 LHGVTKIYGSKVAV-DNLNLNFYEGHITSLLGPNGAGKTTTISMLTGL 1076
Cdd:TIGR03719 7 MNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV 54
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1042-1238 |
1.04e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIfvygkDIKTDLHTVRKNMGVCMQhdvlfsyLTTKEHL 1121
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1122 LLYGSIKvpHWTKKQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP-STGVDPCSRRSIW 1200
Cdd:PRK13545 107 ELKGLMM--GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVGDQTFTKKCLD 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 27881501 1201 DVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLR 1238
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVK 222
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1957-2128 |
1.05e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 43.31 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1957 NISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNIlirnktgslghvdSHSSLVGYCPQEDALDDlVTVEEHLYF 2036
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMP-GTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2037 ------YARVHGIPEKDIKETVHKLlrrlhlmPFKDRATS-----MCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPK 2105
Cdd:cd03291 121 gvsydeYRYKSVVKACQLEEDITKF-------PEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180
....*....|....*....|....
gi 27881501 2106 SKRHLW-KIISEEVQNKCSVILTS 2128
Cdd:cd03291 194 TEKEIFeSCVCKLMANKTRILVTS 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1027-1103 |
1.23e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.68 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1027 GVALHGVTKIYGSKV-AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTIFVYGKDIkTDL---------- 1095
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELepadrdiamv 81
|
90
....*....|....*..
gi 27881501 1096 --------H-TVRKNMG 1103
Cdd:PRK11650 82 fqnyalypHmSVRENMA 98
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1949-2103 |
1.91e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.51 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1949 HKKIIavNNISIGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPS--------SGNILIRNKtgSLGHVDSH--SSLVGYC 2018
Cdd:PRK13547 13 HRAIL--RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGE--PLAAIDAPrlARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 2019 PQED------ALDDLVTVEEhlYFYARVHGIPEKDIKETVHKLLRRLHLMPFKDRATSMCSYGTKRKLSTALAL------ 2086
Cdd:PRK13547 89 PQAAqpafafSAREIVLLGR--YPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180
....*....|....*....|
gi 27881501 2087 ---IGKPSILLLDEPSSGMD 2103
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALD 186
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2073-2132 |
2.55e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.34 E-value: 2.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27881501 2073 SYGTKRKLSTALALIG---KPSILLLDEPSSGMDPKSKRHLWKIISEEVQNK-CSVILTSHSME 2132
Cdd:COG1106 204 SDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNnAQLIFTTHSTE 267
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1042-1232 |
3.00e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1042 AVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGL----FGASAGTIFVYGKD-IKTDLHTVRKNMG--VCMQHDVLFSY 1114
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDlLRLSPRERRKLVGhnVSMIFQEPQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1115 LTTKEHLLLYGSIKVPHWTKK-----QLHEEVKRT---LKDTGLYSHR---HKRVGTLSGGMKRKLSISIALIGGSRVVI 1183
Cdd:PRK15093 102 LDPSERVGRQLMQNIPGWTYKgrwwqRFGWRKRRAielLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27881501 1184 LDEPSTGVDPCSRRSIWDVISK----NKTarTIILSTHHLDEAEVLSDRIAFL 1232
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRlnqnNNT--TILLISHDLQMLSQWADKINVL 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1052-1208 |
3.23e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1052 EGHITSLLGPNGAGKTTTISMLTGL----FG-------------ASAGTIF------VYGKDIKtdlhTVRKNMGVcmqh 1108
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGElipnLGdyeeepswdevlkRFRGTELqnyfkkLYNGEIK----VVHKPQYV---- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881501 1109 DVLFSYL--TTKEHLllygsIKVphwTKKQLHEEVKRTLkdtGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDE 1186
Cdd:PRK13409 170 DLIPKVFkgKVRELL-----KKV---DERGKLDEVVERL---GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180
....*....|....*....|....*
gi 27881501 1187 PSTGVDPCSRRSIWDVI---SKNKT 1208
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIrelAEGKY 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1161-1235 |
3.83e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 3.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1161 LSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIAFLEQG 1235
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1028-1084 |
9.07e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 9.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 27881501 1028 VALHGVTKIYGSKVAVDNLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGASAGTI 1084
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| |
