|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-2291 |
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: 1405.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 5 RRWLLIKMtfdNTTRVLFELIWPLFLFLILMWVRSRGLTVYYPACYNDPKQLGSSGFLPALQTYLCRLNNTCWNYPLSTD 84
Cdd:TIGR01257 13 KNWTLRKR---QKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSPTPGE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 85 DtqiSGFIEMISNASEA-----LSLLLENKDTGPIIFQLYQLIRNTSSNVDVLNTYWDgyisvNLSTQSFNYSKSISNQT 159
Cdd:TIGR01257 90 S---PGIVSNYNNSILArvyrdFQELLMDAPESQHLGQVWAELRTLSQFMDTLRTHPE-----RIAGRGIRIRDILKDEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 160 LNTIFtnpisltnLHQKWLIKDNSTQTKSNSEVMIEillQFSLPIPpvryqnETDVKNAFCTNNQFNKtFQLKPAQQIAR 239
Cdd:TIGR01257 162 ALTLF--------LMKNIGLSDSVVYLLVNSQVRPE---QFAYGVP------DLELKDIACSEALLER-FIIFSQRRGAQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 240 dTAKNELCSLSDSDLFNFLITLKTDLDgiymkeklsnistpiliqnvygMHAVWQNLTVLLNSlnmtlfpseNQNNISFS 319
Cdd:TIGR01257 224 -TVRDALCSLSQGTLQWIEDTLYANVD----------------------FFKLFHVLPTLLDS---------RSQGINLR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 320 FAGicGGREDLSRQFQvspptnsvldesqeinetsvkrlkrsktkDNIKRSSVKAL---ASPSLQHLLESDLTKYSKML- 395
Cdd:TIGR01257 272 SWG--GILSDMSPRIQ-----------------------------EFIHRPSVQDLlwvTRPLLQNGGPETFTQLMGILs 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 396 -IVSSKAETSNSTNTtssDIDWIDfASNLMYFNDTELCEESFIYGSGDiqqiqiiNRTCRCVYMDQILNSISEIRFLIRL 474
Cdd:TIGR01257 321 dLLCGYPEGGGSRVF---SFNWYE-DNNYKAFLGIDSTRKDPIYSYDK-------RTTSFCNALIQSLESNPLTKIAWRA 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 475 IRPLLYGKILYYPNNPQYNQIIKRMNAIFESLDEFIILMKNIQKA------IYPSLTVLNRICSRL--PL---FGN---- 539
Cdd:TIGR01257 390 AKPLLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVgpqiwyFFDKSTQMTMIRDTLqnPTvkdFINrqlg 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 540 ---INCSQIQSYQYMAA---------------IFTV-------FQEFLSCTERNRFQPVESSADLVTKALNLSFTYSFLA 594
Cdd:TIGR01257 470 eegITAEAVLNFLYNGPrekqaddmtnfdwrdIFNItdrflrlANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWA 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 595 GIEFlNDIV--DDELPKHIKYKIRMPLDSVDSTFRQQNRYFSFKPRTDAPLSTKYFSFGFIYLMNSLERAFISIQTNTSL 672
Cdd:TIGR01257 550 GVVF-PDMYpwTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEP 628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 673 GYGVKTQQYPYPCYVNDKFINAVSRMLPLFMVLGWIFTVSMNVKDIVHEKEKRLKEIMKIMGLYDTVHWFSWFIWCSFIM 752
Cdd:TIGR01257 629 PVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIM 708
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 753 MITAIFLVLIIKYGNITRFSNFLILLIFFLCFTFATITQCFLMSVFFNRANLAACGAGILFFLLYLPYTVLLNYSD-VTL 831
Cdd:TIGR01257 709 SMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDrMTA 788
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 832 RWHKIISCLSStVAFGIGCDYIAKWEERAKGIQWDNINKGTRPADNFSFLYCMIMMLIDSIIYMFFTWYIENVFPGEFGI 911
Cdd:TIGR01257 789 DLKTAVSLLSP-VAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGT 867
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 912 PKPWYFPFTKTYWFGYDVNKIRKRTEylinLEKNQ--SENTNELDNRVKQRSASIESYSDGEV-GVEIINLCKYYN--NK 986
Cdd:TIGR01257 868 PLPWYFLLQESYWLGGEGCSTREERA----LEKTEplTEEMEDPEHPEGINDSFFERELPGLVpGVCVKNLVKIFEpsGR 943
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQHNVLFDLLTVREH 1066
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1067 LEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDL 1146
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1147 LLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLKRKYAEGYNLIVeftsvsdeeelkTHSDENVMNNNS 1226
Cdd:TIGR01257 1104 LLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTL------------VRKMKNIQSQRG 1171
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1227 TIDDNASklVNSSNIELRTISRNNK-------SGQFEKLTDFLKSFISDISVKEEHGDQITYVILDDEAHTRFFPEMLKQ 1299
Cdd:TIGR01257 1172 GCEGTCS--CTSKGFSTRCPARVDEitpeqvlDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRE 1249
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1300 LDKRKELFRIKNYGLSNSNLEQVFLNVADEAKCVEDYERSSVWKKLALYIKK-CFGcktlssnvlVSEENNEQEIVSDTC 1378
Cdd:TIGR01257 1250 LEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKRENANLRHpCSG---------PTEKAGQTPQASHTC 1320
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1379 LSDEWGVYAKDR------------HTGLSLIGIQFLALIIKRFHRTKRNTKGFIAELILPIIFVLLAMLVATLKPNQQDS 1446
Cdd:TIGR01257 1321 SPGQPAAHPEGQpppepedpgvplNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEY 1400
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1447 PPLILHPWYwYTPNYFFQSLAKDASNVSQSTLQTFYKSPSIGTRCMNDTMLdrQKYPC-NASAVGYTYVQPSsqIMAALN 1525
Cdd:TIGR01257 1401 PALTLHPWM-YGQQYTFFSMDEPNSEHLEVLADVLLNKPGFGNRCLKEEWL--PEYPCgNSTPWKTPSVSPN--ITHLFQ 1475
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1526 AVNYNQTKISPECDCDKK-----MQTCPVGASG-PPPSYDQIETkDIVKHLTDYNITDWIIKT-------QYNDEYVM-- 1590
Cdd:TIGR01257 1476 KQKWTAAHPSPSCRCSTRekltmLPECPEGAGGlPPPQRTQRST-EILQDLTDRNISDFLVKTypalirsSLKSKFWVne 1554
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1591 KRFGGIEFLSK--ALEENGINTIN-TSLINQLANMNNIVVNEEKIAEL--FRIH---QPQVAVWYDNMGWPSSLAYLNIF 1662
Cdd:TIGR01257 1555 QRYGGISIGGKlpAIPITGEALVGfLSDLGQMMNVSGGPVTREASKEMpdFLKHletEDNIKVWFNNKGWHALVSFLNVA 1634
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1663 NNALLRSLLPSS-DVKDYGITAIQHPLPQTQIEIDLELQSRAYLELFTAICVIFALAFIPASFLVFLIDERATTSKHLQF 1741
Cdd:TIGR01257 1635 HNAILRASLPKDrDPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQF 1714
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1742 VSGVKGIIYWVSNYAWDIVNFTVSLVFCVIIFLAFNVQAYVHKENLLCLILLLFLYGFATIPLMYPFSYLFKTPSTGFVL 1821
Cdd:TIGR01257 1715 ISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVA 1794
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1822 ISCINIFLGLITTISTFTLENISDEPDLQKINVVLMKVFLIFPHYCLGRGLFDMSKLHAADEIISKYNPYYQKkSPFEFN 1901
Cdd:TIGR01257 1795 LSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSA-NPFQWD 1873
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1902 QVGRNLMALAIEGIIFFIFALLIQYRFFIAdRIRRKPPKIVSIEEDDDVAAERQRLYNDPNNTshDVLRMTDLIKVYGwq 1981
Cdd:TIGR01257 1874 LIGKNLVAMAVEGVVYFLLTLLIQHHFFLS-RWIAEPAKEPIFDEDDDVAEERQRIISGGNKT--DILRLNELTKVYS-- 1948
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1982 fGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNLL 2061
Cdd:TIGR01257 1949 -GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLL 2027
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:TIGR01257 2028 TGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2142 FLWDCILTLTRkEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGDGYTIILRTNA-----VADIDTLT 2216
Cdd:TIGR01257 2108 MLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSpkddlLPDLNPVE 2186
|
2330 2340 2350 2360 2370 2380 2390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2217 QYIIEHLPEATLKEKHNKVIHFRVTATiKLYEMFSVLERARVELspAIEDYTVTQVTLDDVFVSFAKYQDVEKDF 2291
Cdd:TIGR01257 2187 QFFQGNFPGSVQRERHYNMLQFQVSSS-SLARIFQLLISHKDSL--LIEEYSVTQTTLDQVFVNFAKQQTETYDL 2258
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1969-2193 |
2.10e-105 |
|
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: 336.01 E-value: 2.10e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNL 2048
Cdd:cd03263 1 LQIRNLTKTYK---KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLtrKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLK 2193
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
974-1191 |
2.59e-102 |
|
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: 327.15 E-value: 2.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNN--KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFT 1051
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1132 TAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLK 1191
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
974-1196 |
2.50e-83 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 273.48 E-value: 2.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQ 1053
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1134 GVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLKRKYAE 1196
Cdd:COG1131 161 GLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLE 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1969-2196 |
1.16e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 245.74 E-value: 1.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNL 2048
Cdd:COG1131 1 IEVRGLTKRYG-----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKF 2196
Cdd:COG1131 156 DEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
975-1186 |
8.23e-67 |
|
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: 226.66 E-value: 8.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQH 1054
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1135 VDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG4555 163 LDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
974-1181 |
9.39e-65 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 217.65 E-value: 9.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQ 1053
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEffarlkgaadetidieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 1134 GVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03230 125 GLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1973-2193 |
1.14e-61 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 210.69 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1973 DLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCP 2052
Cdd:cd03265 5 NLVKKYG-----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2053 QFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPT 2132
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2133 TGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLK 2193
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
974-1191 |
1.17e-61 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 210.69 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQ 1053
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1134 GVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLK 1191
Cdd:cd03265 161 GLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
981-1193 |
1.34e-61 |
|
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: 213.79 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 981 KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQHNVLFDL 1060
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 LTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFAR 1140
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1141 RSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLKRK 1193
Cdd:TIGR01188 161 RAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRR 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
974-1185 |
1.97e-54 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 189.71 E-value: 1.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFyQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQ 1053
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1134 GVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1969-2183 |
1.50e-51 |
|
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: 179.90 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNL 2048
Cdd:cd03230 1 IEVRNLSKRYG-----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYfyarlrgikqqnipyisgcllkrlgltlwadrpvrqYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEF 2183
Cdd:cd03230 120 DEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1981-2198 |
1.59e-51 |
|
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: 182.75 E-value: 1.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKKFtAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNL 2060
Cdd:COG4555 10 KYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 LTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAK 2140
Cdd:COG4555 89 LTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2141 RFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGD 2198
Cdd:COG4555 169 RLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
974-1186 |
6.75e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 171.75 E-value: 6.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLC-KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL-TDIKKIRQNIGFT 1051
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQH--NVLFDlLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:COG1122 81 FQNpdDQLFA-PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
974-1182 |
1.09e-46 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 167.39 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwDILTDIKKIRQNIGFTPQ 1053
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADEtidiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1134 GVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELR 1182
Cdd:cd03268 156 GLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
974-1214 |
4.24e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 169.13 E-value: 4.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwDILTDikKIRQNIGFTPQ 1053
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDP--EDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1134 GVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLKRKYAEgYNLIVEFTsvSDEEE 1212
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR-NTLRLEAD--GDAGW 235
|
..
gi 2041616051 1213 LK 1214
Cdd:COG4152 236 LR 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
978-1180 |
1.15e-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: 164.56 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNN--KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL-TDIKKIRQNIGFTPQH 1054
Cdd:cd03225 4 NLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 -NVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03225 84 pDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2041616051 1134 GVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:cd03225 164 GLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
974-1186 |
2.74e-44 |
|
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: 161.52 E-value: 2.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL----TDIKKIRQNIG 1049
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERM-LDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVIL 1128
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1129 DEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
974-1185 |
4.30e-44 |
|
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: 160.23 E-value: 4.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNK----LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIG 1049
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
969-1186 |
1.02e-42 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 157.06 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 969 DGEVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DIKKI 1044
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1045 RQNIGFTPQHNVLFDLLTVREHLEFFARLKGAADETidiEIERM----LDDLMLTNKRDNYSTELSGGMKRKLSIAIAFC 1120
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEA---EIRELvlekLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1121 ANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
974-1185 |
2.57e-42 |
|
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: 154.75 E-value: 2.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIkkiRQNIGFTPQ 1053
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA---RNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1134 GVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
975-1180 |
7.66e-42 |
|
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: 151.63 E-value: 7.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQ 1053
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 hnvlfdlltvrehleffarlkgaadetidieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2041616051 1134 GVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:cd00267 110 GLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
974-1173 |
1.42e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 152.63 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQ 1053
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADEtiDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 1134 GVDPFARRSIWDLLLKY-KQGRTIIISTHfmDEADLLGDRI 1173
Cdd:COG4133 161 ALDAAGVALLAELIAAHlARGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
974-1178 |
2.90e-41 |
|
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: 152.24 E-value: 2.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY----NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKKIRQNIG 1049
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLK--YKQGRTIIISTHFMDEADLLGDRIAIISS 1178
Cdd:cd03293 157 EPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1961-2181 |
1.10e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 154.60 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1961 PNNTSHDVLRMTDLIKVYGwqfGKkfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKD 2040
Cdd:PRK13536 34 PGSMSTVAIDLAGVSKSYG---DK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2041 IDGVHRNLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALI 2120
Cdd:PRK13536 109 ARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2121 GNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKeHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
974-1180 |
1.91e-40 |
|
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: 148.10 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT---DIKKIRQNIGF 1050
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQHNVLFDLLTVREHLEFfarlkgaadetidieiermlddlmltnkrdnystELSGGMKRKLSIAIAFCANSKTVILDE 1130
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1131 PTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
972-1203 |
2.13e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 153.83 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 972 VGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFT 1051
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1132 TAGVDPFARRSIWDLLLK-YKQGRTIIISTHFMDEADLLGDRIAIISSGelrcvgtsmflkRKYAEG--YNLIVE 1203
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAG------------RKIAEGrpHALIDE 262
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
968-1179 |
2.68e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 151.01 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 968 SDGEVGVEIINLCKYYNNK----LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKK 1043
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1044 IRQNIGFTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANS 1123
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1124 KTVILDEPTAGVDPFARRSIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
978-1187 |
3.41e-40 |
|
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: 149.62 E-value: 3.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDI---KKIRQNIGFTPQH 1054
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLpmhKRARLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1135 VDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGELRCVGTS 1187
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
974-1185 |
3.66e-40 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 148.82 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFTPQ 1053
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1134 GVDPFARRSIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1981-2181 |
6.35e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 151.50 E-value: 6.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNL 2060
Cdd:PRK13537 16 RYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 LTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAK 2140
Cdd:PRK13537 95 FTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 2141 RFLWDCILTLTRKeHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK13537 175 HLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1969-2182 |
1.16e-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: 147.51 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNL 2048
Cdd:cd03266 2 ITADALTKRFR-DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
974-1197 |
1.30e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 150.34 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQ 1053
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1134 GVDPFARRSIWDLLLK-YKQGRTIIISTHFMDEADLLGDRIAIISSGelrcvgtsmflkRKYAEG 1197
Cdd:PRK13537 168 GLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEG------------RKIAEG 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
989-1133 |
1.37e-39 |
|
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: 144.71 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKI-RQNIGFTPQHNVLFDLLTVREHL 1067
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1068 EFFARLKGAADETIDIEIERMLDDLMLTNKRD----NYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
974-1181 |
3.62e-39 |
|
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: 146.10 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNN----KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKI--- 1044
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIskLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1045 RQNIGFTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSK 1124
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1125 TVILDEPTAGVDPFARRSIWDLLLKY--KQGRTIIISTHFMDEADlLGDRIAIISSGEL 1181
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
974-1186 |
4.47e-39 |
|
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: 147.11 E-value: 4.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTP 1052
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDLLTVRE--------HLEFFARLkGAADETIdieIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSK 1124
Cdd:COG1120 82 QEPPAPFGLTVRElvalgrypHLGLFGRP-SAEDREA---VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1125 TVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
975-1182 |
4.93e-39 |
|
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: 146.00 E-value: 4.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDG--WDiltdiKKIRQNIGFTP 1052
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGhpWT-----RKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDLLTVREHLEFFARLKGAADETIDieieRMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPT 1132
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLPDSRID----EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1133 AGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELR 1182
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
974-1186 |
6.41e-39 |
|
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: 146.29 E-value: 6.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNN-KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL-TDIKKIRQNIGFT 1051
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLML--TNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1969-2187 |
6.65e-39 |
|
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: 145.03 E-value: 6.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqFGKKFTAVN-NICAGVkqgecFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRN 2047
Cdd:cd03264 1 LQLENLTKRYG--KKRALDGVSlTLGPGM-----YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2048 LGYCPQ-FDALDNlLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVI 2126
Cdd:cd03264 74 IGYLPQeFGVYPN-FTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2127 FMDEPTTGMDVRAK-RFlwdciLTLTRK--EHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFG 2187
Cdd:cd03264 153 IVDEPTAGLDPEERiRF-----RNLLSElgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
978-1187 |
5.53e-38 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 143.57 E-value: 5.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDI---KKIRQNIGFTPQH 1054
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLpmhERARLGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLTVREHLEFFARLKGAADET-IDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:TIGR04406 85 ASIFRKLTVEENIMAVLEIRKDLDRAeREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1134 GVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGELRCVGTS 1187
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1981-2279 |
6.56e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 145.25 E-value: 6.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVL---KDIDGVHRN-LGYCPQFDA 2056
Cdd:COG4152 10 RFGDK-TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG-------EVLwdgEPLDPEDRRrIGYLPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2057 LDNLLTAREHLYFYARLRGIK----QQNIPYisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPT 2132
Cdd:COG4152 82 LYPKMKVGEQLVYLARLKGLSkaeaKRRADE----WLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2133 TGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGdGYTIILRTNAVADi 2212
Cdd:COG4152 158 SGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEADGDAG- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 2213 dtltqyIIEHLPEATLKEKHNKVIHFRVTATIKLYEmfsVLERArVELSPaIEDYTVTQVTLDDVFV 2279
Cdd:COG4152 235 ------WLRALPGVTVVEEDGDGAELKLEDGADAQE---LLRAL-LARGP-VREFEEVRPSLNEIFI 290
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1969-2178 |
1.47e-37 |
|
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: 141.20 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVhRNL 2048
Cdd:cd03268 1 LKTNDLTKTYG-----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL-RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYIsgclLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIM 2178
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGII 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1982-2182 |
2.59e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 140.49 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1982 FGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlkDIDGVHRnLGYCPQFDALDNLL 2061
Cdd:cd03269 10 FGRV-TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL--DIAARNR-IGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 2142 FLWDCILTLTRKEhKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03269 166 LLKDVIRELARAG-KTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
974-1181 |
3.03e-37 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 141.18 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY----NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DIKKIR 1045
Cdd:cd03258 2 IELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKT 1125
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1126 VILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1988-2296 |
6.50e-37 |
|
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: 154.02 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNLLTAREHL 2067
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2068 YFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDci 2147
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD-- 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2148 LTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGDGY--TIILRTNAV---------------- 2209
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFylTLVRKMKNIqsqrggcegtcsctsk 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2210 --------------------ADIDTLTQYIIEHLPEATLKE---------KHNKVIHFRVTATiklyeMFSVLERARVEL 2260
Cdd:TIGR01257 1183 gfstrcparvdeitpeqvldGDVNELMDLVYHHVPEAKLVEcigqeliflLPNKNFKQRAYAS-----LFRELEETLADL 1257
|
330 340 350
....*....|....*....|....*....|....*.
gi 2041616051 2261 spAIEDYTVTQVTLDDVFVSFAKYQDVEKDFLNESQ 2296
Cdd:TIGR01257 1258 --GLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQ 1291
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
974-1181 |
9.02e-37 |
|
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: 139.62 E-value: 9.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIP-----PTSGTAYIDGWDILT---DIKKIR 1045
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDLlTVREHLEFFARLKGAAD-ETIDIEIERMLDDLMLTN--KRDNYSTELSGGMKRKLSIAIAFCAN 1122
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1123 SKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
975-1187 |
3.71e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 138.24 E-value: 3.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDI---KKIRQNIGFT 1051
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLpmhKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1132 TAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEAdlLG--DRIAIISSGELRCVGTS 1187
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKErGIGVLITDHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1968-2163 |
6.70e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.45 E-value: 6.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGWQfgkkfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRN 2047
Cdd:COG4133 2 MLEAENLSCRRGER-----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2048 LGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIF 2127
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 2041616051 2128 MDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSH 2163
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTH 189
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1004-1186 |
9.90e-36 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 148.73 E-value: 9.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1004 FLGRNGAGKSTTWSILTGLIPPTSGTAY-----IDGWDILTdikkiRQNIGFTPQHNVLFDLLTVREHLEFFARLKGAAD 1078
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT-----RRRVGYMSQAFSLYGELTVRQNLELHARLFHLPA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1079 ETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTI 1156
Cdd:NF033858 372 AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLieLSREDGVTI 451
|
170 180 190
....*....|....*....|....*....|
gi 2041616051 1157 IISTHFMDEAdLLGDRIAIISSGELRCVGT 1186
Cdd:NF033858 452 FISTHFMNEA-ERCDRISLMHAGRVLASDT 480
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
975-1176 |
1.69e-35 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 135.35 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKKIRQNIGFTPQH 1054
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 -NVLFDL-LTVRE--------HLEFFARLKGAADEtidiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSK 1124
Cdd:cd03235 77 rSIDRDFpISVRDvvlmglygHKGLFRRLSKADKA----KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1125 TVILDEPTAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAII 1176
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
974-1186 |
3.45e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKKIRQNIGFTPQ 1053
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HnVLFDL---LTVRE--------HLEFFARLKGAADEtidiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCAN 1122
Cdd:COG1121 83 R-AEVDWdfpITVRDvvlmgrygRRGLFRRPSRADRE----AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1123 SKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIIsSGELRCVGT 1186
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
975-1186 |
1.65e-34 |
|
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: 133.33 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIK---KIRQNIGFT 1051
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPpheIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLE-----------FFARLKGAADETIDiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFC 1120
Cdd:cd03219 81 FQIPRLFPELTVLENVMvaaqartgsglLLARARREEREARE-RAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1121 ANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
975-1187 |
2.17e-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: 132.56 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIRQNIGFTP 1052
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDLLTVREHLE--FFARLKGAADETidieIERMLdDL--MLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVIL 1128
Cdd:cd03224 82 EGRRIFPELTVEENLLlgAYARRRAKRKAR----LERVY-ELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1129 DEPTAGVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTS 1187
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
974-1181 |
2.27e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.47 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY----NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIK--KIR 1045
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIssLSERElaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 -QNIGFTPQ-HNvLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFcANS 1123
Cdd:COG1136 85 rRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL-VNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1124 KTVIL-DEPTAGVDPFARRSIWDLLLKY--KQGRTIIISTHfmdEADLLG--DRIAIISSGEL 1181
Cdd:COG1136 163 PKLILaDEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTH---DPELAAraDRVIRLRDGRI 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
975-1181 |
2.36e-34 |
|
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: 132.00 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLC-KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIltDIKKIRQNIGFTPQ 1053
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 ---HNVLFDllTVREHLEFFARLKGAADETIdieiERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDE 1130
Cdd:cd03226 79 dvdYQLFTD--SVREELLLGLKELDAGNEQA----ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1131 PTAGVDPFARRSIWDLLLK-YKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03226 153 PTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
974-1180 |
3.82e-34 |
|
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: 129.81 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNN--KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGF 1050
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQHNVLFDlLTVREHLeffarlkgaadetidieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDE 1130
Cdd:cd03228 81 VPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1131 PTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADlLGDRIAIISSGE 1180
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1984-2277 |
5.74e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 134.44 E-value: 5.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1984 KKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVmehsvlkdidgvhrnLGYCPQFDALDNL--- 2060
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV---------------LGYVPFKRRKEFArri 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 -------------LTAREHLYFYARLRGIK----QQNIPYisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNP 2123
Cdd:COG4586 98 gvvfgqrsqlwwdLPAIDSFRLLKAIYRIPdaeyKKRLDE----LVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2124 SVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEfKCF-GSVQHLKAKFGDGYTI 2202
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGR-IIYdGSLEELKERFGPYKTI 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2203 ILRTNAVADIDTLTQYiiehlpeATLKEKHNKVIHFRVTATIKLYEMFS-VLERArvelspAIEDYTVTQVTLDDV 2277
Cdd:COG4586 253 VLELAEPVPPLELPRG-------GEVIEREGNRVRLEVDPRESLAEVLArLLARY------PVRDLTIEEPPIEEV 315
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
975-1185 |
1.83e-33 |
|
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: 128.32 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQ 1053
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 hnvlfdlltvrehleffarlkgaadetidieierMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1134 GVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:cd03214 127 HLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
959-1187 |
4.52e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.57 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 959 QRSASIESYSDGEVGVEIINLCKYYNNK-----LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYID 1033
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1034 GWDILT----DIKKIRQNIGFTPQH--NVLFDLLTVREHLEFFARLKGAAD-ETIDIEIERMLDDLMLTNK-RDNYSTEL 1105
Cdd:COG1123 326 GKDLTKlsrrSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSrAERRERVAELLERVGLPPDlADRYPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1106 SGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRC 1183
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
....
gi 2041616051 1184 VGTS 1187
Cdd:COG1123 486 DGPT 489
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
987-1187 |
4.71e-33 |
|
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: 130.46 E-value: 4.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DIKKIRQN-IGFTPQHNVLFDLL 1061
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkELRELRRKkISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1062 TVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARR 1141
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2041616051 1142 SIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTS 1187
Cdd:cd03294 198 EMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
974-1186 |
7.53e-33 |
|
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: 128.51 E-value: 7.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFTPQ 1053
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1134 GVDPFARRsiwDLLLKYKQ-----GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:cd03300 160 ALDLKLRK---DMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
974-1181 |
2.03e-32 |
|
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: 127.24 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKL----ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DIKKIR 1045
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQH--NVLFDLLTVREHLE--FFARLKGAADETIDIEIERMLDDLMLTNKR-DNYSTELSGGMKRKLSIAIAFC 1120
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1121 ANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
974-1185 |
3.30e-32 |
|
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: 125.83 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFTPQ 1053
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1134 GVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:cd03301 160 NLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
974-1186 |
3.69e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 126.68 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNkLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFTPQ 1053
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1134 GVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:cd03299 159 ALDVRTKEKLREELkkIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGK 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
974-1181 |
8.57e-32 |
|
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: 124.56 E-value: 8.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL---TDIKKIRQNIGF 1050
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQHNVLFDLLTVREHL-EFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:cd03262 81 VFQQFNLFPHLTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
988-1186 |
1.04e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 133.35 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDLlTVREH 1066
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQRPHLFDT-TLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1067 LeffaRLkgAADETIDIEIERMLDDL----MLTNKRDNYSTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTAGV 1135
Cdd:COG4987 429 L----RL--ARPDATDEELWAALERVglgdWLAALPDGLDTWlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1136 DPFARRSIWDLLLKYKQGRTIIISTHFMDEADlLGDRIAIISSGELRCVGT 1186
Cdd:COG4987 503 DAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGT 552
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1989-2133 |
1.53e-31 |
|
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: 121.60 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKD-IDGVHRNLGYCPQFDALDNLLTAREHL 2067
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2068 YFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVR----QYSGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
974-1181 |
1.83e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.01 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY-NNKLALKNLSVKFYQNQITsFL-GRNGAGKSTTWSILTGLIPPTSGTAYIDGWDiLTDIKK-----IRQ 1046
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-LSRLKRreipyLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1047 NIGFTPQ-HNVLFDLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKT 1125
Cdd:COG2884 80 RIGVVFQdFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1126 VILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHfmDEA--DLLGDRIAIISSGEL 1181
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATH--DLElvDRMPKRVLELEDGRL 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
984-1181 |
6.99e-31 |
|
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: 122.38 E-value: 6.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 984 NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPP---TSGTAYIDGWDIltDIKKIRQNIGFTPQHNVLFDL 1060
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 LTVREHLEFFARLKG---AADETIDIEIERM-LDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:cd03234 96 LTVRETLTYTAILRLprkSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2041616051 1137 PFARRSIWDLLLKY-KQGRTIIISTHfMDEADL--LGDRIAIISSGEL 1181
Cdd:cd03234 176 SFTALNLVSTLSQLaRRNRIVILTIH-QPRSDLfrLFDRILLLSSGEI 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
974-1186 |
9.08e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 129.64 E-value: 9.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNN--KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPT---SGTAYIDGWDILTDIKKIR-QN 1047
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1048 IGFTPQH-NVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTV 1126
Cdd:COG1123 85 IGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1127 ILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
975-1180 |
2.33e-30 |
|
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: 121.52 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNN-KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DIKKIRQNIG 1049
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQH-----------NVLFDLLTVREHLEFFARLKGAADETIDIEIermLDDLMLTNKRDNYSTELSGGMKRKLSIAIA 1118
Cdd:cd03256 82 MIFQQfnlierlsvleNVLSGRLGRRSTWRSLFGLFPKEEKQRALAA---LERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1119 FCANSKTVILDEPTAGVDPFARRSIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1988-2182 |
2.48e-30 |
|
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: 120.26 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLK-DIDGVHRNLGYCPQfDALDNLL--TAR 2064
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLVFQ-NPDDQFFgpTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 EHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLW 2144
Cdd:cd03225 95 EEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 2041616051 2145 DCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03225 175 ELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
974-1186 |
6.04e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 120.57 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL-TDIKKIRQNIGFTP 1052
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAtTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDLLTVREHLEF--FARLKG---AADETIdieIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVI 1127
Cdd:COG4604 82 QENHINSRLTVRELVAFgrFPYSKGrltAEDREI---IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1128 LDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLrrLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
973-1186 |
1.05e-29 |
|
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: 119.75 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 973 GVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFTP 1052
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLM----LTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVIL 1128
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1129 DEPTAGVDPFARRSI--WDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:cd03296 161 DEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
988-1186 |
1.38e-29 |
|
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: 119.76 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIK--KI-RQNIGFTPQHNVLFDLLTVR 1064
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPphRIaRLGIARTFQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1065 EHL-------------EFFARLKGAADETIDI--EIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:COG0411 98 ENVlvaaharlgrgllAALLRLPRARREEREAreRAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKYK--QGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
989-1181 |
1.43e-29 |
|
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: 117.65 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPP--TSGTAYIDGWDIltDIKKIRQNIGFTPQHNVLFDLLTVREH 1066
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1067 LEFFARLKGaadetidieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDL 1146
Cdd:cd03213 103 LMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2041616051 1147 LLKY-KQGRTIIISTH---------FmdeadllgDRIAIISSGEL 1181
Cdd:cd03213 154 LRRLaDTGRTIICSIHqpsseifelF--------DKLLLLSQGRV 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1969-2181 |
1.75e-29 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 118.01 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVL---KDIDGV- 2044
Cdd:cd03259 1 LELKGLSKTYG-----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSG-------EILidgRDVTGVp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 --HRNLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGN 2122
Cdd:cd03259 69 peRRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2123 PSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1987-2197 |
2.69e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDIDGVHRNLGYCPQFDALDNL--LTAR 2064
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGYVPQRAEVDWDfpITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 E--------HLYFYARLRG-----IKQqnipyisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEP 2131
Cdd:COG1121 96 DvvlmgrygRRGLFRRPSRadreaVDE---------ALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2132 TTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLsIMVAGEFKCFGSVQ------HLKAKFG 2197
Cdd:COG1121 167 FAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEevltpeNLSRAYG 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1987-2190 |
3.09e-29 |
|
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: 117.82 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL-KDIDGVHRNLGYCPQfDALDNLL--TA 2063
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGLVFQ-NPDDQLFapTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2064 REHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFL 2143
Cdd:COG1122 94 EEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRREL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2041616051 2144 WDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQ 2190
Cdd:COG1122 174 LELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1970-2182 |
3.11e-29 |
|
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: 115.42 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1970 RMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLK-DIDGVHRNL 2048
Cdd:cd00267 1 EIENLSFRYG-----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFdaldnlltarehlyfyarlrgikqqnipyisgcllkrlgltlwadrpvrqySGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd00267 76 GYVPQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
982-1181 |
7.25e-29 |
|
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: 116.53 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 982 YYNN--KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQNIGFTPQHNVLF 1058
Cdd:cd03245 11 SYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 dLLTVREHLEFFARLkgAADETIdIEIERM--LDDLMLTNKrDNYSTE-------LSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:cd03245 91 -YGTLRDNITLGAPL--ADDERI-LRAAELagVTDFVNKHP-NGLDLQigergrgLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLgDRIAIISSGEL 1181
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1969-2182 |
9.78e-29 |
|
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: 116.77 E-value: 9.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKvygwQFGKkFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVL---KDIDG-- 2043
Cdd:cd03219 1 LEVRGLTK----RFGG-LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSG-------SVLfdgEDITGlp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 VHR--NLGYC---------PQFDALDNLLTA----REHLYFYARLRGIKQQNIPYISGcLLKRLGLTLWADRPVRQYSGG 2108
Cdd:cd03219 69 PHEiaRLGIGrtfqiprlfPELTVLENVMVAaqarTGSGLLLARARREEREARERAEE-LLERVGLADLADRPAGELSYG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2109 NKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
968-1186 |
1.47e-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: 123.33 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 968 SDGEVGVEIINLC-KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIR 1045
Cdd:COG4988 331 AAGPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDLlTVREHLEFFARlkGAADETIDIEIER-MLDDLmLTNKRDNYSTE-------LSGGMKRKLSIAI 1117
Cdd:COG4988 411 RQIAWVPQNPYLFAG-TIRENLRLGRP--DASDEELEAALEAaGLDEF-VAALPDGLDTPlgeggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1118 AFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHfmDEADL-LGDRIAIISSGELRCVGT 1186
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
975-1187 |
1.87e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 115.85 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL---TDiKKIRQNIGFT 1051
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglpPH-RIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLE---FFARLKGAADETidieIERMLdDL--MLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTV 1126
Cdd:COG0410 84 PEGRRIFPSLTVEENLLlgaYARRDRAEVRAD----LERVY-ELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1127 ILDEPTAGVDPFARRSIWDLL--LKyKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTS 1187
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
983-1181 |
2.08e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 115.89 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 983 YNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFT-PQHNVLFDLL 1061
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1062 TVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARR 1141
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2041616051 1142 SIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03267 191 NIRNFLKEYnrERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1968-2182 |
3.44e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 114.91 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGV--- 2044
Cdd:cd03257 1 LLEVKNLSVSFP-TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 -HRNLGYCPQ--FDALDNLLTAREHLY--FYARLRGIKQQNIPYISGCLLKRLGLTL-WADRPVRQYSGGNKRKLSTAIA 2118
Cdd:cd03257 80 rRKEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2119 LIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1987-2182 |
4.65e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 114.74 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYC-PQFDALDNLLTARE 2065
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2066 HLYFYARLRGIK----QQNIPYISgcllKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:cd03267 115 SFYLLAAIYDLPparfKKRLDELS----ELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 2142 FLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
974-1186 |
5.69e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.87 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFTPQ 1053
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:COG3839 83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1134 GVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
971-1186 |
6.97e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 6.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 971 EVGVEIINLCKYYNN--KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTD-IKKIRQN 1047
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1048 IGFTPQH-NVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTV 1126
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1127 ILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEAdLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1987-2187 |
8.61e-28 |
|
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: 113.01 E-value: 8.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVmehsVLKDIDGVHRNLGYCPQFDALDNL--LTAR 2064
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV----FGKPLEKERKRIGYVPQRRSIDRDfpISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 E--------HLYFYARLRGIKQQNIPYisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:cd03235 89 DvvlmglygHKGLFRRLSKADKAKVDE----ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2137 VRAKRFLWDCILTLTRKEhKSVIITSHSMEECEVLCNRLsIMVAGEFKCFG 2187
Cdd:cd03235 165 PKTQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1971-2192 |
8.82e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 120.39 E-value: 8.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1971 MTDLIKVYGWQF---GKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLT---SGNAYVMEHSVLKDIDGV 2044
Cdd:COG1123 1 MTPLLEVRDLSVrypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 H-RNLGYCPQfDALDNL--LTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIG 2121
Cdd:COG1123 81 RgRRIGMVFQ-DPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2122 NPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHL 2192
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
978-1186 |
1.00e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.84 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIRQNIGFTPQHN 1055
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIslLPLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1056 VLFDLLTVREHLefFARLKGAADETIDIEIER---MLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPT 1132
Cdd:PRK10895 88 SIFRRLSVYDNL--MAVLQIRDDLSAEQREDRaneLMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1133 AGVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
974-1186 |
1.04e-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: 111.37 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDG--WDILTDIKKIRQNIGFT 1051
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQhnvlfdlltvrehleffarlkgaadetidieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1132 TAGVDPFARRSIWDLL--LKyKQGRTIIISTHFMDEADLLGDRIAIISSGelRCVGT 1186
Cdd:cd03216 110 TAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
974-1181 |
1.08e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.82 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY----NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DIKKIR 1045
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHnvlFDLL---TVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFcAN 1122
Cdd:PRK11153 82 RQIGMIFQH---FNLLssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL-AS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1123 SKTVIL-DEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK11153 158 NPKVLLcDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
981-1237 |
1.22e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.79 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 981 KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIK---KIRQNIGFTPQH--N 1055
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTVGIVFQNpdD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1056 VLFdLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGV 1135
Cdd:PRK13639 90 QLF-APTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1136 DPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT--SMFLKRKYAEGYNLivEFTSVSDEEE 1212
Cdd:PRK13639 169 DPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTpkEVFSDIETIRKANL--RLPRVAHLIE 246
|
250 260
....*....|....*....|....*
gi 2041616051 1213 LKTHSDENVMNNNSTIDDNASKLVN 1237
Cdd:PRK13639 247 ILNKEDNLPIKMGYTIGEARRNIKE 271
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
974-1181 |
1.38e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 116.33 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNK----LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DIKKIR 1045
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHnvlFDLL---TVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFcAN 1122
Cdd:COG1135 82 RKIGMIFQH---FNLLssrTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL-AN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1123 SKTVIL-DEPTAGVDPFARRSIWDLLLK--YKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:COG1135 158 NPKVLLcDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
974-1186 |
1.42e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYN-----NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTD----IKKI 1044
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDkkvkLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1045 RQNIGFT---PQHNvLFDLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNK--RDNYSTELSGGMKRKLSIAIAF 1119
Cdd:PRK13637 82 RKKVGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1120 CANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
974-1181 |
1.79e-27 |
|
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: 112.50 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY-NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTD--IKKIRQNI 1048
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdLRGraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1049 GFTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVIL 1128
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1129 DEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
974-1198 |
2.59e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.95 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKST---TWSILTGLIP--PTSGTAYIDGWDIL---TDIKKIR 1045
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIYsprTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDLlTVREHLEFFARLKGAAD-ETIDIEIERMLDDLMLTNK-RD---NYSTELSGGMKRKLSIAIAFC 1120
Cdd:PRK14239 86 KEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDkQVLDEAVEKSLKGASIWDEvKDrlhDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1121 ANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT--SMFL--KRKYAE 1196
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDtkQMFMnpKHKETE 244
|
..
gi 2041616051 1197 GY 1198
Cdd:PRK14239 245 DY 246
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
983-1214 |
2.91e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 114.80 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 983 YNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGftpqhnVLF---- 1058
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIG------VVFgqrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 ----DlLTVREHLEFFARL----KGAADETIDIEIERM-LDDLMLTNKRdnystELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:COG4586 106 qlwwD-LPAIDSFRLLKAIyripDAEYKKRLDELVELLdLGELLDTPVR-----QLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLKRKYAEGYNLIVEFTSV 1207
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEP 259
|
....*..
gi 2041616051 1208 SDEEELK 1214
Cdd:COG4586 260 VPPLELP 266
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1981-2197 |
3.75e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 121.00 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKkFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSV-LKDIDgVHRNLGYCPQFDALDN 2059
Cdd:NF033858 275 RFGD-FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIA-TRRRVGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2060 LLTAREHLYFYARLRGIKQQNIP-YISGcLLKRLGLTLWAD-RP------VRQysggnkrKLSTAIALIGNPSVIFMDEP 2131
Cdd:NF033858 353 ELTVRQNLELHARLFHLPAAEIAaRVAE-MLERFDLADVADaLPdslplgIRQ-------RLSLAVAVIHKPELLILDEP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2132 TTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEvLCNRLSIMVAGEFKCFGSVQHLKAKFG 2197
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
974-1186 |
4.65e-27 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 119.94 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY--NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGF 1050
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQHNVLFDLlTVREHLEFF------ARLKGAADET-IDIEIERMLD--DLMLTNKRDNysteLSGGMKRKLSIAIAFCA 1121
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGdpdatdEEIIEAARLAgLHDFIEALPMgyDTVVGEGGSN----LSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1122 NSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH---FMDEAdllgDRIAIISSGELRCVGT 1186
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----DRIIVLDKGRIVEDGT 692
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
974-1181 |
5.03e-27 |
|
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: 112.20 E-value: 5.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY----NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQNI 1048
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1049 GFTPQH--NVLFDLLTVREHLEFFARLKGAADetIDIEIERMLDDLMLTNK-RDNYSTELSGGMKRKLSIAIAFCANSKT 1125
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1126 VILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1969-2166 |
2.76e-26 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 109.12 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDG----- 2043
Cdd:cd03255 1 IELKNLSKTYG-GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 VHRNLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNP 2123
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2041616051 2124 SVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSME 2166
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
978-1182 |
3.14e-26 |
|
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: 108.92 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQN-QITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKI-----RQNIGFT 1051
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLNeEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLEFfaRLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:cd03297 81 FQQYALFPHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1132 TAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELR 1182
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1930-2201 |
4.13e-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: 115.39 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1930 IADRIR-RKPPKIVSIEEDDDVAAERQRLYNDPNNTSHD------------VLRMTDLIKVYGWQFGKKFTAVNNICAGV 1996
Cdd:COG1123 209 IADRVVvMDDGRIVEDGPPEEILAAPQALAAVPRLGAARgraapaaaaaepLLEVRNLSKRYPVRGKGGVRAVDDVSLTL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1997 KQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL----KDIDGVHRNLGYCPQ--FDALDNLLTAREHLYFY 2070
Cdd:COG1123 289 RRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEP 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2071 ARLRGIkqqnipyISGC--------LLKRLGLTLW-ADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:COG1123 369 LRLHGL-------LSRAerrervaeLLERVGLPPDlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQA 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2142 FLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGDGYT 2201
Cdd:COG1123 442 QILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYT 501
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
982-1166 |
7.50e-26 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 106.74 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 982 YYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIK---KIRQNIGFTPQH--NV 1056
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKgllERRQRVGLVFQDpdDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1057 LFDLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:TIGR01166 81 LFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 2041616051 1137 PFARRSIWDLLLKYK-QGRTIIISTHFMDEA 1166
Cdd:TIGR01166 160 PAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
978-1161 |
1.12e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.88 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIltDIKKIRQNIGFTPQHNVL 1057
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1058 FDLLTVREHLEFFARLKGAADETIDIEIERM-LDDlmLTNKRDNYsteLSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:PRK13539 85 KPALTVAENLEFWAAFLGGEELDIAAALEAVgLAP--LAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*.
gi 2041616051 1137 PFARRSIWDLLLKY-KQGRTIIISTH 1161
Cdd:PRK13539 160 AAAVALFAELIRAHlAQGGIVIAATH 185
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1591-1923 |
1.27e-25 |
|
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: 110.56 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1591 KRFGGIEFLSKALEENGINTIntslinqlanmnnIVVNEEKIAELFRIHQPQVAVWYDNMGWPSSLAYLNIFNNALLRSL 1670
Cdd:pfam12698 62 QYVDSEEEAKEALKNGKIDGL-------------LVIPKGFSKDLLKGESATVTVYINSSNLLVSKLILNALQSLLQQLN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1671 LPSSDVKdygITAIQHPLPQTQIEIDLELQSRAYLELFTAICVIFALAFIPASFLVFLIDERATTSKHLQFVSGVKGIIY 1750
Cdd:pfam12698 129 ASALVLL---LEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1751 WVSNYAWDIVNFTVSLVFCVIIFLAFNVQAYvhkeNLLCLILLLFLYGFATIPLMYPFSYLFKTPSTGFVLISCINIFLG 1830
Cdd:pfam12698 206 WLGKILGDFLVGLLQLLIILLLLFGIGIPFG----NLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1831 LITTIsTFTLENISDepdlqkinvVLMKVFLIFPHYCLGRGLFDmsklhaadeiISKYNPYYqkkspfefnQVGRNLMAL 1910
Cdd:pfam12698 282 GFFGG-LFPLEDPPS---------FLQWIFSIIPFFSPIDGLLR----------LIYGDSLW---------EIAPSLIIL 332
|
330
....*....|...
gi 2041616051 1911 AIEGIIFFIFALL 1923
Cdd:pfam12698 333 LLFAVVLLLLALL 345
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1969-2201 |
1.41e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 107.97 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGV-HRN 2047
Cdd:COG1124 2 LEVRNLSVSYG-QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2048 LGYCPQ--FDALDNLLTAREHLYFYARLRGIKQQNiPYISGcLLKRLGLTL-WADRPVRQYSGGNKRKLSTAIALIGNPS 2124
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE-ERIAE-LLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2125 VIFMDEPTTGMD--VRAKrflwdcILTL---TRKEHK-SVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGD 2198
Cdd:COG1124 159 LLLLDEPTSALDvsVQAE------ILNLlkdLREERGlTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
...
gi 2041616051 2199 GYT 2201
Cdd:COG1124 233 PYT 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
984-1186 |
1.94e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 984 NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIRQNIGFTPQH--NVLFD 1059
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDIRNKAGMVFQNpdNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1060 LLtVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFA 1139
Cdd:PRK13633 101 TI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 1140 RRSIWDLL--LKYKQGRTIIISTHFMDEAdLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13633 180 RREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1969-2183 |
2.54e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLikvyGWQFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVmEHSVLKDIDGVH--R 2046
Cdd:COG4619 1 LELEGL----SFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYL-DGKPLSAMPPPEwrR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 NLGYCPQ----FDAldnllTAREHLYFYARLRGIKQQNIPYISgcLLKRLGLTLWA-DRPVRQYSGGNKRKLSTAIALIG 2121
Cdd:COG4619 75 QVAYVPQepalWGG-----TVRDNLPFPFQLRERKFDRERALE--LLERLGLPPDIlDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2122 NPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEF 2183
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
987-1186 |
5.16e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.12 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL----TDIKKIR-QNIGFTPQHNVLFDLL 1061
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1062 TVREHLEFFARLKGAADETidiEIERMLDDLM---LTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPF 1138
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEE---RREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1139 ARRSIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK10070 199 IRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1979-2163 |
5.86e-25 |
|
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: 104.05 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1979 GWQFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKdidgvhrnlgycpqfdald 2058
Cdd:cd03214 6 SVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 nlLTAREhlyfYARLRGIKQQnipyisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVR 2138
Cdd:cd03214 66 --LSPKE----LARKIAYVPQ--------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180
....*....|....*....|....*
gi 2041616051 2139 AKRFLWDCILTLTRKEHKSVIITSH 2163
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLH 156
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1969-2178 |
8.07e-25 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 104.86 E-value: 8.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDIDGVHRNL 2048
Cdd:cd03293 1 LEVRNVSKTYG-GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIM 2178
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1969-2182 |
9.09e-25 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 104.93 E-value: 9.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKdiDGVHR-- 2046
Cdd:cd03218 1 LRAENLSKRYG-----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK--LPMHKra 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 --NLGYCPQ----FDAL---DNLLTAREHLYFyarLRGIKQQNIPYisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAI 2117
Cdd:cd03218 74 rlGIGYLPQeasiFRKLtveENILAVLEIRGL---SKKEREEKLEE----LLEEFHITHLRKSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2118 ALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKeHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
982-1161 |
1.48e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.02 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 982 YYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKKI-----RQNIGFTPQHNV 1056
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG----VDIRDLtleslRRQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1057 LFDLlTVREHLEFFArlKGAADEtidiEIER-----MLDDLmLTNKRDNYSTE-------LSGGMKRKLSIAIAFCANSK 1124
Cdd:COG1132 425 LFSG-TIRENIRYGR--PDATDE----EVEEaakaaQAHEF-IEALPDGYDTVvgergvnLSGGQRQRIAIARALLKDPP 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 2041616051 1125 TVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1969-2182 |
1.97e-24 |
|
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: 105.03 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGWQFGKKFT-------------------AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGN 2029
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2030 AYV-------MEHSVL-----KDIDGVHRNLGYCPQFDALDNllTArehlyFYARLRGIKQQNIPYISGCLLKRLGLTLW 2097
Cdd:cd03294 81 VLIdgqdiaaMSRKELrelrrKKISMVFQSFALLPHRTVLEN--VA-----FGLEVQGVPRAEREERAAEALELVGLEGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2098 ADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSI 2177
Cdd:cd03294 154 EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAI 233
|
....*
gi 2041616051 2178 MVAGE 2182
Cdd:cd03294 234 MKDGR 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1983-2163 |
2.33e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 103.89 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1983 GKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIP---LTSGNAYVMEHSVlkDIDGVHRNLGYCPQFDALDN 2059
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2060 LLTAREHLYFYARLRGIKQQNIPYIS----GCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGM 2135
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKkrveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190
....*....|....*....|....*....|
gi 2041616051 2136 DVRAKRFLwdcILTLTR--KEHKSVIITSH 2163
Cdd:cd03234 175 DSFTALNL---VSTLSQlaRRNRIVILTIH 201
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
974-1200 |
2.54e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLC-KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIK---KIRQNIG 1049
Cdd:PRK13636 6 LKVEELNyNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 --FTPQHNVLFDlLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVI 1127
Cdd:PRK13636 86 mvFQDPDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1128 LDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT--SMFLKRKYAEGYNL 1200
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNpkEVFAEKEMLRKVNL 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
974-1181 |
2.95e-24 |
|
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: 103.34 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLC-KYYNN-KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGF 1050
Cdd:cd03244 3 IEFKNVSlRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQHNVLFDlLTVREHLEFFARlkgAADETID-----------IEIERMLDDLMLTNKRDNYSTelsgGMKRKLSIAIAF 1119
Cdd:cd03244 83 IPQDPVLFS-GTIRSNLDPFGE---YSDEELWqalervglkefVESLPGGLDTVVEEGGENLSV----GQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1120 CANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH----FMDEadllgDRIAIISSGEL 1181
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIIDS-----DRILVLDKGRV 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
984-1181 |
3.31e-24 |
|
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: 101.62 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 984 NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQHNVLFDlltv 1063
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFD---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1064 rehleffarlkgaadetidieiermlddlmlTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSI 1143
Cdd:cd03247 89 -------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2041616051 1144 WDLLLKYKQGRTIIISTHfmdeaDLLG----DRIAIISSGEL 1181
Cdd:cd03247 138 LSLIFEVLKDKTLIWITH-----HLTGiehmDKILFLENGKI 174
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1962-2221 |
3.83e-24 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 106.36 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1962 NNTSHDVLRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTtfkmltGEIPLTSGN-----------A 2030
Cdd:NF000106 7 SNGARNAVEVRGLVKHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHV*Gpdagrrpwrf*T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2031 YVMEHSVLKDIDGVHRnlgycPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNK 2110
Cdd:NF000106 76 WCANRRALRRTIG*HR-----PVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2111 RKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRkEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQ 2190
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
250 260 270
....*....|....*....|....*....|.
gi 2041616051 2191 HLKAKFGdGYTIILRTNAVADIDTLTQYIIE 2221
Cdd:NF000106 230 ELKTKVG-GRTLQIRPAHAAELDRMVGAIAQ 259
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1968-2182 |
6.35e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.80 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYgwqfgKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYvmehsvlkdIDG---- 2043
Cdd:COG1137 3 TLEAENLVKSY-----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF---------LDGedit 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 ---VHR----NLGYCPQ----FDAL---DNLLTAREHLYFYARLRGIKQQNipyisgcLLKRLGLTLWADRPVRQYSGGN 2109
Cdd:COG1137 69 hlpMHKrarlGIGYLPQeasiFRKLtveDNILAVLELRKLSKKEREERLEE-------LLEEFGITHLRKSKAYSLSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2110 KRKLSTAIALIGNPSVIFMDEPTTGMD----VRAKRFlwdcILTLtrKEHK-SVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpiavADIQKI----IRHL--KERGiGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
970-1186 |
8.76e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.81 E-value: 8.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdILTDIKK----IR 1045
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG--KPVRIRSprdaIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDLLTVREHL--------EFFARLKGAADETIDIeIERM-LD-DLmltnkrDNYSTELSGGMKRKLSI 1115
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIvlgleptkGGRLDRKAARARIREL-SERYgLDvDP------DAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1116 AIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKyKQGRTIIISTHFMDEADLLGDRIAIISSGELrcVGT 1186
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILrrLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
974-1186 |
1.05e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.34 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLC-KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL-TDIKKIRQNIGFT 1051
Cdd:PRK13652 4 IETRDLCySYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQH--NVLFDLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:PRK13652 84 FQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1130 EPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
974-1165 |
1.13e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.99 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL---TDIKKIRQNIGF 1050
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQH-NvLFDLLTVREHLEFfA--RLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKtVI 1127
Cdd:COG1126 82 VFQQfN-LFPHLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK-VM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1128 L-DEPTAGVDPfarRSIWDLL-----LKyKQGRTIIISTH-------------FMDE 1165
Cdd:COG1126 159 LfDEPTSALDP---ELVGEVLdvmrdLA-KEGMTMVVVTHemgfarevadrvvFMDG 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1968-2163 |
1.42e-23 |
|
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: 102.43 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLikvyGWQFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDIDGVH-- 2045
Cdd:COG1120 1 MLEAENL----SVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG----RDLASLSrr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 ---RNLGYCPQFDALDNLLTARE--------HLYFYARLRG-----IKQqnipyisgcLLKRLGLTLWADRPVRQYSGGN 2109
Cdd:COG1120 72 elaRRIAYVPQEPPAPFGLTVRElvalgrypHLGLFGRPSAedreaVEE---------ALERTGLEHLADRPVDELSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2110 KRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSH 2163
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
988-1186 |
2.13e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.78 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKI------RQNIGFT---PQHNVLF 1058
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 DllTVREHLEFFARLKGAADETIDIEIERMLDDLMLTN---KRDNYstELSGGMKRKLSIAIAFCANSKTVILDEPTAGV 1135
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyvKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1136 DPFARRSIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13645 182 DPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
989-1179 |
3.50e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 100.62 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT---DIKKIRQNIGFTPqhnvlfdLLTVRE 1065
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1066 HL-----EFFARLKGAADETIdieIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFAR 1140
Cdd:TIGR01184 74 NIalavdRVLPDLSKSERRAI---VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 1141 RSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:TIGR01184 151 GNLQEELMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
968-1181 |
4.95e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.88 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 968 SDGEVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKST---TWSILTGLIPP--TSGTAYIDGWDIL---T 1039
Cdd:COG1117 6 STLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGEDIYdpdV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1040 DIKKIRQNIGFTPQHNVLFDLlTVREHLEFFARLKGAAD-ETIDIEIERMLDDLML----TNKRDNYSTELSGGMKRKLS 1114
Cdd:COG1117 86 DVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSkSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1115 IAIAFcANSKTVIL-DEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:COG1117 165 IARAL-AVEPEVLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
986-1197 |
8.59e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.32 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 986 KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdiltdiKKIRQ---NIGFTPQHNVLFDLLT 1062
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-------VPVTGpgaDRGVVFQKDALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1063 VREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRS 1142
Cdd:COG4525 93 VLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1143 IWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT-SMFLKRKYAEG 1197
Cdd:COG4525 173 MQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERlELDFSRRFLAG 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1969-2192 |
9.61e-23 |
|
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: 99.68 E-value: 9.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlKDIDGVH--R 2046
Cdd:cd03295 1 IEFENVTKRYG----GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDPVElrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 NLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGL--TLWADRPVRQYSGGNKRKLSTAIALIGNPS 2124
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2125 VIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHL 2192
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
988-1181 |
1.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-----DIKKIRQNIGFTPQ--HNVLFDL 1060
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 lTVREHLEFFARLKGAADEtidiEIERM-LDDLMLT----NKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGV 1135
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQE----EAEALaREKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2041616051 1136 DPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
970-1161 |
1.32e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.84 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLcKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNI 1048
Cdd:cd03254 1 GEIEFENVNF-SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1049 GFTPQHNVLFDLlTVREHLEFFARLKGAADETIDIEIERMLDDLM-LTNKRDNYSTE----LSGGMKRKLSIAIAFCANS 1123
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMkLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2041616051 1124 KTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
976-1182 |
1.47e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 98.37 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 976 IINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKKIRQNIGFTPQhn 1055
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSLLGLGGGFNPE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1056 vlfdlLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRD----NYSTelsgGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:cd03220 99 -----LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDlpvkTYSS----GMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1132 TAGVDP-FARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELR 1182
Cdd:cd03220 170 LAVGDAaFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1979-2182 |
2.46e-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: 96.85 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1979 GWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG--EIPLTSGNAYVMEHSVlkDIDGVHRNLGYCPQFDA 2056
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL--DKRSFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2057 LDNLLTAREHLYFYARLRGIkqqnipyisgcllkrlgltlwadrpvrqySGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:cd03213 93 LHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2137 VRAKRFLWDCILTLtRKEHKSVIITSH----SMEEcevLCNRLSIMVAGE 2182
Cdd:cd03213 144 SSSALQVMSLLRRL-ADTGRTIICSIHqpssEIFE---LFDKLLLLSQGR 189
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1956-2189 |
4.33e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.84 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1956 RLYNDPNNtshdvlRMTDLIKVYGWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV-ME 2034
Cdd:COG1134 15 RLYHEPSR------SLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVnGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2035 HSVLKDIdgvhrNLGYCPQfdaldnlLTAREHLYFYARLRGIKQQNI----PYI---SGcllkrLGLTLwaDRPVRQYSG 2107
Cdd:COG1134 89 VSALLEL-----GAGFHPE-------LTGRENIYLNGRLLGLSRKEIdekfDEIvefAE-----LGDFI--DQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2108 GNKRKLSTAIALIGNPSVIFMDEPTTGMDVR-AKRFLwDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCF 2186
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCL-ARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
...
gi 2041616051 2187 GSV 2189
Cdd:COG1134 228 GDP 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1984-2187 |
4.36e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.22 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1984 KKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVME--HSVLkdidgvhrNLGYcpqfdALDNLL 2061
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLL--------GLGG-----GFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2041616051 2142 FLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFG 2187
Cdd:cd03220 180 KCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1981-2184 |
4.76e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 96.56 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLKDIDGVH-----RNLGYCPQfD 2055
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSG-------SILLNGKPIKakerrKSIGYVMQ-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2056 ALDNLL--TAREHLYFYARLRGIKQQNIPyisgCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:cd03226 80 VDYQLFtdSVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2134 GMDVRAKRFLWDCILTLTrKEHKSVIITSHSMEECEVLCNRLSIMVAGEFK 2184
Cdd:cd03226 156 GLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
970-1181 |
5.99e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 95.19 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLCkyynNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIRQN 1047
Cdd:cd03215 1 GEPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1048 IGFTP---QHNVLFDLLTVREHLeFFARLkgaadetidieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSK 1124
Cdd:cd03215 77 IAYVPedrKREGLVLDLSVAENI-ALSSL-------------------------------LSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1125 TVILDEPTAGVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
988-1200 |
6.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.31 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTD-----IKKIRQNIGFT---PQHNVLFD 1059
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRKRIGMVfqfPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1060 llTVREHLEFfarlkGAADETIDIE--IERMLDDLM-LTNKRDNYST---ELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PRK13646 102 --TVEREIIF-----GPKNFKMNLDevKNYAHRLLMdLGFSRDVMSQspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1134 GVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGEL--RCVGTSMFLKRKYAEGYNL 1200
Cdd:PRK13646 175 GLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKKLADWHI 245
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1969-2182 |
6.59e-22 |
|
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: 94.95 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV--MEHSVLKDIDGVHR 2046
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 -NLGYCPQFDALDNLLTAREhlyfyarlrgikqqNIpyisgcllkRLGLtlwadrpvrqySGGNKRKLSTAIALIGNPSV 2125
Cdd:cd03229 76 rRIGMVFQDFALFPHLTVLE--------------NI---------ALGL-----------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 2126 IFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1968-2192 |
7.73e-22 |
|
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: 96.50 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGNAYVMEHSVL----KDID 2042
Cdd:cd03258 1 MIELKNVSKVFG-DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERP-TSGSVLVDGTDLTllsgKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2043 GVHRNLGYCPQ-FdaldNLL---TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIA 2118
Cdd:cd03258 79 KARRRIGMIFQhF----NLLssrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2119 LIGNPSVIFMDEPTTGMDVRAKrflwDCILTLTRKEHKS-----VIITsHSMEECEVLCNRLSIMVAGEFKCFGSVQHL 2192
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETT----QSILALLRDINRElgltiVLIT-HEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
978-1186 |
9.30e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 9.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDiKKIRQNIGFTPQHN 1055
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmLSS-RQLARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1056 VLFDLLTVRE--------HLEFFARLKGAADETIDIEIERM-LDDlmLTNKRdnySTELSGGMKRKLSIAIAFCANSKTV 1126
Cdd:PRK11231 86 LTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTrINH--LADRR---LTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1127 ILDEPTAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
988-1161 |
1.21e-21 |
|
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: 101.59 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDiLTDI--KKIRQNIGFTPQHNVLFDLlTVRE 1065
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADAdaDSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1066 HLEFfaRLKGAADETIDIEIERM-LDDL------MLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPF 1138
Cdd:TIGR02857 415 NIRL--ARPDASDAEIREALERAgLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180
....*....|....*....|...
gi 2041616051 1139 ARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:TIGR02857 493 TEAEVLEALRALAQGRTVLLVTH 515
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
986-1181 |
1.31e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.59 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 986 KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTD-----IKKIRQNIGFTPQ--HNVLF 1058
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 DLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYST-ELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDP 1137
Cdd:PRK13641 100 EN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2041616051 1138 FARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK13641 179 EGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1963-2178 |
1.41e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 96.70 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1963 NTSHDVLRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDID 2042
Cdd:COG1116 2 SAAAPALELRGVSKRFP-TGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2043 GVHRNLGYCPQFDALdnL--LTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALI 2120
Cdd:COG1116 77 GPGPDRGVVFQEPAL--LpwLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2121 GNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIM 2178
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1968-2166 |
1.49e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 95.50 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSV--LKDIDGVH 2045
Cdd:COG1136 4 LLELRNLTKSYG-TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIssLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 ---RNLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGN 2122
Cdd:COG1136 83 lrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2041616051 2123 PSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSME 2166
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
974-1179 |
2.37e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.34 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYY-NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQNIG-- 1049
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGlv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:PRK13647 85 FQDPDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLK-YKQGRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
982-1196 |
2.69e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 94.99 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 982 YYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDL 1060
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 lTVREHLEFfARLKGAADETIDIEIERMLDDLMLtNKRDNYSTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03253 90 -TIGYNIRY-GRPDATDEEVIEAAKAAQIHDKIM-RFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1134 GVDPFARRSIWDLLLKYKQGRTIIISTH----FMDeadllGDRIAIISSGELRCVGTSMFLKRK---YAE 1196
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGRTTIVIAHrlstIVN-----ADKIIVLKDGRIVERGTHEELLAKgglYAE 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
984-1186 |
3.22e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.24 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 984 NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDG--------WDILTDIKKIRQN-----IGF 1050
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvWDVRRQVGMVFQNpdnqfVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQHNVLFDLltvrehleffarlkgaadETIDIE----IERMLDDLMLTNKRDNYSTE---LSGGMKRKLSIAIAFCANS 1123
Cdd:PRK13635 98 TVQDDVAFGL------------------ENIGVPreemVERVDQALRQVGMEDFLNREphrLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1124 KTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEAdLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGT 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1969-2178 |
4.04e-21 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 92.11 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlkdidgvhrnl 2048
Cdd:cd03216 1 LELRGITKRFG-----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 gycpqfdaldNLLTAREhlyfyARLRGIkqqnipyisgcllkrlgltlwadRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03216 65 ----------SFASPRD-----ARRAGI-----------------------AMVYQLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2129 DEPTTGMDVR-AKRFLwdCILTLTRKEHKSVIITSHSMEECEVLCNRLSIM 2178
Cdd:cd03216 107 DEPTAALTPAeVERLF--KVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
958-1186 |
5.51e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.46 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 958 KQRSASIESYSDGEVgVEIINLCKYYNNK-----LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYI 1032
Cdd:PRK13631 7 KKKLKVPNPLSDDII-LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1033 DGWDI-----------------LTDIKKIRQNIGFT---PQHNVLFDllTVREHLEF----FARLKGAADETIDIEIERM 1088
Cdd:PRK13631 86 GDIYIgdkknnhelitnpyskkIKNFKELRRRVSMVfqfPEYQLFKD--TIEKDIMFgpvaLGVKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1089 -LDDLMLtnkrDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEA 1166
Cdd:PRK13631 164 gLDDSYL----ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHV 239
|
250 260
....*....|....*....|
gi 2041616051 1167 DLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGT 259
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1969-2187 |
5.75e-21 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 93.47 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlKDIDGVHRNL 2048
Cdd:cd03301 1 VELENVTKRFG-----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFG 2187
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1005-1161 |
5.96e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 99.36 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1005 LGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDLlTVREHLEFfARlKGAADEtidi 1083
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVRENLRL-AR-PDATDE---- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1084 EIERMLDDLMLTN----KRDNYSTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ 1152
Cdd:TIGR02868 440 ELWAALERVGLADwlraLPDGLDTVlgeggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS 519
|
....*....
gi 2041616051 1153 GRTIIISTH 1161
Cdd:TIGR02868 520 GRTVVLITH 528
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
974-1175 |
7.51e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 95.89 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKL----ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPP---TSGTAYIDGWDILT----DIK 1042
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1043 KIRQN-IGFTPQhnvlfD-------LLTVREHL-EFFARLKGAADETIDIEIERMLDDLMLTNKR---DNYSTELSGGMK 1110
Cdd:COG0444 82 KIRGReIQMIFQ-----DpmtslnpVMTVGDQIaEPLRIHGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1111 RKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHfmdeaDL-----LGDRIAI 1175
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITH-----DLgvvaeIADRVAV 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
974-1186 |
8.13e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQN-IGFT 1051
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrFRSPRDAQAAgIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLeFFARLKG-------------AAD--ETIDIEIErmLDDLMltnkrdnysTELSGGMKRKLSIA 1116
Cdd:COG1129 85 HQELNLVPNLSVAENI-FLGREPRrgglidwramrrrAREllARLGLDID--PDTPV---------GDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1117 IAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKyKQGRTIIISTHFMDEADLLGDRIAIISSGELrcVGT 1186
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIrrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1968-2194 |
1.22e-20 |
|
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: 93.51 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL----KDIDG 2043
Cdd:COG1127 5 MIEVRNLTKSFG-----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 VHRNLGYCPQFDAL-DNlLTAREHLYFYAR-LRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIG 2121
Cdd:COG1127 80 LRRRIGMLFQGGALfDS-LTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2122 NPSVIFMDEPTTGMD-VRAKRFLwDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKA 2194
Cdd:COG1127 159 DPEILLYDEPTAGLDpITSAVID-ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
986-1186 |
1.36e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 94.70 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 986 KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIdGWDILT------DIKKIRQNIGFT---PQHNv 1056
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITagkknkKLKPLRKKVGIVfqfPEHQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1057 LFDlLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNK-RDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGV 1135
Cdd:PRK13634 98 LFE-ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1136 DPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13634 177 DPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
974-1179 |
1.43e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.23 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL---TDIKKIRQNIGF 1050
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQHNVLFDLLTVREHLEFFA-RLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1130 EPTAGVDPFARRSIwdllLKYKQ-----GRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:PRK09493 162 EPTSALDPELRHEV----LKVMQdlaeeGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
979-1161 |
1.45e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.97 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 979 LCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPP---TSGTAYIDGWDIltDIKKIRQNIGFTPQHN 1055
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1056 VLFDLLTVREHLEFFARLKGAADETIDIEIER---MLDDLMLTNKRD------NYSTELSGGMKRKLSIAIAFCANSKTV 1126
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAHLRMPRRVTKKEKRERvdeVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 2041616051 1127 ILDEPTAGVDPFARRSIWDLLLKYKQ-GRTIIISTH 1161
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQkGKTIICTIH 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1996-2190 |
1.47e-20 |
|
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: 93.17 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDIDGV---HRNLGYCPQFDALDNLLTAREHLYFYAR 2072
Cdd:cd03299 22 VERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLppeKRDISYVPQNYALFPHMTVYKNIAYGLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2073 LRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTR 2152
Cdd:cd03299 98 KRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRK 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 2041616051 2153 KEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQ 2190
Cdd:cd03299 178 EFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
932-1185 |
1.74e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.95 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 932 IRKRTEYLINLEKN---QSENTNELDNRVKQRSASIESYSDGEVGVEII---NLCKYYNNK-----LALKNLSVKFYQNQ 1000
Cdd:TIGR03269 232 IEDLSDKAIWLENGeikEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIkvrNVSKRYISVdrgvvKAVDNVSLEVKEGE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1001 ITSFLGRNGAGKSTTWSILTGLIPPTSGTAYI---DGWDILTDIK-----KIRQNIGFTPQ------HNVLFDLLTVREH 1066
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEWVDMTKPGpdgrgRAKRYIGILHQeydlypHRTVLDNLTEAIG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1067 LEF---FARLKGaadetidIEIERM--LDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARR 1141
Cdd:TIGR03269 392 LELpdeLARMKA-------VITLKMvgFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKV 464
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2041616051 1142 SIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:TIGR03269 465 DVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
981-1186 |
1.91e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 981 KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDG---WdiLTDIkkirqNIGFTPQhnvl 1057
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsA--LLEL-----GAGFHPE---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1058 fdlLTVREHLEFFARLKGAADEtidiEIERMLDDLM----LTNKRD----NYSTelsgGMKRKLSIAIAFCANSKTVILD 1129
Cdd:COG1134 103 ---LTGRENIYLNGRLLGLSRK----EIDEKFDEIVefaeLGDFIDqpvkTYSS----GMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1130 EPTAGVDP-FARRSIwDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG1134 172 EVLAVGDAaFQKKCL-ARIRELrESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
974-1185 |
2.53e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.98 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLI-----PPTSGTAYIDGWDILT---DIKKIR 1045
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSpdvDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDLLTVREHLEFFARLKGAAD--ETIDIEIERMLDDLML----TNKRDNYSTELSGGMKRKLSIAIAF 1119
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1120 CANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
974-1167 |
3.13e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.66 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDiKKIRQN----IG 1049
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-AD-ARHRRAvcprIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQ---HNvLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTV 1126
Cdd:NF033858 80 YMPQglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2041616051 1127 ILDEPTAGVDPFARRSIWDLLLKYKQGR---TIIISTHFMDEAD 1167
Cdd:NF033858 159 ILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAE 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1982-2194 |
4.52e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 91.41 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1982 FGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL----KDIDGVHRNLGYCPQFDAL 2057
Cdd:cd03261 10 FGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMGMLFQSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2058 DNLLTAREHLYFYARLRGIKQQN-IPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:cd03261 89 FDSLTVFENVAFPLREHTRLSEEeIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2137 VRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKA 2194
Cdd:cd03261 169 PIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1969-2188 |
5.08e-20 |
|
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: 91.14 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVmEHSVLKDIDGVHRNL 2048
Cdd:cd03300 1 IELENVSKFYG-----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL-DGKDITNLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGS 2188
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
971-1174 |
6.31e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.77 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 971 EVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKST---TWSILTGLIPP--TSGTAYIDGWDIL---TDIK 1042
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPGfrVEGKVTFHGKNLYapdVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1043 KIRQNIGFTPQHNVLFDLlTVREHLEFFARL---KGAADETIdieiERMLDDLML----TNKRDNYSTELSGGMKRKLSI 1115
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPK-SIYDNIAYGARIngyKGDMDELV----ERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1116 AIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIA 1174
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1996-2167 |
7.17e-20 |
|
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: 91.30 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGN-AYVMEHSVLK-DIDGVHRNLGYcpqfdaldnlLTAREHLYFYARL 2073
Cdd:COG1119 26 VKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGeDVWELRKRIGL----------VSPALQLRFPRDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2074 RGIkqqNIpYISG--------------------CLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:COG1119 96 TVL---DV-VLSGffdsiglyreptdeqrerarELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190
....*....|....*....|....*....|....
gi 2041616051 2134 GMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEE 2167
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
983-1166 |
7.71e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 983 YNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdiltdikkiRQNIGFTPQHNVLFDLL- 1061
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1062 -TVRE--------HLEFFARLkGAADETIdieIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPT 1132
Cdd:NF040873 72 lTVRDlvamgrwaRRGLWRRL-TRDDRAA---VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*
gi 2041616051 1133 AGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEA 1166
Cdd:NF040873 148 TGLDAESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
973-1166 |
9.44e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 973 GVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-------LTDIKKIR 1045
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDLLTVREHL-EFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSK 1124
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2041616051 1125 TVILDEPTAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEA 1166
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFA 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
974-1165 |
1.16e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 90.91 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSG-TAYI-----DGWDILtdikKIRQN 1047
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVW----ELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1048 IGFTpqHNVLFDLLTVREHLE------FFARLkGAADETIDIEIER---MLDDLMLTNKRDNYSTELSGGMKRKLSIAIA 1118
Cdd:COG1119 80 IGLV--SPALQLRFPRDETVLdvvlsgFFDSI-GLYREPTDEQRERareLLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 1119 FCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDE 1165
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
974-1185 |
1.56e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDiLTDIKKIRQNIGFTPQ 1053
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1134 GVDPFARR----SIWDLLLKYkqGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK11607 179 ALDKKLRDrmqlEVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
934-1182 |
1.66e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 934 KRTEYLINLEKNQSENTNELDNRVKQRSasiesysdGEVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKS 1013
Cdd:COG0488 284 KALEKLEREEPPRRDKTVEIRFPPPERL--------GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1014 TTWSILTGLIPPTSGTayidgwdiltdikkIRQ----NIGFTPQHNVLFDL-LTVREHleffarLKGAADETIDIEIERM 1088
Cdd:COG0488 356 TLLKLLAGELEPDSGT--------------VKLgetvKIGYFDQHQEELDPdKTVLDE------LRDGAPGGTEQEVRGY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1089 LDDLMLTNKR-DNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKqGrTIIISTH---FMD 1164
Cdd:COG0488 416 LGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdryFLD 493
|
250
....*....|....*...
gi 2041616051 1165 EadlLGDRIAIISSGELR 1182
Cdd:COG0488 494 R---VATRILEFEDGGVR 508
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1968-2178 |
1.79e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwqfGkkFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLkdIDG---- 2043
Cdd:COG1129 4 LLEMRGISKSFG---G--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSG-------EIL--LDGepvr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 --------------VHRNLGYCPQFDALDNLLTARE----HLYFYARLRGIKQQnipyisgcLLKRLGLTLWADRPVRQY 2105
Cdd:COG1129 70 frsprdaqaagiaiIHQELNLVPNLSVAENIFLGREprrgGLIDWRAMRRRARE--------LLARLGLDIDPDTPVGDL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2106 SGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIM 2178
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1969-2197 |
2.56e-19 |
|
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: 94.45 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLikVYGWQfGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSvLKDIDG--VHR 2046
Cdd:COG4987 334 LELEDV--SFRYP-GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD-LRDLDEddLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 NLGYCPQ----FDA--LDNLLTAREHLYFyARLRGikqqnipyisgcLLKRLGLTLWADR-------PV----RQYSGGN 2109
Cdd:COG4987 410 RIAVVPQrphlFDTtlRENLRLARPDATD-EELWA------------ALERVGLGDWLAAlpdgldtWLgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2110 KRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRkeHKSVIITSHSMEECEvLCNRLSIMVAGEFKCFGSV 2189
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTH 553
|
....*...
gi 2041616051 2190 QHLKAKFG 2197
Cdd:COG4987 554 EELLAQNG 561
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1969-2182 |
3.24e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.70 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVL---KDIDGV- 2044
Cdd:COG3842 6 LELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG-------RILldgRDVTGLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 --HRNLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNK-RklsTAIA--L 2119
Cdd:COG3842 74 peKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VALAraL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2120 IGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
974-1185 |
3.44e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.59 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLI-----PPTSGTAYIDGWDILT-DIKKIR-- 1045
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKmDVIELRrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 -----------------QNIGFTPQHNVLfdlltVREHLEFFARLKGAadetidIEIERMLDDLmlTNKRDNYSTELSGG 1108
Cdd:PRK14247 84 vqmvfqipnpipnlsifENVALGLKLNRL-----VKSKKELQERVRWA------LEKAQLWDEV--KDRLDAPAGKLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1109 MKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
974-1186 |
4.43e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.30 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQnIGFTPQ 1053
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEF----FARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:PRK10851 82 HYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1130 EPTAGVDPFARRSIWDLL------LKYkqgrTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
987-1181 |
4.73e-19 |
|
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: 88.70 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQNIGFTPQHNVLFDlLTVRE 1065
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQENVLFN-RSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1066 HLeffARLKGAADETIDIEIERMLDDLMLTNK-RDNYST-------ELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDP 1137
Cdd:cd03252 95 NI---ALADPGMSMERVIEAAKLAGAHDFISElPEGYDTivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2041616051 1138 FARRSIWDLLLKYKQGRTIIISTHFMdEADLLGDRIAIISSGEL 1181
Cdd:cd03252 172 ESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRI 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
989-1161 |
4.75e-19 |
|
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: 88.75 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDlLTVREHL 1067
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFD-GTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1068 EFfarlkGAADETiDIEIERM-----LDDL--MLTNKRD----NYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:cd03249 98 RY-----GKPDAT-DEEVEEAakkanIHDFimSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180
....*....|....*....|....*
gi 2041616051 1137 PFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:cd03249 172 AESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
974-1186 |
4.97e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.79 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLC-KYYNN--KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwDILT--DIKKIRQNI 1048
Cdd:PRK13650 5 IEVKNLTfKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTeeNVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1049 GFTPQH-NVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVI 1127
Cdd:PRK13650 84 GMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1128 LDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEAdLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
987-1186 |
5.80e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 5.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQH--------NVL 1057
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLRKHIGIVFQNpdnqfvgsIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1058 FDlltVREHLEFFArlkgAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDP 1137
Cdd:PRK13648 103 YD---VAFGLENHA----VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1138 FARRSIWDLLLKYKQGR--TIIISTHFMDEAdLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGT 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1969-2182 |
7.13e-19 |
|
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: 88.39 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLK--------- 2039
Cdd:cd03256 1 IEVENLSKTYP----NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkalrql 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2040 --DIDGVHRNLGYCPQFDALDNLLTAR--EHLYFYARLRGIKQQNIPYISGCLlKRLGLTLWADRPVRQYSGGNKRKLST 2115
Cdd:cd03256 77 rrQIGMIFQQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPKEEKQRALAAL-ERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 2116 AIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1988-2194 |
1.20e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 88.26 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKD--IDGVHRNLGYCpqFDALDNLL---T 2062
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEenLWEIRKKVGMV--FQNPDNQFvgaT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2063 AREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRF 2142
Cdd:TIGR04520 95 VEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2143 LWDCILTLTRKEHKSVIITSHSMEECeVLCNRLSIMVAGEFK-------CFGSVQHLKA 2194
Cdd:TIGR04520 175 VLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVaegtpreIFSQVELLKE 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
974-1185 |
1.30e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.77 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDG--WDILTDIKKIRQNIGFT 1051
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLeFFARL---KGAADETID-----IEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANS 1123
Cdd:PRK09700 86 YQELSVIDELTVLENL-YIGRHltkKVCGVNIIDwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1124 KTVILDEPTAG-----VDP-FArrsIWDLLlkYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK09700 165 KVIIMDEPTSSltnkeVDYlFL---IMNQL--RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
974-1161 |
1.33e-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: 87.29 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNK--LALKNLSVKFYQNQITSFLGRNGAGKSTtwsiLTGLIP----PTSGTAYIDGWDILT-DIKKIRQ 1046
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKST----LVNLIPrfydVDSGRILIDGHDVRDyTLASLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1047 NIGFTPQHNVLFDLlTVREHLEFFARlkGAADETIdIEIERM--LDDLmLTNKRDNYSTE-------LSGGMKRKLSIAI 1117
Cdd:cd03251 77 QIGLVSQDVFLFND-TVAENIAYGRP--GATREEV-EEAARAanAHEF-IMELPEGYDTVigergvkLSGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2041616051 1118 AFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
970-1187 |
1.63e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLCKYY---NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGW------DIL-T 1039
Cdd:PRK14246 4 GKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFqI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1040 DIKKIRQNIGFTPQHNVLFDLLTVREHLEFFARLKGAADETidiEIERMLDDLM--------LTNKRDNYSTELSGGMKR 1111
Cdd:PRK14246 84 DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKR---EIKKIVEECLrkvglwkeVYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1112 KLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTS 1187
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
992-1179 |
2.49e-18 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 86.01 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 992 LSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFTPQHNVLFDLLTVREHLEFFA 1071
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1072 ----RLKGAADETIDIEIERM-LDDLMLTNKRdnystELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDL 1146
Cdd:cd03298 96 spglKLTAEDRQAIEVALARVgLAGLEKRLPG-----ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2041616051 1147 LLKY--KQGRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:cd03298 171 VLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
974-1202 |
2.92e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.24 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFTPQ 1053
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1134 GVDpFARRSIWDLLLKYKQ---GRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSmflKRKYAEGYNLIV 1202
Cdd:PRK09452 174 ALD-YKLRKQMQNELKALQrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP---REIYEEPKNLFV 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
975-1197 |
3.07e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKKIRQNIGFTPQH 1054
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KPVEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1135 VDPFARRSIWDLLLK--YKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT-SMFLKRKYAEG 1197
Cdd:PRK11248 159 LDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERlPLNFARRFVAG 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
988-1186 |
3.19e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDgwDILT-------DIKKIRQNIGFTPQ--HNVLF 1058
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVsstskqkEIKPVRKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 DLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNK-RDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDP 1137
Cdd:PRK13643 99 EE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1138 FARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13643 178 KARIEMMQLFESIHQsGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1981-2181 |
3.85e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 85.42 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVmEHSVLKDID-GVH-----RNLGYCPQF 2054
Cdd:cd03297 5 DIEKRLPDFTLKIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFDSRkKINlppqqRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2055 DALDNLLTAREHLYFYARLRGIKQQNIPYISgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTG 2134
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRNREDRISVDE--LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2135 MDVRAKrflwDCILTLTRKEHKS----VIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:cd03297 162 LDRALR----LQLLPELKQIKKNlnipVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
983-1185 |
4.16e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 983 YNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIltDIKK-----IRQNIGFT---PQH 1054
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL--DYSKrgllaLRQQVATVfqdPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDllTVREHLEFFARLKGAADEtidiEIERMLDDLMLTNKRDNYSTE----LSGGMKRKLSIAIAFCANSKTVILDE 1130
Cdd:PRK13638 89 QIFYT--DIDSDIAFSLRNLGVPEA----EITRRVDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1131 PTAGVDPFARRSIWDLLLK-YKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1988-2181 |
4.40e-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: 85.33 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLkdIDGV----------HRNLGYCPQfdal 2057
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSG-------SVL--LDGTdirqldpadlRRNIGYVPQ---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2058 DNLLtarehlyFYARLRgikqQNI----PYISGCLL----KRLGLTLWA-------DRPV----RQYSGGNKRKLSTAIA 2118
Cdd:cd03245 86 DVTL-------FYGTLR----DNItlgaPLADDERIlraaELAGVTDFVnkhpnglDLQIgergRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2119 LIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRkeHKSVIITSH--SMEEcevLCNRLSIMVAG 2181
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHrpSLLD---LVDRIIVMDSG 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1968-2188 |
5.46e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYgwqfgKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEH--SVLKDIDGVH 2045
Cdd:PRK10895 3 TLTAKNLAKAY-----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 RNLGYCPQ----------FDALDNLLTAREHLYFYARLRGIKQqnipyisgcLLKRLGLTLWADRPVRQYSGGNKRKLST 2115
Cdd:PRK10895 78 RGIGYLPQeasifrrlsvYDNLMAVLQIRDDLSAEQREDRANE---------LMEEFHIEHLRDSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 2116 AIALIGNPSVIFMDEPTTGMD----VRAKRflwdcILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGS 2188
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDpisvIDIKR-----IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1971-2190 |
8.05e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 8.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1971 MTDLIKVYGwqFGKKF---TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV--MEHSVLKDIDGVH 2045
Cdd:PRK09700 2 ATPYISMAG--IGKSFgpvHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInnINYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 RNLGYCPQFDALDNLLTAREHLYFyARLRGIKQQNIPYI--------SGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAI 2117
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLYI-GRHLTKKVCGVNIIdwremrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2118 ALIGNPSVIFMDEPTTGMDVRAKRFLWdCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQ 2190
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1981-2163 |
8.60e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAyvmehSVLKDIDgvhrnLGYCPQFDALDNL 2060
Cdd:COG0488 7 SFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----SIPKGLR-----IGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 LTAREHLYF-YARLRGIKQQ-------------------------------NIPYISGCLLKRLGLTLW-ADRPVRQYSG 2107
Cdd:COG0488 76 LTVLDTVLDgDAELRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEdLDRPVSELSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2108 GNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCIltltRKEHKSVIITSH 2163
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSH 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1978-2194 |
9.70e-18 |
|
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: 84.41 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1978 YGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVL---KDIDG------VHRNL 2048
Cdd:cd03224 10 YG-----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSG-------SIRfdgRDITGlppherARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQ----FDAL---DNLLTARehlyfYARLRGIKQQNIPYISGcLLKRLGlTLWaDRPVRQYSGGNKRKLSTAIALIG 2121
Cdd:cd03224 78 GYVPEgrriFPELtveENLLLGA-----YARRRAKRKARLERVYE-LFPRLK-ERR-KQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2122 NPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKA 2194
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
975-1180 |
1.34e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.42 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKfyQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILtdikkiRQNIGFTP-- 1052
Cdd:COG3840 3 RLDDLTYRYGDFPLRFDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT------ALPPAERPvs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 ---QHNVLFDLLTVREH--LEFFARLK-GAADETidiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTV 1126
Cdd:COG3840 75 mlfQENNLFPHLTVAQNigLGLRPGLKlTAEQRA---QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1127 ILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVdeLCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1967-2183 |
1.79e-17 |
|
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: 88.32 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1967 DVLRMTDLIKVYGWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV-------------- 2032
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2033 MEHSVLKDIDGV-HRNLGYCPQFDALDNLLTA--REHLYFYARLRGIKqqnipyisgcLLKRLGLT-----LWADRPVRQ 2104
Cdd:TIGR03269 358 DGRGRAKRYIGIlHQEYDLYPHRTVLDNLTEAigLELPDELARMKAVI----------TLKMVGFDeekaeEILDKYPDE 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2105 YSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEF 2183
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
978-1182 |
2.34e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDgwdiltdiKKIRqnIGFTPQHNVL 1057
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP--------KGLR--IGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1058 FDLLTVREH----------------------------LEFFARLKGAADE----TIDIEIERMLDDLMLTnkRDNYS--- 1102
Cdd:COG0488 73 DDDLTVLDTvldgdaelraleaeleeleaklaepdedLERLAELQEEFEAlggwEAEARAEEILSGLGFP--EEDLDrpv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1103 TELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDpfaRRSI-W--DLLLKYKqGrTIIISTH---FMDEadlLGDRIAII 1176
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIeWleEFLKNYP-G-TVLVVSHdryFLDR---VATRILEL 222
|
....*.
gi 2041616051 1177 SSGELR 1182
Cdd:COG0488 223 DRGKLT 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1969-2192 |
2.51e-17 |
|
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: 83.38 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPL-----TSGNAYVMEHSVLKDIDG 2043
Cdd:cd03260 1 IELRDLNVYYG-----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 V---HRNLGYCPQ----FDAldnllTAREHLYFYARLRGIK-QQNIPYISGCLLKRLGLtlW---ADRP-VRQYSGGNKR 2111
Cdd:cd03260 76 VlelRRRVGMVFQkpnpFPG-----SIYDNVAYGLRLHGIKlKEELDERVEEALRKAAL--WdevKDRLhALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2112 KLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHkSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQH 2191
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEY-TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 2041616051 2192 L 2192
Cdd:cd03260 227 I 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1006-1161 |
2.97e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.41 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1006 GRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQHNVLFDLLTVREHLEFFARLKGAADETIdiei 1085
Cdd:TIGR01189 33 GPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFWAAIHGGAQRTI---- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1086 ERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTH 1161
Cdd:TIGR01189 109 EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlARGGIVLLTTH 185
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1983-2188 |
4.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.98 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1983 GKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV--MEHSVLKDIDGVHRNLGYCpqFDALDNL 2060
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgLDTSDEENLWDIRNKAGMV--FQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 LTA---REHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDV 2137
Cdd:PRK13633 98 IVAtivEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2138 RAKRFLWDCILTLTRKEHKSVIITSHSMEECeVLCNRLSIMVAGEFKCFGS 2188
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
969-1181 |
4.79e-17 |
|
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: 82.07 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 969 DGEVgvEIINLCKYYNNKL--ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIR 1045
Cdd:cd03369 4 HGEI--EVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDlLTVREHLEFFarlkgaaDETIDIEIermLDDLMLTNKRDNysteLSGGMKRKLSIAIAFCANSKT 1125
Cdd:cd03369 82 SSLTIIPQDPTLFS-GTIRSNLDPF-------DEYSDEEI---YGALRVSEGGLN----LSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1126 VILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDE-ADLlgDRIAIISSGEL 1181
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEV 201
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
978-1181 |
5.81e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTD---IKKIRQNIGFTPQH 1054
Cdd:PRK11614 10 KVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDwqtAKIMREAVAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLTVREHLE---FFARlkgaaDETIDIEIERMLDDL-MLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDE 1130
Cdd:PRK11614 89 RRVFSRMTVEENLAmggFFAE-----RDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1131 PTAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1985-2161 |
6.62e-17 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 81.54 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1985 KFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLT---SGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNLL 2061
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 TAREHLYFYARLRGikqqnipyisgcllkrlgltlwaDRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD-VRAK 2140
Cdd:cd03233 99 TVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDsSTAL 155
|
170 180
....*....|....*....|.
gi 2041616051 2141 RFLwDCILTLTRKEHKSVIIT 2161
Cdd:cd03233 156 EIL-KCIRTMADVLKTTTFVS 175
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
984-1181 |
8.79e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 80.34 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 984 NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQNIGFTPQHNVLFDllt 1062
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGYLPQDDELFS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1063 vrehleffarlkGAADETIdieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRS 1142
Cdd:cd03246 90 ------------GSIAENI-----------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 1143 IWDLL--LKyKQGRTIIISTHFMdEADLLGDRIAIISSGEL 1181
Cdd:cd03246 135 LNQAIaaLK-AAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1986-2235 |
8.92e-17 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 82.88 E-value: 8.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1986 FTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV-------------------------------ME 2034
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgrditakkkkklkdlrkkvglvfqfpehqlFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2035 HSVLKDIDGVHRNLGYCPQfdaldnllTAREHLYFYARLRGIKQQnipyisgcLLKRLGLTLwadrpvrqySGGNKRKLs 2114
Cdd:TIGR04521 98 ETVYKDIAFGPKNLGLSEE--------EAEERVKEALELVGLDEE--------YLERSPFEL---------SGGQMRRV- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2115 tAIA--LIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHL 2192
Cdd:TIGR04521 152 -AIAgvLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2041616051 2193 kakFGDGytiilrtnavadiDTLTQYIIeHLPEAT-----LKEKHNKV 2235
Cdd:TIGR04521 231 ---FSDV-------------DELEKIGL-DVPEITelarkLKEKGLPV 261
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
991-1181 |
1.09e-16 |
|
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: 81.65 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 991 NLSVKfyQNQITSFLGRNGAGKSTTWSILTGLIPP----TSGTAYIDGWDILT------DIKKIRQN--IGFTPQHNVLF 1058
Cdd:TIGR02770 6 NLSLK--RGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPlsirgrHIATIMQNprTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 DLL-TVREHLEFFARLKGAADETIDI----EIERMLDdlmltnkrdNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:TIGR02770 84 HAIeTLRSLGKLSKQARALILEALEAvglpDPEEVLK---------KYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1134 GVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:TIGR02770 155 DLDVVNQARVLKLLreLRQLFGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
970-1186 |
1.15e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLCKYY--NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQ 1046
Cdd:PRK11160 335 DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1047 NIGFTPQHNVLFDLlTVREHLEFfarlkgAADETIDIEIERM-----LDDLMLTNKR-DNYSTE----LSGGMKRKLSIA 1116
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLL------AAPNASDEALIEVlqqvgLEKLLEDDKGlNAWLGEggrqLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1117 IAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHfmdeaDLLG----DRIAIISSGELRCVGT 1186
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH-----RLTGleqfDRICVMDNGQIIEQGT 556
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
973-1182 |
1.34e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 973 GVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLiPPTSGTAYIDG---------WDILTDIKK 1043
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrveffnqniYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1044 IRQNIGFT-PQHNvLFDLlTVREHLEFFARLKGAADET-IDIEIERMLDDLML----TNKRDNYSTELSGGMKRKLSIAI 1117
Cdd:PRK14258 86 LRRQVSMVhPKPN-LFPM-SVYDNVAYGVKIVGWRPKLeIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1118 AFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELR 1182
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
988-1186 |
1.54e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.54 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIK--KIRQNIGFTPQHNVLFDLlTVRE 1065
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL-ADYTlaSLRRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1066 HLEFfarlkGAADETIDIEIERMLDDLMLTNKRDNY-----------STELSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:TIGR02203 425 NIAY-----GRTEQADRAEIERALAAAYAQDFVDKLplgldtpigenGVLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1135 VDPFARRSIWDLLLKYKQGRTIIISTHFMDEADlLGDRIAIISSGELRCVGT 1186
Cdd:TIGR02203 500 LDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGT 550
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1996-2137 |
1.67e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.23 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNLLTAREHLYFYARLRG 2075
Cdd:cd03231 23 LAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHS 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2076 ikqqnipyISGCL--LKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDV 2137
Cdd:cd03231 103 --------DEQVEeaLARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
973-1185 |
2.28e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.54 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 973 GVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwDILTDIKKIRQNIGFTP 1052
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-KRMNDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPT 1132
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1133 AGVDPFAR---RSIWDLLLKyKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK11000 162 SNLDAALRvqmRIEISRLHK-RLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1968-2182 |
2.66e-16 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 81.03 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGWQFGkkftaVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNA-YVM----EHSVLKDID 2042
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG-----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMrsgaELELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2043 GVHRNL-----GYCPQfDALDNL-LTAREHLYFYARLRGIKQQ---NIPYISGCLLKR--LGLTLWADRPvRQYSGGNKR 2111
Cdd:TIGR02323 78 AERRRLmrtewGFVHQ-NPRDGLrMRVSAGANIGERLMAIGARhygNIRATAQDWLEEveIDPTRIDDLP-RAFSGGMQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2112 KLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGR 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
974-1180 |
2.74e-16 |
|
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: 77.87 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGtayidgwdILTDIKKIRqnIGFTPQ 1053
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG--------IVTWGSTVK--IGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 hnvlfdlltvrehleffarlkgaadetidieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1134 GVDPFARRSIWDLLLKYKqgRTIIISTH---FMDEadlLGDRIAIISSGE 1180
Cdd:cd03221 100 HLDLESIEALEEALKEYP--GTVILVSHdryFLDQ---VATKIIELEDGK 144
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
974-1166 |
2.90e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.44 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDG--WDILT-----DIKKIRQ 1046
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKtpsdkAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1047 NIGFTPQHNVLFDLLTVREHL-EFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKT 1125
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2041616051 1126 VILDEPTAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEA 1166
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVA 204
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
999-1186 |
3.29e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 82.85 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 999 NQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKI-----RQNIGFTPQHNVLFDLLTVREHLEFfaRL 1073
Cdd:TIGR02142 23 QGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRGNLRY--GM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1074 KGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYK 1151
Cdd:TIGR02142 101 KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLerLHAE 180
|
170 180 190
....*....|....*....|....*....|....*
gi 2041616051 1152 QGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:TIGR02142 181 FGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1981-2188 |
4.46e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 80.08 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKkFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGNAYVMEhsvlKDIDGVH---RNLGYCPQFDA 2056
Cdd:cd03296 11 RFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERP-DSGTILFGG----EDATDVPvqeRNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2057 LDNLLTAREHLYFYARLRGIKQ----QNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPT 2132
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2133 TGMDVRAKRFL--WdciltlTRKEHKSVIITS----HSMEECEVLCNRLSIMVAGEFKCFGS 2188
Cdd:cd03296 165 GALDAKVRKELrrW------LRRLHDELHVTTvfvtHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1996-2181 |
4.88e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.29 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDidGVHRnlGYCPQFDALDNLLTAREHLYFYARLRG 2075
Cdd:COG4525 30 IESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP--GADR--GVVFQKDALLPWLNVLDNVAFGLRLRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2076 IKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEH 2155
Cdd:COG4525 106 VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTG 185
|
170 180
....*....|....*....|....*.
gi 2041616051 2156 KSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:COG4525 186 KGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1971-2172 |
5.02e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1971 MTDLI--KVYGWQFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayVMEHSVLKDIdgvhrnl 2048
Cdd:PRK09544 1 MTSLVslENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG---VIKRNGKLRI------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNL--LTAREHLyfyaRLR-GIKQQNIpyisGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSV 2125
Cdd:PRK09544 70 GYVPQKLYLDTTlpLTVNRFL----RLRpGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2126 IFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSM-----EECEVLC 2172
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaKTDEVLC 193
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1990-2139 |
6.11e-16 |
|
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: 78.44 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1990 NNICAGVKQGECFGLLGINGSGKSTTFKMLTGEipltsGNAYVMEHSVLkdIDG------VHRNLGYCPQFDALDNLLTA 2063
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGR-----KTAGVITGEIL--INGrpldknFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2064 REHLYFYARLRGIKQQNipyisgcllkrlgltlwadrpvrqysggnKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:cd03232 97 REALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
987-1185 |
6.26e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVKFYQNQITS-------------FLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQNIGFTP 1052
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDgvdlsvregslvgLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVL---FDLLTVRE-----HLEFFARlkgaADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSK 1124
Cdd:PRK09536 84 QDTSLsfeFDVRQVVEmgrtpHRSRFDT----WTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1125 TVILDEPTAGVDpfARRSIWDLLLKYK---QGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK09536 160 VLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1988-2178 |
7.06e-16 |
|
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: 77.42 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSvLKDIDG--VHRNLGYCPQ----FDA--LDN 2059
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRDLDLesLRKNIAYVPQdpflFSGtiREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2060 LLtarehlyfyarlrgikqqnipyisgcllkrlgltlwadrpvrqySGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:cd03228 96 IL--------------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 2041616051 2140 KRFLWDCILTLTRKehKSVIITSHSMEECEvLCNRLSIM 2178
Cdd:cd03228 132 EALILEALRALAKG--KTVIVIAHRLSTIR-DADRIIVL 167
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1968-2182 |
7.35e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 81.25 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIP---LTSGNAYV-------MEHSV 2037
Cdd:COG0444 1 LLEVRNLKVYFP-TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFdgedllkLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2038 LKDIDGvhRNLGYCPQ--FDALDNLLTAREHL-----YFY------ARLRGIKqqnipyisgcLLKRLGLTLWADRpVRQ 2104
Cdd:COG0444 80 LRKIRG--REIQMIFQdpMTSLNPVMTVGDQIaeplrIHGglskaeARERAIE----------LLERVGLPDPERR-LDR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2105 Y----SGGNKRKLSTAIALIGNPSVIFMDEPTTGMDV--RAKrflwdcILTL----TRKEHKSVIITSHSMEECEVLCNR 2174
Cdd:COG0444 147 YphelSGGMRQRVMIARALALEPKLLIADEPTTALDVtiQAQ------ILNLlkdlQRELGLAILFITHDLGVVAEIADR 220
|
....*...
gi 2041616051 2175 LSIMVAGE 2182
Cdd:COG0444 221 VAVMYAGR 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
974-1179 |
8.23e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.41 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTD---------IKKI 1044
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1045 RQNIGFTPQHNVLFDLLTVREH-LEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANS 1123
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1124 KTVILDEPTAGVDPfarRSIWDLLLKYKQ----GRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:PRK11264 164 EVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
978-1186 |
8.66e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.43 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDiLTDIK-----KIRqniGFTP 1052
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSpaelaRRR---AVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVL-FDlLTVREHLEF----FARLKGAADETIDieieRMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFC------A 1121
Cdd:PRK13548 83 QHSSLsFP-FTVEEVVAMgrapHGLSRAEDDALVA----AALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1122 NSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1968-2226 |
9.78e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 9.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAyvmehSVL-KDI-DGVH 2045
Cdd:NF033858 1 VARLEGVSHRYG-----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-----EVLgGDMaDARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 RN-----LGYCPQfdAL-DNL---LTAREHLYFYARLRGI----KQQNIpyisGCLLKRLGLTLWADRPVRQYSGGNKRK 2112
Cdd:NF033858 71 RRavcprIAYMPQ--GLgKNLyptLSVFENLDFFGRLFGQdaaeRRRRI----DELLRATGLAPFADRPAGKLSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2113 LSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHK--SVIITSHSMEECEvLCNRLSIMVAGEFKCFGSVQ 2190
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRI-RAERPgmSVLVATAYMEEAE-RFDWLVAMDAGRVLATGTPA 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 2041616051 2191 HLKAkfgdgytiilRTNAvadiDTLTQYIIEHLPEA 2226
Cdd:NF033858 223 ELLA----------RTGA----DTLEAAFIALLPEE 244
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1987-2181 |
1.16e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKdidGVHRNL-GYCPQFDALD-NLLTAR 2064
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLvAYVPQSEEVDwSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 EHLYFYAR------LRGIKQQNIPYISGClLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVR 2138
Cdd:PRK15056 98 EDVVMMGRyghmgwLRRAKKRDRQIVTAA-LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2041616051 2139 AKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNrLSIMVAG 2181
Cdd:PRK15056 177 TEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
929-1181 |
1.28e-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: 83.25 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 929 VNKIRKRTEYLINLEKNQSENTNELDNRVKQRSASIESYSDGevgveiinlckyYNNKlALKNLSVKFYQNQITSFLGRN 1008
Cdd:TIGR01193 443 VANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYG------------YGSN-ILSDISLTIKMNSKTTIVGMS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1009 GAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDLlTVREHLEFFARLKGAADET------- 1080
Cdd:TIGR01193 510 GSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQDEIwaaceia 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1081 -IDIEIERMldDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQgRTIIIS 1159
Cdd:TIGR01193 589 eIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFV 665
|
250 260
....*....|....*....|..
gi 2041616051 1160 THFMDEADLLgDRIAIISSGEL 1181
Cdd:TIGR01193 666 AHRLSVAKQS-DKIIVLDHGKI 686
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1969-2182 |
1.31e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.20 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGWQFGkkftavnniCAGVK----QGECFGLLGINGSGKSTTFKMLTGEIPLTSGNA-YVMEHSVLKDIDG 2043
Cdd:PRK11701 7 LSVRGLTKLYGPRKG---------CRDVSfdlyPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 V----HRNL-----GYCPQfDALDNL----------------LTAReHlyfYARLRGIKQQ-----NIPyisgclLKRLG 2093
Cdd:PRK11701 78 LseaeRRRLlrtewGFVHQ-HPRDGLrmqvsaggnigerlmaVGAR-H---YGDIRATAGDwlervEID------AARID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2094 ltlwaDRPvRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCN 2173
Cdd:PRK11701 147 -----DLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAH 220
|
....*....
gi 2041616051 2174 RLSIMVAGE 2182
Cdd:PRK11701 221 RLLVMKQGR 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1983-2196 |
1.32e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 79.09 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1983 GKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNayVMEHSvlkDIDGVHRNLGycpqfdaLDNLLT 2062
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK--VDRNG---EVSVIAISAG-------LSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2063 AREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEpttGMDVRAKRF 2142
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2143 LWDCILTLT--RKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKF 2196
Cdd:PRK13546 179 AQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1987-2167 |
1.82e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.89 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLKdidGVHRNLGYCPQFDALDNLL--TAR 2064
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRR---AGGARVAYVPQRSEVPDSLplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 E--HLYFYAR---LRGIKQQNIPYISGCLlKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:NF040873 76 DlvAMGRWARrglWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....*...
gi 2041616051 2140 KRFLWDcILTLTRKEHKSVIITSHSMEE 2167
Cdd:NF040873 155 RERIIA-LLAEEHARGATVVVVTHDLEL 181
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
989-1181 |
2.75e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.60 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTD-IKKIRQNIGFTPQH-NVLFDLLTVREH 1066
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1067 LEFFARLKGAADETIdieIERMLDDLMLTNKRDNYSTE---LSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSI 1143
Cdd:PRK13642 103 VAFGMENQGIPREEM---IKRVDEALLAVNMLDFKTREparLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2041616051 1144 WDLL--LKYKQGRTIIISTHFMDEAdLLGDRIAIISSGEL 1181
Cdd:PRK13642 180 MRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1967-2132 |
2.96e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1967 DVLRMTDLIKVYGwqfGKKFtaVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVmehsvlkdidGVHR 2046
Cdd:COG0488 314 KVLELEGLSKSYG---DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----------GETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 NLGYCPQ-FDALDNLLTAREHLyfyarLRGIKQQNIPYISGcLLKRLGLTlwADR---PVRQYSGGNKRKLSTAIALIGN 2122
Cdd:COG0488 379 KIGYFDQhQEELDPDKTVLDEL-----RDGAPGGTEQEVRG-YLGRFLFS--GDDafkPVGVLSGGEKARLALAKLLLSP 450
|
170
....*....|
gi 2041616051 2123 PSVIFMDEPT 2132
Cdd:COG0488 451 PNVLLLDEPT 460
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
693-900 |
3.08e-15 |
|
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: 79.74 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 693 NAVSRMLPLFMVLGWIFTVSMNVKDIVHEKEKRLKEIMKIMGLYDTVHWFSWFIWCSFIMMITAIFLVLIIKYGNITrFS 772
Cdd:pfam12698 158 GYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIP-FG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 773 NFLILLIFFLCFTFATITQCFLMSVFFNRANLAACGAGILFFLLYLPYTVLLNYSDVTLRWHKIISCLSSTvAFGIGCdy 852
Cdd:pfam12698 237 NLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFF-SPIDGL-- 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2041616051 853 iakweerakgiqwDNINKGtrpADNFSFLYCMIMMLIDSIIYMFFTWY 900
Cdd:pfam12698 314 -------------LRLIYG---DSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
986-1181 |
3.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.30 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 986 KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAY---IDGWDILTD-IKKIRQNIGFTPQH-NVLFDL 1060
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTAKtVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 LTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFAR 1140
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2041616051 1141 RSIWDLL--LKYKQGRTIIISTHFMDEADlLGDRIAIISSGEL 1181
Cdd:PRK13640 180 EQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
974-1166 |
5.12e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKL-----ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTD-------- 1040
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1041 -----------------IKKIRQNIGFTPQ--HNVLFDLlTVREHLEFFARLKGAADETidiEIERMLDDLMLTNKRDNY 1101
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEE---AKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1102 ----STELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLK-YKQGRTIIISTHFMDEA 1166
Cdd:PRK13651 159 lqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNV 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1990-2136 |
6.15e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.86 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1990 NNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPL-TSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNLLTAREHLY 2068
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2069 FYARLR-------GIKQQNIPYIsgclLKRLGLTLWAD------RPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGM 2135
Cdd:TIGR00955 122 FQAHLRmprrvtkKEKRERVDEV----LQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
.
gi 2041616051 2136 D 2136
Cdd:TIGR00955 198 D 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1968-2182 |
6.18e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.25 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIP--------LTSGNAYVMEH---S 2036
Cdd:TIGR02633 1 LLEMKGIVKTFG-----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiYWSGSPLKASNirdT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2037 VLKDIDGVHRNLGYCPQFDALDNLLTAREhlyfyARLRGIKQQNIPYISGC--LLKRLGLTLWAD-RPVRQYSGGNKRKL 2113
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELSVAENIFLGNE-----ITLPGGRMAYNAMYLRAknLLRELQLDADNVtRPVGDYGGGQQQLV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2114 STAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIItSHSMEECEVLCNRLSIMVAGE 2182
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYI-SHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1000-1161 |
6.65e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.36 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1000 QITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIR-----QNIGFTPQHNVLFDLLTVREHLEFFARLK 1074
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALENVELPALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1075 GAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQ 1152
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNREH 196
|
....*....
gi 2041616051 1153 GRTIIISTH 1161
Cdd:PRK10584 197 GTTLILVTH 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
966-1181 |
6.87e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 966 SYSDGEVGVEIinlckyynnklaLKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DI 1041
Cdd:PRK10535 13 SYPSGEEQVEV------------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1042 KKI-RQNIGFTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFc 1120
Cdd:PRK10535 81 AQLrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1121 ANSKTVIL-DEPTAGVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADlLGDRIAIISSGEL 1181
Cdd:PRK10535 160 MNGGQVILaDEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1988-2182 |
7.12e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKD-IDGVHRNLGYCpqFDALDNL---LTA 2063
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGII--FQNPDNQfigATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2064 REHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFL 2143
Cdd:PRK13632 102 EDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 2041616051 2144 WDCILTLTRKEHKSVIITSHSMEECeVLCNRLSIMVAGE 2182
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGK 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
978-1170 |
7.22e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.39 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNN-KL---ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKK--IR-QNI 1048
Cdd:PRK11629 10 NLCKRYQEgSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMskLSSAAKaeLRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1049 GFTPQ-HNVLFDLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVI 1127
Cdd:PRK11629 90 GFIYQfHHLLPDF-TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2041616051 1128 LDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLG 1170
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
989-1161 |
8.00e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.22 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQHNVLFDLLTVREHLE 1068
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1069 FFARLKGaadetiDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLL 1148
Cdd:cd03231 96 FWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....
gi 2041616051 1149 KY-KQGRTIIISTH 1161
Cdd:cd03231 170 GHcARGGMVVLTTH 183
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
974-1181 |
8.89e-15 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 76.41 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTA-YIDGWDILTDIKKI-------- 1044
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELELYQLseaerrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1045 -RQNIGFTPQH-------------NVLFDLLTV-REHlefFARLKGAADETID-IEIERmlddlmltNKRDNYSTELSGG 1108
Cdd:TIGR02323 84 mRTEWGFVHQNprdglrmrvsagaNIGERLMAIgARH---YGNIRATAQDWLEeVEIDP--------TRIDDLPRAFSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1109 MKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1969-2131 |
9.57e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.19 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDIDGV---H 2045
Cdd:COG3839 4 LELENVSKSYG-----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTDLppkD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 RNLGYCPQFDAL-DNLlTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPS 2124
Cdd:COG3839 75 RNIAMVFQSYALyPHM-TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
....*..
gi 2041616051 2125 VIFMDEP 2131
Cdd:COG3839 154 VFLLDEP 160
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
974-1181 |
1.07e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 75.59 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNK---LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQNIG 1049
Cdd:cd03248 12 VKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDlLTVREHLEFfaRLKGAADETIDIEIERMLDDLMLTNKRDNYSTE-------LSGGMKRKLSIAIAFCAN 1122
Cdd:cd03248 92 LVGQEPVLFA-RSLQDNIAY--GLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1123 SKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADlLGDRIAIISSGEL 1181
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
982-1181 |
1.17e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 982 YYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL----TDIKKIRQNIGFTPQ-HNV 1056
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQIGMIFQdHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1057 LFDLlTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAfCANSKTVIL-DEPTAGV 1135
Cdd:PRK10908 91 LMDR-TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARA-VVNKPAVLLaDEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2041616051 1136 DPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK10908 169 DDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1996-2178 |
1.25e-14 |
|
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: 79.88 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSvLKDID--GVHRNLGYCPQ----FDA--LDNLLTAR--- 2064
Cdd:COG2274 498 IKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID-LRQIDpaSLRRQIGVVLQdvflFSGtiRENITLGDpda 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 --EHLYFYARLRGIKQ--QNIPyisgcllkrLGLtlwaDRPV----RQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:COG2274 577 tdEEIIEAARLAGLHDfiEALP---------MGY----DTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2041616051 2137 VRAKRFLWDCILTLTRKehKSVIITSHsmeecevlcnRLSIM 2178
Cdd:COG2274 644 AETEAIILENLRRLLKG--RTVIIIAH----------RLSTI 673
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1996-2183 |
1.30e-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: 74.01 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYvmehsvlkdIDG--VHRnlgycpqfdaldnlLTAREhlyfyARL 2073
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT---------LDGkpVTR--------------RSPRD-----AIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2074 RGIKqqnipYISGcllKRLGLTLWADRPVR-------QYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDC 2146
Cdd:cd03215 75 AGIA-----YVPE---DRKREGLVLDLSVAenialssLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRL 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 2041616051 2147 ILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEF 2183
Cdd:cd03215 147 IREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
974-1190 |
1.51e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.45 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDiKKIRQ-NIGFTP 1052
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-TH-RSIQQrDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPT 1132
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1133 AGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVGT---------SMFL 1190
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFM 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
985-1161 |
1.63e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 74.20 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 985 NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGliPPTSGTayIDGwDILTDIKKIRQN----IGFTPQHNVLFDL 1060
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGV--ITG-EILINGRPLDKNfqrsTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 LTVREHLEFFARLKGaadetidieiermlddlmltnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFAR 1140
Cdd:cd03232 94 LTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|..
gi 2041616051 1141 RSIWDLLLKY-KQGRTIIISTH 1161
Cdd:cd03232 145 YNIVRFLKKLaDSGQAILCTIH 166
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
975-1179 |
1.82e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIRQNIGFTP 1052
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIARMGVVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDLLTVRE--------HLE--FFARL------KGAADETIDIEIErMLDDLMLTNKRDNYSTELSGGMKRKLSIA 1116
Cdd:PRK11300 87 QHVRLFREMTVIEnllvaqhqQLKtgLFSGLlktpafRRAESEALDRAAT-WLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1117 IAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
970-1181 |
1.82e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLCKyynnkLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTD--------- 1040
Cdd:PRK10762 254 GEVRLKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglang 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1041 ---IKKIRQNIGFtpqhnVLFdlLTVREH-----LEFFARLKGAadetIDIEIERM-LDDLML-----TNKRDNYSTELS 1106
Cdd:PRK10762 329 ivyISEDRKRDGL-----VLG--MSVKENmsltaLRYFSRAGGS----LKHADEQQaVSDFIRlfnikTPSMEQAIGLLS 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1107 GGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEadLLG--DRIAIISSGEL 1181
Cdd:PRK10762 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1969-2182 |
1.98e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.24 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVY--GWQFGKKftAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV-----MEHSV-LKD 2040
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKK--ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvdiTDKKVkLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2041 IdgvHRNLGYC---PQFDALDNllTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTL--WADRPVRQYSGGNKRKLST 2115
Cdd:PRK13637 81 I---RKKVGLVfqyPEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2116 AIALIGNPSVIFMDEPTTGMDVRAKrflwDCILTLTRKEHK----SVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGR----DEILNKIKELHKeynmTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1991-2171 |
2.08e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1991 NICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlkDIDGVHRNLGYCPQFDALDNLLTAREHLYFY 2070
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2071 ARLRGikqQNIPYISGCLlKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTl 2150
Cdd:PRK13539 98 AAFLG---GEELDIAAAL-EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA- 172
|
170 180
....*....|....*....|....
gi 2041616051 2151 TRKEHKSVIITSHS---MEECEVL 2171
Cdd:PRK13539 173 HLAQGGIVIAATHIplgLPGAREL 196
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1968-2166 |
2.15e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 74.70 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwqfgKKFTAVNNICAGVKQGE-CFgLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLK----DID 2042
Cdd:COG2884 1 MIRFENVSKRYP----GGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2043 GVHRNLGYCPQ-FDALDNlLTAREHLYFYARLRGIK----QQNIPYIsgclLKRLGLTLWADRPVRQYSGGNKRKLSTAI 2117
Cdd:COG2884 76 YLRRRIGVVFQdFRLLPD-RTVYENVALPLRVTGKSrkeiRRRVREV----LDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 2118 ALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSME 2166
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE 198
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
982-1186 |
3.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 982 YYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIRQNIGFTPQH-NVLF 1058
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNpETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 DLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPF 1138
Cdd:PRK13644 91 VGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 1139 ARRSIWDLLLK-YKQGRTIIISTHFMDEADlLGDRIAIISSGELRCVGT 1186
Cdd:PRK13644 171 SGIAVLERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGE 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
989-1181 |
4.82e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.46 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL----TDIKKIRQNI---------GFTPQHN 1055
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldrKQRRAFRRDVqlvfqdspsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1056 VLFdllTVREHLEFFARLKGAADETidiEIERMLDDLML-TNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:TIGR02769 107 VRQ---IIGEPLRHLTSLDESEQKA---RIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 1135 VDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1005-1181 |
4.90e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 74.01 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1005 LGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKKI---------RQNIGFTPQHNVLFDLLTVREH----LEFfA 1071
Cdd:COG4181 44 VGASGSGKSTLLGLLAGLDRPTSGTVRLAG----QDLFALdedararlrARHVGFVFQSFQLLPTLTALENvmlpLEL-A 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1072 RLKGAADETidieiERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LK 1149
Cdd:COG4181 119 GRRDARARA-----RALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLN 193
|
170 180 190
....*....|....*....|....*....|...
gi 2041616051 1150 YKQGRTIIISTHfmDEADLL-GDRIAIISSGEL 1181
Cdd:COG4181 194 RERGTTLVLVTH--DPALAArCDRVLRLRAGRL 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
985-1186 |
6.76e-14 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 77.10 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 985 NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDLlTV 1063
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1064 REHLeffARLKGAADETIdIEIERM--LDDLMLTnKRDNYSTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:COG4618 423 AENI---ARFGDADPEKV-VAAAKLagVHEMILR-LPDGYDTRigeggarLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1135 VDPFARRSIWDLL--LKyKQGRTIIISTH---FMDEAdllgDRIAIISSGELRCVGT 1186
Cdd:COG4618 498 LDDEGEAALAAAIraLK-ARGATVVVITHrpsLLAAV----DKLLVLRDGRVQAFGP 549
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1983-2183 |
7.11e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 7.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1983 GKKF---TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEH-----SVLKDID-GV---HRNLGY 2050
Cdd:PRK11288 11 GKTFpgvKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaSTTAALAaGVaiiYQELHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2051 CPQFDALDNLLTARehlyFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDE 2130
Cdd:PRK11288 91 VPEMTVAENLYLGQ----LPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2131 PTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEF 2183
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1987-2186 |
7.21e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSvLKDIDGVHRNLGYCPQFDALDNLLTAREH 2066
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2067 LYFYARLR---GIKQQNIPYISGCLLKRLGL-----TLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVR 2138
Cdd:PLN03211 161 LVFCSLLRlpkSLTKQEKILVAESVISELGLtkcenTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 2139 AKRFLwdcILTLTRKEHK-SVIITSHSMEECEVLCNRLSIMVAGEFKCF 2186
Cdd:PLN03211 241 AAYRL---VLTLGSLAQKgKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
989-1181 |
8.58e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPtSGTAYIDGWDI----LTDIKKIRqniGFTPQHNVLFDLLTVR 1064
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLsdwsAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1065 EHLEFFARlKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFC-------ANSKTVILDEPTAGVDp 1137
Cdd:COG4138 88 QYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLD- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1138 FARRSIWDLLLKY--KQGRTIIISTHfmdeaDL-----LGDRIAIISSGEL 1181
Cdd:COG4138 166 VAQQAALDRLLRElcQQGITVVMSSH-----DLnhtlrHADRVWLLKQGKL 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
973-1181 |
9.50e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.58 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 973 GVEIINLCKYYNNKLaLKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPP----TSGTAYIDGWDIL------TDIK 1042
Cdd:PRK10418 4 QIELRNIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVApcalrgRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1043 KIRQN--IGFTPqhnvlfdLLTVREH-LEFFARLKGAADETIDIEIermLDDLMLTNKR---DNYSTELSGGMKRKLSIA 1116
Cdd:PRK10418 83 TIMQNprSAFNP-------LHTMHTHaRETCLALGKPADDATLTAA---LEAVGLENAArvlKLYPFEMSGGMLQRMMIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1117 IAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1981-2181 |
1.00e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.18 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKkFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDN 2059
Cdd:COG1118 11 RFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIVLNGRDLFTNLPPRERRVGFVFQHYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2060 LLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:COG1118 89 HMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2041616051 2140 KRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:COG1118 169 RKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
981-1161 |
1.07e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.54 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 981 KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFD 1059
Cdd:PRK13657 343 SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1060 lLTVREHLeffaRLkGAADETiDIEIERMLD-----DLMLTnKRDNYST-------ELSGGMKRKLSIAIAFCANSKTVI 1127
Cdd:PRK13657 423 -RSIEDNI----RV-GRPDAT-DEEMRAAAEraqahDFIER-KPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190
....*....|....*....|....*....|....
gi 2041616051 1128 LDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
975-1186 |
1.08e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 73.23 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDiLTDIK-----KIRqniG 1049
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP-LAAWSpwelaRRR---A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVL-FDlLTVRE--------HleffaRLKGAADETIdieIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFC 1120
Cdd:COG4559 79 VLPQHSSLaFP-FTVEEvvalgrapH-----GSSAAQDRQI---VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1121 -------ANSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
973-1193 |
1.25e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.77 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 973 GVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAgksttwSILTGLIPptsgtAYIDG-------WDILT---DIK 1042
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA------A**RGALP-----AHV*GpdagrrpWRF*TwcaNRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1043 KIRQNIGF-TPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCA 1121
Cdd:NF000106 82 ALRRTIG*hRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1122 NSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLKRK 1193
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
952-1181 |
1.29e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 952 ELDNRVKQRSASIeSYSDGEVGVEIINLCKYYNNKLalKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAY 1031
Cdd:PRK09700 245 ELQNRFNAMKENV-SNLAHETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1032 IDGWDI-----LTDIKKIRQNIGFTPQHNVLFDLLTVREHLEF-----FARLKGA------ADETIDIEIERMLDDLMLT 1095
Cdd:PRK09700 322 LNGKDIsprspLDAVKKGMAYITESRRDNGFFPNFSIAQNMAIsrslkDGGYKGAmglfheVDEQRTAENQRELLALKCH 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1096 NKRDNYsTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIA 1174
Cdd:PRK09700 402 SVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIA 480
|
....*..
gi 2041616051 1175 IISSGEL 1181
Cdd:PRK09700 481 VFCEGRL 487
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1988-2332 |
1.42e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.07 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV------------MEHSVLKDIDGVHRNLGYCPQFD 2055
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdgvdiakisdaeLREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2056 ALDNllTArehlyFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGM 2135
Cdd:PRK10070 123 VLDN--TA-----FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2136 DVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGDGYtiiLRTnAVADIDTL 2215
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY---VRT-FFRGVDIS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2216 TQYIIEHLPEATLKEKHNKVIHFRVTATIKLyemfsvLERARVELSPAIE--DYTVTQVTLDDVFVSFAKYQDVEKDFLN 2293
Cdd:PRK10070 272 QVFSAKDIARRTPNGLIRKTPGFGPRSALKL------LQDEDREYGYVIErgNKFVGAVSIDSLKTALTQQQGLDAALID 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2041616051 2294 ESQAVDG--PVSKISNLTAR------IIQDEQNKIEKPLKRNIFSKL 2332
Cdd:PRK10070 346 APLAVDAqtPLSELLSHVGQapcavpVVDEDQQYVGIISKGMLLRAL 392
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2003-2194 |
1.44e-13 |
|
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: 74.76 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2003 GLLGINGSGKSTTFKMLTGEIPLTSG----NAYVMEHSVLKDIDGVH-RNLGYCPQFDALDNLLTAREHL-YFYARLRGi 2076
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGeivlNGRTLFDSRKGIFLPPEkRRIGYVFQEARLFPHLSVRGNLrYGMKRARP- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2077 KQQNIPYISgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHK 2156
Cdd:TIGR02142 106 SERRISFER--VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGI 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 2041616051 2157 SVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKA 2194
Cdd:TIGR02142 184 PILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
974-1244 |
1.44e-13 |
|
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: 75.99 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGL--IPPTSG-----TAY--------------- 1031
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhVALcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1032 -------------IDGWDILTDIKK-IRQNIGFTPQHN-VLFDLLTVREH-LEFFARLKGAADETIDIEIErMLDDLMLT 1095
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRRrIRKRIAIMLQRTfALYGDDTVLDNvLEALEEIGYEGKEAVGRAVD-LIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1096 NKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLK--YKQGRTIIISTHFMDEADLLGDRI 1173
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1174 AIISSGELRCVGTSMFLKRKYAEGYNLIVEFTSVSDEEE-LKThsdENVMNNNSTIDDNASKLVNSSNIELR 1244
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPiIKV---RNVSKRYISVDRGVVKAVDNVSLEVK 308
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1968-2183 |
1.52e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.87 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGWQFgkkftAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGnAYVMEHSVLKDIDGVHR 2046
Cdd:PRK11607 19 LLEIRNLTKSFDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP-TAG-QIMLDGVDLSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 NLGYCPQFDALDNLLTAREHLYFyarlrGIKQQNIPY--ISGCLLKRLGLT---LWADRPVRQYSGGNKRKLSTAIALIG 2121
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAF-----GLKQDKLPKaeIASRVNEMLGLVhmqEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2122 NPSVIFMDEPTTGMDVRAK-RFLWDCILTLTRKEHKSVIITsHSMEECEVLCNRLSIMVAGEF 2183
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRdRMQLEVVDILERVGVTCVMVT-HDQEEAMTMAGRIAIMNRGKF 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
952-1181 |
1.75e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 952 ELDNRVKQRSASIesysdGEVGVEIINLCKyynnKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAY 1031
Cdd:COG1129 240 ELEDLFPKRAAAP-----GEVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1032 IDG--WDILTDIKKIRQNIGFTP---QHNVLFDLLTVRE-----HLEFFARL----KGAADETIDIEIERM------LDD 1091
Cdd:COG1129 311 LDGkpVRIRSPRDAIRAGIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGglldRRRERALAEEYIKRLriktpsPEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1092 LMLTnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTII-ISTHfMDEadLL 1169
Cdd:COG1129 391 PVGN---------LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIvISSE-LPE--LL 458
|
250
....*....|....
gi 2041616051 1170 G--DRIAIISSGEL 1181
Cdd:COG1129 459 GlsDRILVMREGRI 472
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1968-2192 |
1.84e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYgwqfgKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTS---------GNAYVMEHSVL 2038
Cdd:PRK09984 4 IIRVEKLAKTF-----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2039 KDIDGVHRNLGYCPQFDALDNLLTAREHLYFYARlrgikqQNIPYISGCL--------------LKRLGLTLWADRPVRQ 2104
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENVLIGAL------GSTPFWRTCFswftreqkqralqaLTRVGMVHFAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2105 YSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFK 2184
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
....*...
gi 2041616051 2185 CFGSVQHL 2192
Cdd:PRK09984 233 YDGSSQQF 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
976-1181 |
2.23e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.69 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 976 IINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-----------LTDIKKI 1044
Cdd:PRK10619 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1045 ---RQNIGFTPQHNVLFDLLTVREH-LEFFARLKGAADETIDIEIERMLDDLMLTNK-RDNYSTELSGGMKRKLSIAIAF 1119
Cdd:PRK10619 88 rllRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1120 CANSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
974-1173 |
2.33e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.43 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNN-----KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIR- 1045
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYKRAKy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 -----QN--IGFTPQhnvlfdlLTVREHL----------------------EFFARLKgaadeTIDIEIERMLDDLM-Lt 1095
Cdd:COG1101 82 igrvfQDpmMGTAPS-------MTIEENLalayrrgkrrglrrgltkkrreLFRELLA-----TLGLGLENRLDTKVgL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1096 nkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPfaRRSiwDLLLKY------KQGRTIIISTHFMDEADLL 1169
Cdd:COG1101 149 ---------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDP--KTA--ALVLELtekiveENNLTTLMVTHNMEQALDY 215
|
....
gi 2041616051 1170 GDRI 1173
Cdd:COG1101 216 GNRL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1971-2166 |
5.64e-13 |
|
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: 70.13 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1971 MTDLIKVYGwqfgKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV--MEHSVLKD--IDGVHR 2046
Cdd:cd03292 3 FINVTKTYP----NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVngQDVSDLRGraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 NLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVI 2126
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2041616051 2127 FMDEPTTGMDVRAKRflwdCILTLTRKEHK---SVIITSHSME 2166
Cdd:cd03292 159 IADEPTGNLDPDTTW----EIMNLLKKINKagtTVVVATHAKE 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1996-2184 |
5.76e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSvLKDIDGVHR------NLGYCPQFDALDNLLTAREHLYF 2069
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEARaklrakHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2070 YARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILT 2149
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 2041616051 2150 LTRKEHKSVIITSHSmEECEVLCNRLSIMVAGEFK 2184
Cdd:PRK10584 192 LNREHGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1971-2165 |
6.34e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.17 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1971 MTDLIKVYGWQ--FGKkFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDID------ 2042
Cdd:PRK11300 2 SQPLLSVSGLMmrFGG-LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiarm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2043 GVHR---NLGYCPQFDALDNLLTArEHlyfyarlrgiKQQNIPYISGCL-------------------LKRLGLTLWADR 2100
Cdd:PRK11300 81 GVVRtfqHVRLFREMTVIENLLVA-QH----------QQLKTGLFSGLLktpafrraesealdraatwLERVGLLEHANR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2101 PVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHK-SVIITSHSM 2165
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAEL-RNEHNvTVLLIEHDM 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
985-1186 |
6.35e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 985 NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDlLTV 1063
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFS-GSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1064 REHLEFfaRLKGAADETIDIEIERMLDDLMLTNKRDNYSTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:TIGR00958 572 RENIAY--GLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1137 PFARRSIWDllLKYKQGRTIIISTHFMDEADlLGDRIAIISSGELRCVGT 1186
Cdd:TIGR00958 650 AECEQLLQE--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGT 696
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
984-1136 |
7.11e-13 |
|
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: 69.60 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 984 NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPT---SGTAYIDGWDILTDIKKIRQNIGFTPQHNVLFDL 1060
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1061 LTVREHLEFFARLKGaadetidieiermlddlmltnkrDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:cd03233 98 LTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
982-1161 |
7.95e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 982 YYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILtdiKKIRQN-IGFTPQHN----- 1055
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR---QALQKNlVAYVPQSEevdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1056 --VLFD---LLTVREHLEFFARLKGAADETIDIEIER--MLDdlmltnKRDNYSTELSGGMKRKLSIAIAFCANSKTVIL 1128
Cdd:PRK15056 93 fpVLVEdvvMMGRYGHMGWLRRAKKRDRQIVTAALARvdMVE------FRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....
gi 2041616051 1129 DEPTAGVDPFARRSIWDLLLKYK-QGRTIIISTH 1161
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRdEGKTMLVSTH 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
974-1179 |
7.98e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIRQNIGFT 1051
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarLTPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLEFfaRL-KGAADETidiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDE 1130
Cdd:PRK15439 92 PQEPLLFPNLSVKENILF--GLpKRQASMQ---KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1131 PTAGVDPFAR----RSIWDLLlkyKQGRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:PRK15439 167 PTASLTPAETerlfSRIRELL---AQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1983-2163 |
8.00e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 68.88 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1983 GKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCPQfdaldnllt 2062
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2063 aREHLYfyarlrgikqqnipyiSGCLLKRLGltlwadrpvRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRF 2142
Cdd:cd03247 83 -RPYLF----------------DTTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180
....*....|....*....|.
gi 2041616051 2143 LWDCILTLTrkEHKSVIITSH 2163
Cdd:cd03247 137 LLSLIFEVL--KDKTLIWITH 155
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1988-2182 |
8.24e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.26 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSV---LKDIDGVHRNLGYCpqFDALDNLL--- 2061
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKTVGIV--FQNPDDQLfap 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAK- 2140
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAs 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2041616051 2141 ---RFLWDciltlTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK13639 175 qimKLLYD-----LNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
985-1180 |
8.30e-13 |
|
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: 69.42 E-value: 8.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 985 NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdiltdikkirqNIGFTPQ----HNvlfdl 1060
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQepwiQN----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 LTVREHLEFFAR---------LKGAADETiDIEIermLDDLMLTNKRDNYSTeLSGGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:cd03250 80 GTIRENILFGKPfdeeryekvIKACALEP-DLEI---LPDGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1132 TAGVDPFARRSIWDLLL--KYKQGRTIIISTH---FMDEAdllgDRIAIISSGE 1180
Cdd:cd03250 155 LSAVDAHVGRHIFENCIlgLLLNNKTRILVTHqlqLLPHA----DQIVVLDNGR 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1996-2183 |
9.14e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSV-LKDI-DGVHRNLGYCP----------QFDALDNL-LT 2062
Cdd:COG1129 275 VRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSPrDAIRAGIAYVPedrkgeglvlDLSIRENItLA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2063 AREHLYFYARLRGIKQQNI--PYIsgcllKRLGL-TLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:COG1129 355 SLDRLSRGGLLDRRRERALaeEYI-----KRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2041616051 2140 KRFLWDCILTLTRkEHKSVIITSHSMEECEVLCNRLSIM----VAGEF 2183
Cdd:COG1129 430 KAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRILVMregrIVGEL 476
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
975-1198 |
1.04e-12 |
|
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: 69.09 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 975 EIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGlIP---PTSGTAYIDGWDIlTDIK---KIRQNI 1048
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPpeeRARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1049 GFTPQHNVLFDLLTVREHLeffarlkgaadetidieiermlddlmltnkRD-NYSteLSGGMKRKLSIAIAFCANSKTVI 1127
Cdd:cd03217 80 FLAFQYPPEIPGVKNADFL------------------------------RYvNEG--FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 1128 LDEPTAGVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLL-GDRIAIISSGELRCVGTSMFLKRKYAEGY 1198
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1001-1186 |
1.44e-12 |
|
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: 71.67 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1001 ITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwDILTDIKKI------RQNIGFTPQHNVLFDLLTVREHLEFFARLK 1074
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGiflpphRRRIGYVFQEARLFPHLSVRGNLLYGRKRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1075 GAADETIDIE--IERM-LDDLMltnkrDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LK 1149
Cdd:COG4148 106 PRAERRISFDevVELLgIGHLL-----DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLerLR 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 2041616051 1150 YKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGT 1186
Cdd:COG4148 181 DELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1988-2183 |
1.47e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL----KD-----IDGVHRNLGYCPQFDALD 2058
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSsqeagIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLLTAREhlyFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVR 2138
Cdd:PRK10762 99 NIFLGRE---FVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2041616051 2139 AKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEF 2183
Cdd:PRK10762 176 ETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1964-2176 |
1.55e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.46 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1964 TSHDVLRMTDLIKVYgwQFGKKFTAV-NNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDID 2042
Cdd:PRK11629 1 MNKILLQCDNLCKRY--QEGSVQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2043 GV-----HRNLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAI 2117
Cdd:PRK11629 79 AAkaelrNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2118 ALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEecevLCNRLS 2176
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ----LAKRMS 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1969-2182 |
1.66e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.11 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVM--------EHSVLKD 2040
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklpEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2041 IDGVHRN--LGYCPQFDALDNLLTArehlyfYAR-----LR-GIKQQNIPYISGcLLKRLGLTLwADR---PVRQYSGGN 2109
Cdd:COG1101 82 IGRVFQDpmMGTAPSMTIEENLALA------YRRgkrrgLRrGLTKKRRELFRE-LLATLGLGL-ENRldtKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 2110 KRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFlwdcILTLTRK---EHK-SVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAAL----VLELTEKiveENNlTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
978-1180 |
1.75e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.95 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTA-YIDGWDILTDIKKI---------RQN 1047
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALseaerrrllRTE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1048 IGFTPQH-------------NVLFDLLTVRE-HlefFARLKGAAD---ETIDIEIERMlDDLmltnkrdnySTELSGGMK 1110
Cdd:PRK11701 91 WGFVHQHprdglrmqvsaggNIGERLMAVGArH---YGDIRATAGdwlERVEIDAARI-DDL---------PTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1111 RKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1988-2192 |
1.79e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.22 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLK-DIDGVHRNLGYCPQfDALDNLL--TAR 2064
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRKFVGLVFQ-NPDDQIFspTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 EHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLW 2144
Cdd:PRK13652 98 QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2041616051 2145 DCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHL 2192
Cdd:PRK13652 178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1988-2201 |
1.98e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.73 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDIDG-------VHRNLGYCPQFDALDNL 2060
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KPVEGpgaergvVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 LtarehlyFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAK 2140
Cdd:PRK11248 92 A-------FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2141 RFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCfgsVQHLKAKFGDGYT 2201
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRFV 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1896-2183 |
2.14e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1896 SPFEFNQVGRNLMALAIEGI-IFFIFALLIQYRFfIADRIR-RKPPKIVSIEE-----DDDV------------AAERQR 1956
Cdd:PRK15439 172 TPAETERLFSRIRELLAQGVgIVFISHKLPEIRQ-LADRISvMRDGTIALSGKtadlsTDDIiqaitpaareksLSASQK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1957 LYND-PNN---TSHD--VLRMTDLIkvygwqfGKKFTavnNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNA 2030
Cdd:PRK15439 251 LWLElPGNrrqQAAGapVLTVEDLT-------GEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2031 YVMEHSV--LKDIDGVHRNLGYCPQ--------FDA---------LDNLL-----TAREHLYF--YARLRGIKQQNipyi 2084
Cdd:PRK15439 321 MLNGKEInaLSTAQRLARGLVYLPEdrqssglyLDAplawnvcalTHNRRgfwikPARENAVLerYRRALNIKFNH---- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2085 sgcllkrlgltlwADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTrKEHKSVIITSHS 2164
Cdd:PRK15439 397 -------------AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSD 462
|
330
....*....|....*....
gi 2041616051 2165 MEECEVLCNRLSIMVAGEF 2183
Cdd:PRK15439 463 LEEIEQMADRVLVMHQGEI 481
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1973-2182 |
2.45e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1973 DLIKVYGwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGNAYVmehsvlkdiDGV------- 2044
Cdd:PRK11153 6 NISKVFP-QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlERP-TSGRVLV---------DGQdltalse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 ------HRNLGYCPQ-FdaldNLLTAR---EHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLS 2114
Cdd:PRK11153 75 kelrkaRRQIGMIFQhF----NLLSSRtvfDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2115 TAIALIGNPSVIFMDEPTTGMDVRAKRflwdCILTLTRKEHKS-----VIITsHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTR----SILELLKDINRElgltiVLIT-HEMDVVKRICDRVAVIDAGR 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
974-1187 |
2.60e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIP----PTS-----GTAYIDGWDILTDIKKI 1044
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGShiellGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1045 RQNIGFTPQHNVLFDLLTVREHLeffarLKGAADET----------IDIEIERMLDDL----MLTNKRDNYSTeLSGGMK 1110
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENV-----LIGALGSTpfwrtcfswfTREQKQRALQALtrvgMVHFAHQRVST-LSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1111 RKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVGTS 1187
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
973-1167 |
3.34e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.89 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 973 GVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPP---TSGTAYIDGWDIlTDIKKIRQNIG 1049
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-TALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDLLTVREHLEFF--ARLKGAADETidiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVI 1127
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFAlpPTIGRAQRRA---RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2041616051 1128 LDEPTAGVDPFARRSIWDLLLKYKQGRTI--IISTHfmDEAD 1167
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTH--DEED 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1989-2182 |
3.51e-12 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 66.86 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLkdIDGV----------HRNLGYCPQFDALd 2058
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSG-------RVR--LDGAdisqwdpnelGDHVGYLPQDDEL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 nlltarehlyfyarLRGIKQQNIpyisgcllkrlgltlwadrpvrqYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVR 2138
Cdd:cd03246 88 --------------FSGSIAENI-----------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2041616051 2139 AKRFLWDCILTLtRKEHKSVIITSHSMEECEvLCNRLSIMVAGE 2182
Cdd:cd03246 131 GERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGR 172
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1965-2182 |
3.65e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1965 SHDVLRMTDLIKVYGwqfGKKftAVNNICAGVKQGECFGLLGINGSGKSTTFKML---------TGEI-----PLTSGNA 2030
Cdd:PRK13549 2 MEYLLEMKNITKTFG---GVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphgtyEGEIifegeELQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2031 YVMEHsvlKDIDGVHRNLGYCPQFDALDNLLTAREHLYFyarlrGIKQQNIPYiSGC--LLKRLGLTLWADRPVRQYSGG 2108
Cdd:PRK13549 77 RDTER---AGIAIIHQELALVKELSVLENIFLGNEITPG-----GIMDYDAMY-LRAqkLLAQLKLDINPATPVGNLGLG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2109 NKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIItSHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYI-SHKLNEVKAISDTICVIRDGR 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1996-2163 |
3.72e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNLLTAREHLYFYARLRG 2075
Cdd:PRK13538 24 LNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFYQRLHG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2076 -IKQQNIPYIsgclLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAkrflwdcILTLTR-- 2152
Cdd:PRK13538 104 pGDDEALWEA----LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG-------VARLEAll 172
|
170
....*....|....*
gi 2041616051 2153 KEHKS----VIITSH 2163
Cdd:PRK13538 173 AQHAEqggmVILTTH 187
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
986-1234 |
5.08e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 986 KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIdgwdiltdikkIRQNIGFTPQHNVLFDLlTVRE 1065
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1066 HLEFFARLK----GAAdetidIEIERMLDDLMLTNKRD-----NYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:PLN03232 698 NILFGSDFEseryWRA-----IDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1137 PFARRSIWDLLLKYK-QGRTIIIST---HFMDeadlLGDRIAIISSGELRCVGTSMFLKrKYAEGYNLIVEFTSVSDEEE 1212
Cdd:PLN03232 773 AHVAHQVFDSCMKDElKGKTRVLVTnqlHFLP----LMDRIILVSEGMIKEEGTFAELS-KSGSLFKKLMENAGKMDATQ 847
|
250 260
....*....|....*....|..
gi 2041616051 1213 LKTHSDENVMNNNSTIDDNASK 1234
Cdd:PLN03232 848 EVNTNDENILKLGPTVTIDVSE 869
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
983-1166 |
6.04e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 983 YNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDLL 1061
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1062 TVRE--------HLEFFARLKGAADETIDieieRMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PRK10253 97 TVQElvargrypHQPLFTRWRKEDEEAVT----KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2041616051 1134 GVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEA 1166
Cdd:PRK10253 173 WLDISHQIDLLELLseLNREKGYTLAAVLHDLNQA 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1988-2195 |
7.11e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 68.34 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSG----NAYVMEHSVlKDIDGVHRNLGYCpqFDALDNLL-- 2061
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGrilfDGKPIDYSR-KGLMKLRESVGMV--FQDPDNQLfs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 -TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAK 2140
Cdd:PRK13636 98 aSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2141 RFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAK 2195
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1989-2181 |
7.13e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 67.49 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLK---DIDGVHRNLGYCPQFDALDNLLTA-- 2063
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNYSLLPWLTVRENIALAvd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2064 --REHLYFYARlRGIKQQNIPYIsgcllkrlGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:TIGR01184 81 rvLPDLSKSER-RAIVEEHIALV--------GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2041616051 2142 FLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1000-1161 |
8.85e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1000 QITSFLGRNGAGKSTTWSILTGLIPPTS--GTAYIDGWDIltdIKKIRQNIGFTPQHNVLFDLLTVREHLEFFARLKGAA 1077
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP---TKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1078 DETIDIEI---ERMLDDLMLTnKRDN------YSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPF-ARRSIWDLL 1147
Cdd:PLN03211 172 SLTKQEKIlvaESVISELGLT-KCENtiignsFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATaAYRLVLTLG 250
|
170
....*....|....
gi 2041616051 1148 LKYKQGRTIIISTH 1161
Cdd:PLN03211 251 SLAQKGKTIVTSMH 264
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1969-2165 |
1.27e-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: 66.40 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL---KDIDGVH 2045
Cdd:cd03262 1 IEIKNLHKSFG-----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 RNLGYC-------PQFDALDNLLTARehlyfyARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIA 2118
Cdd:cd03262 76 QKVGMVfqqfnlfPHLTVLENITLAP------IKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2041616051 2119 LIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTrKEHKSVIITSHSM 2165
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEM 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
939-1161 |
1.28e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.05 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 939 LINLEKNQSENTNELDnRVKqrsasiesysdGEVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSI 1018
Cdd:PRK11176 321 ILDLEQEKDEGKRVIE-RAK-----------GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1019 LTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDLlTV-------------REHLEFFARLKGAADEtidie 1084
Cdd:PRK11176 389 LTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQNVHLFND-TIanniayarteqysREQIEEAARMAYAMDF----- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1085 IERM---LDDLMLTNkrdnySTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:PRK11176 463 INKMdngLDTVIGEN-----GVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1989-2183 |
1.58e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLKDIDGVHRNlgyCPQfDALDN--------- 2059
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSG-------YVTLDGHEVVTR---SPQ-DGLANgivyisedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2060 ---------------LLTAREHL-YFYARLRGIKQQNI--PYISGCLLKrlglTLWADRPVRQYSGGNKRKLSTAIALIG 2121
Cdd:PRK10762 337 krdglvlgmsvkenmSLTALRYFsRAGGSLKHADEQQAvsDFIRLFNIK----TPSMEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2122 NPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIM----VAGEF 2183
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMhegrISGEF 477
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
965-1182 |
1.79e-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: 69.08 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 965 ESYSDGEVGVEIINLCKYYNNKLALK---NLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPT-SGTAYIDG--WDIL 1038
Cdd:TIGR02633 249 EPHEIGDVILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1039 TDIKKIRQNIGFTPQ----HNVLFDL-------LTVREHLEFFARLKGAADE-TIDIEIERMLddlMLTNKRDNYSTELS 1106
Cdd:TIGR02633 329 NPAQAIRAGIAMVPEdrkrHGIVPILgvgknitLSVLKSFCFKMRIDAAAELqIIGSAIQRLK---VKTASPFLPIGRLS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1107 GGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELR 1182
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
2003-2192 |
1.80e-11 |
|
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: 68.20 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2003 GLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHsVLKDIDG-----VH-RNLGYCPQFDALDNLLTAREHLyFYARLRGI 2076
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARgiflpPHrRRIGYVFQEARLFPHLSVRGNL-LYGRKRAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2077 KQQNIPYISGcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHK 2156
Cdd:COG4148 107 RAERRISFDE-VVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDI 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 2041616051 2157 SVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHL 2192
Cdd:COG4148 186 PILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1978-2181 |
1.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1978 YGWQFGK--KFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVME---HSVLKD--IDGVHRNLGY 2050
Cdd:PRK13646 10 YTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDkyIRPVRKRIGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2051 CPQFDAL----DNLltAREHLY----FYARLRGIKQQNIPyisgcLLKRLGLT--LWADRPVrQYSGGNKRKLSTAIALI 2120
Cdd:PRK13646 90 VFQFPESqlfeDTV--EREIIFgpknFKMNLDEVKNYAHR-----LLMDLGFSrdVMSQSPF-QMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2121 GNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1987-2195 |
1.95e-11 |
|
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: 69.40 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSvLKDIDG--VHRNLGYCPQFDAL------D 2058
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD-LSDLDPasWRRQIAWVPQNPYLfagtirE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLLTAR-----EHLYFYARLRGIKQqnipyisgcLLKRL--GLtlwaDRPV----RQYSGGNKRKLSTAIALIGNPSVIF 2127
Cdd:COG4988 430 NLRLGRpdasdEELEAALEAAGLDE---------FVAALpdGL----DTPLgeggRGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2128 MDEPTTGMDVRAKRFLWDCILTLTRkeHKSVIITSHSMEECEvLCNRLSIMVAGEFKCFGSVQHLKAK 2195
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1982-2181 |
2.40e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.80 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1982 FGKkfTAV-NNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnaYVMEHSvlKDIDGVH---RNLGYCPQFDAL 2057
Cdd:PRK10851 12 FGR--TQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG--HIRFHG--TDVSRLHardRKVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2058 DNLLTAREHLYFYAR-LRGIKQQNIPYISG---CLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:PRK10851 86 FRHMTVFDNIAFGLTvLPRRERPNAAAIKAkvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2134 GMDVRAKRFL--WdciltlTRKEHK-----SVIITsHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK10851 166 ALDAQVRKELrrW------LRQLHEelkftSVFVT-HDQEEAMEVADRVVVMSQG 213
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
974-1161 |
2.84e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQ 1053
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1054 HNVLFDLLTVREHLEFFARLKGAAdetidIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGA-----VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180
....*....|....*....|....*....
gi 2041616051 1134 GVDPFARRSIWDLLLKY-KQGRTIIISTH 1161
Cdd:PRK13540 157 ALDELSLLTIITKIQEHrAKGGAVLLTSH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1990-2163 |
2.95e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 63.24 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1990 NNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNayVMEHSVLKdidgvhrnlgycpqfdaldnlltarehlyf 2069
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--VTWGSTVK------------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2070 yarlrgikqqnIPYISgcllkrlgltlwadrpvrQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCIlt 2149
Cdd:cd03221 65 -----------IGYFE------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL-- 113
|
170
....*....|....
gi 2041616051 2150 ltRKEHKSVIITSH 2163
Cdd:cd03221 114 --KEYPGTVILVSH 125
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1950-2184 |
3.11e-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: 68.31 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1950 VAAERQRLY-NDPNNTSHDVLRMTDLIkvyGWQ-FGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIP-LT 2026
Cdd:TIGR02633 238 VGREITSLYpHEPHEIGDVILEARNLT---CWDvINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKF 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2027 SGNAYVMEHSV-----LKDID-GV------HRNLGYCPQFDALDNL-LTAREHLYFYARLRGIKQQNIpyiSGCLLKRLG 2093
Cdd:TIGR02633 315 EGNVFINGKPVdirnpAQAIRaGIamvpedRKRHGIVPILGVGKNItLSVLKSFCFKMRIDAAAELQI---IGSAIQRLK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2094 L-TLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRkEHKSVIITSHSMEECEVLC 2172
Cdd:TIGR02633 392 VkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLS 470
|
250
....*....|..
gi 2041616051 2173 NRLSIMVAGEFK 2184
Cdd:TIGR02633 471 DRVLVIGEGKLK 482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1953-2198 |
3.85e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 68.38 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1953 ERQRLYNDPNNTSHDVLRMTdlikvygwQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV 2032
Cdd:PRK13545 12 KKYKMYNKPFDKLKDLFFRS--------KDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2033 MEHSVLKDIDGvhrnlgycpqfdALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRK 2112
Cdd:PRK13545 84 KGSAALIAISS------------GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2113 LSTAIALIGNPSVIFMDEpttGMDVRAKRFLWDCILTLT--RKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQ 2190
Cdd:PRK13545 152 LGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIK 228
|
....*...
gi 2041616051 2191 HLKAKFGD 2198
Cdd:PRK13545 229 EVVDHYDE 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1985-2188 |
3.97e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.18 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1985 KFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSV------LKDIDGVHRNLGYCPQFDALD 2058
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLL-TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTL-WADRPVRQYSGGNKRKLSTA--IALIGNPSVifMDEPTTG 2134
Cdd:PRK13645 103 LFQeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAgiIAMDGNTLV--LDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2135 MDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGS 2188
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
977-1196 |
4.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.27 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 977 INLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAY-----IDGWDILT--DIKKIRQNIG 1049
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNyrDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFD-------LLTVREH-LEFFARLKGAADETIdieIERMLDDlMLTNKRDNYSTELSGGMKRKLSIAIAFCA 1121
Cdd:PRK14271 105 MLFQRPNPFPmsimdnvLAGVRAHkLVPRKEFRGVAQARL---TEVGLWD-AVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1122 NSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTS--MFLKRKYAE 1196
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTeqLFSSPKHAE 257
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
989-1165 |
5.50e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLF-DllTVREH 1066
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFgD--TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1067 LEFFARLKGAADETidieiERMLDDLM-------LTNKRDNystELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFA 1139
Cdd:PRK10247 101 LIFPWQIRNQQPDP-----AIFLDDLErfalpdtILTKNIA---ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180
....*....|....*....|....*...
gi 2041616051 1140 RRSIWDLLLKY--KQGRTIIISTHFMDE 1165
Cdd:PRK10247 173 KHNVNEIIHRYvrEQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1978-2167 |
5.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1978 YGWQFGKKFT--AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSG-----NAYVMEHSVLKDIDGVHRNLGY 2050
Cdd:PRK13643 9 YTYQPNSPFAsrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKEIKPVRKKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2051 CPQFDAlDNLL--TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLT--LWADRPVrQYSGGNKRKLSTAIALIGNPSVI 2126
Cdd:PRK13643 89 VFQFPE-SQLFeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdeFWEKSPF-ELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 2127 FMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEE 2167
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDD 206
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
982-1182 |
6.24e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.69 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 982 YYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI-LTDIKKIRQNIG--FTPQHnvLF 1058
Cdd:PRK10522 332 YQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSavFTDFH--LF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 DLLTVREHLEffarlkgAADETIDIEIERM-------LDDLMLTNkrdnysTELSGGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:PRK10522 410 DQLLGPEGKP-------ANPALVEKWLERLkmahkleLEDGRISN------LKLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1132 TAGVDPFARRSIWDLLLKYKQ--GRTII-IS--THFMDEAdllgDRIAIISSGELR 1182
Cdd:PRK10522 477 AADQDPHFRREFYQVLLPLLQemGKTIFaIShdDHYFIHA----DRLLEMRNGQLS 528
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1955-2166 |
7.34e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.03 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1955 QRLYNDPNNTSHD-VLRMTDLIKVYGWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVM 2033
Cdd:PRK13631 7 KKKLKVPNPLSDDiILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2034 EHSVLKDIDGVHRNLGYCPQ----FDALDNLL--------------TAREHLYFYARLRGIKQQNIPYISGCLLKRLGL- 2094
Cdd:PRK13631 87 DIYIGDKKNNHELITNPYSKkiknFKELRRRVsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLd 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2095 TLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTlTRKEHKSVIITSHSME 2166
Cdd:PRK13631 167 DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTME 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1000-1161 |
1.22e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1000 QITsflGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdilTDIKKIR----QNIGFTPQHNVLFDLLTVREHLEFFARLKG 1075
Cdd:PRK13538 31 QIE---GPNGAGKTSLLRILAGLARPDAGEVLWQG----EPIRRQRdeyhQDLLYLGHQPGIKTELTALENLRFYQRLHG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1076 AADETidiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEP-----TAGVDPFARRsiwdLLLKY 1150
Cdd:PRK13538 104 PGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPftaidKQGVARLEAL----LAQHA 176
|
170
....*....|.
gi 2041616051 1151 KQGRTIIISTH 1161
Cdd:PRK13538 177 EQGGMVILTTH 187
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1989-2198 |
1.53e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKD-IDGVHRNLGYCpqFDALDNLL---TAR 2064
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIGMV--FQNPDNQFvgaTVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 EHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLW 2144
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2145 DCILTLTRKEHKSVIITSHSMEECeVLCNRLSIMVAGEFKCFGSVQHLKAKFGD 2198
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
989-1192 |
2.21e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDLLTVREHL 1067
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1068 EF--------FARLkGAADETidiEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFA 1139
Cdd:PRK10575 107 AIgrypwhgaLGRF-GAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1140 RRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLKR 1192
Cdd:PRK10575 183 QVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1988-2182 |
2.55e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.88 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVmEHSVLKD--IDGVHRNLGYCpqFDALDNLL---T 2062
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEetVWDVRRQVGMV--FQNPDNQFvgaT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2063 AREHLYFYARLRGI-KQQNIPYISGCLlKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:PRK13635 99 VQDDVAFGLENIGVpREEMVERVDQAL-RQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 2142 FLWDCILTLTRKEHKSVIITSHSMEECeVLCNRLSIMVAGE 2182
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGE 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1988-2197 |
2.62e-10 |
|
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: 62.89 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSV-LKDIDGVHRNLGYCPQFDAL------DNL 2060
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQENVLfnrsirDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 LTA-----REHLYFYARLRGIKQ--QNIPYISGCLLKRLGLTLwadrpvrqySGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:cd03252 97 ALAdpgmsMERVIEAAKLAGAHDfiSELPEGYDTIVGEQGAGL---------SGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2134 GMDVRAKRflwdcilTLTRKEHK-----SVIITSHSMEecEVLC-NRLSIMVAGEFKCFGSVQHLKAKFG 2197
Cdd:cd03252 168 ALDYESEH-------AIMRNMHDicagrTVIIIAHRLS--TVKNaDRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
988-1179 |
3.18e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWD---------ILTDIKKIRQNIGFTPQhnvlf 1058
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaaLAAGVAIIYQELHLVPE----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 dlLTVREHLeFFARL--------KGAADETIDIEIERMLDDLmltnKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDE 1130
Cdd:PRK11288 94 --MTVAENL-YLGQLphkggivnRRLLNYEAREQLEHLGVDI----DPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1131 PTAGVDpfAR------RSIWDLllkYKQGRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:PRK11288 167 PTSSLS--AReieqlfRVIREL---RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
983-1147 |
3.20e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 983 YNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTayidgwdiltdIKKIRQ-NIGFTPQhNVLFDL- 1060
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-----------IKRNGKlRIGYVPQ-KLYLDTt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 --LTVREhlefFARLK-GAADETIDIEIERMLDDLMLtnkrDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDP 1137
Cdd:PRK09544 82 lpLTVNR----FLRLRpGTKKEDILPALKRVQAGHLI----DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170
....*....|
gi 2041616051 1138 FARRSIWDLL 1147
Cdd:PRK09544 154 NGQVALYDLI 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1968-2182 |
3.34e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlkDIDG---- 2043
Cdd:COG3845 5 ALELRGITKRFG-----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV--RIRSprda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 -------VHRNLGYCPQFDALDNLLTAREHL-YFYARLRGIKQQnipyISGcLLKRLGLTLWADRPVRQYSGGNKRKLST 2115
Cdd:COG3845 78 ialgigmVHQHFMLVPNLTVAENIVLGLEPTkGGRLDRKAARAR----IRE-LSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 2116 AIALIGNPSVIFMDEPTTGMDVRAKRFLWDcILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFE-ILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1968-2182 |
3.40e-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: 63.29 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVY--GWQFGKK--FTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKdIDG 2043
Cdd:TIGR02769 2 LLEVRDVTHTYrtGGLFGAKqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ-LDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 -----VHRNLGYCPQ--FDALDNLLTAR----EHLYFYARLRGIKQQNipYISGcLLKRLGL-TLWADRPVRQYSGGNKR 2111
Cdd:TIGR02769 81 kqrraFRRDVQLVFQdsPSAVNPRMTVRqiigEPLRHLTSLDESEQKA--RIAE-LLDMVGLrSEDADKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2112 KLSTAIALIGNPSVIFMDEPTTGMDvrakRFLWDCILTLTRKEHK----SVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKLQQafgtAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1977-2182 |
4.12e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1977 VYGWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV-MEHSVLKDIDGVHRNLGYCpqFD 2055
Cdd:PRK13642 11 VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKIGMV--FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2056 ALDNLL---TAREHLYFYARLRGI-KQQNIPYISGCLLKRLGLTLWADRPVRqYSGGNKRKLSTAIALIGNPSVIFMDEP 2131
Cdd:PRK13642 89 NPDNQFvgaTVEDDVAFGMENQGIpREEMIKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2132 TTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVlCNRLSIMVAGE 2182
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGE 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1971-2141 |
4.35e-10 |
|
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: 62.07 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1971 MTDLIKVYGwqFGKKFT----------AVNNICAGVKQGECFGLLGINGSGKSTTFKML-------TGEIPLTSGNAYV- 2032
Cdd:COG4778 1 MTTLLEVEN--LSKTFTlhlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVRHDGGWVd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2033 ----MEHSVLkdidGVHRN-LGYCPQFdaLDNL--LTAREHLYFYARLRGIKQQNIPYISGCLLKRLGL--TLWADRPVr 2103
Cdd:COG4778 79 laqaSPREIL----ALRRRtIGYVSQF--LRVIprVSALDVVAEPLLERGVDREEARARARELLARLNLpeRLWDLPPA- 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 2041616051 2104 QYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
989-1182 |
4.71e-10 |
|
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: 62.95 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPpTSGTAYIDG--WDILTdIKKIRQNIGFTPQHNVLFDLlTVREH 1066
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvsWNSVP-LQKWRKAFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1067 LEFFARLKgaadetiDIEIERMLDDLMLTNKRDNYSTEL-----------SGGMKRKLSIAIAFCANSKTVILDEPTAGV 1135
Cdd:cd03289 97 LDPYGKWS-------DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2041616051 1136 DPFARRSIWDLLLKYKQGRTIIISTHFMdEADLLGDRIAIISSGELR 1182
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1969-2182 |
4.93e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.56 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYgWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGnayvmehSVLkdIDGVH-- 2045
Cdd:COG1135 2 IELENLSKTF-PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlERP-TSG-------SVL--VDGVDlt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 -----------RNLGYCPQ-FdaldNLL---TAREhlyfyarlrgikqqNIPY---ISGC-----------LLKRLGLTL 2096
Cdd:COG1135 71 alserelraarRKIGMIFQhF----NLLssrTVAE--------------NVALpleIAGVpkaeirkrvaeLLELVGLSD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2097 WADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD---VRAkrflwdcILTLTRKEHKS-----VIITsHSMeec 2168
Cdd:COG1135 133 KADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRS-------ILDLLKDINRElgltiVLIT-HEM--- 201
|
250
....*....|....*..
gi 2041616051 2169 EV---LCNRLSIMVAGE 2182
Cdd:COG1135 202 DVvrrICDRVAVLENGR 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
987-1179 |
5.40e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVkFYQNQITSF------------LGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDiLTDIKKIRQNIGFTPQH 1054
Cdd:PRK10771 2 LKLTDITW-LYHHLPMRFdltvergervaiLGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLTVREH----LEFFARLKGAADETIDIEIERM-LDDLMltnkrDNYSTELSGGMKRKLSIAIAFCANSKTVILD 1129
Cdd:PRK10771 80 NNLFSHLTVAQNiglgLNPGLKLNAAQREKLHAIARQMgIEDLL-----ARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKYKQGR--TIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1996-2136 |
6.12e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.40 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAyvmehsvlkDIDGVH-------RNLGYCPQFDALDNLLTAREHLY 2068
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---------QIDGKTatrgdrsRFMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2069 FYARLRGIKQQNIPyisGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:PRK13543 105 FLCGLHGRRAKQMP---GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
974-1191 |
6.32e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.48 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI----LTDIKKIRQNIG 1049
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDLLTVREHLEFFARLKGAADETIDIEIERM-LDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVIL 1128
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1129 DEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLK 1191
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1989-2188 |
6.83e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.99 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVmEHSVL---KDI---DGV--HRNLGYCPQFDALDNL 2060
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV-DGKVLyfgKDIfqiDAIklRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 LTAREHLYFYARLRGIKQQ-NIPYISGCLLKRLGLtlWA---DR---PVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGL--WKevyDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2134 GMDVRAKRFLWDCILTLtrKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGS 2188
Cdd:PRK14246 183 MIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
978-1181 |
7.98e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.00 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSG-----TAYIDgwDILTDIKKIRQNIGFTP 1052
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagTAPLA--EAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1053 QHNVLFDL-LTVREHLEFFARlkgaadetidieieRMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:PRK11247 95 WKKVIDNVgLGLKGQWRDAAL--------------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1132 TAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK11247 161 LGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1006-1161 |
8.39e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 64.07 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1006 GRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKK--IRQNIGFTPQHNVLF-DllTVREHLEFfARLkGAADEtid 1082
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQasLRAAIGIVPQDTVLFnD--TIAYNIAY-GRP-DASEE--- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1083 iEIER-----MLDDLMLTNKrDNYSTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKY 1150
Cdd:COG5265 463 -EVEAaaraaQIHDFIESLP-DGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV 540
|
170
....*....|.
gi 2041616051 1151 KQGRTIIISTH 1161
Cdd:COG5265 541 ARGRTTLVIAH 551
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
992-1180 |
8.61e-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: 61.66 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 992 LSVK---FYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGtayidgwdiltDIKKIRQNIGFTPQHNVLFDLLTVREHLe 1068
Cdd:cd03237 15 LEVEggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----------DIEIELDTVSYKPQYIKADYEGTVRDLL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1069 fFARLKGAADET---IDIEIERMLDDLMltnkrDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFAR----R 1141
Cdd:cd03237 83 -SSITKDFYTHPyfkTEIAKPLQIEQIL-----DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2041616051 1142 SIWDLLLKYKqgRTIIISTHFMDEADLLGDRIaIISSGE 1180
Cdd:cd03237 157 VIRRFAENNE--KTAFVVEHDIIMIDYLADRL-IVFEGE 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
989-1169 |
9.64e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPptsgTAYIDGWDILTDIKKI----RQNIGFTPQHNVLFDLLTVR 1064
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT----TGVITGGDRLVNGRPLdssfQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1065 EHLEFFARLKGAADETIDiEIERMLDDLMLTNKRDNYSTELSG----GM----KRKLSIAIAFCANSKTVI-LDEPTAGV 1135
Cdd:TIGR00956 855 ESLRFSAYLRQPKSVSKS-EKMEYVEEVIKLLEMESYADAVVGvpgeGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2041616051 1136 DPFARRSIWDLLLKY-KQGRTIIISTH-----FMDEADLL 1169
Cdd:TIGR00956 934 DSQTAWSICKLMRKLaDHGQAILCTIHqpsaiLFEEFDRL 973
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
972-1220 |
9.79e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 972 VGVEIINLCK----YYNNK----------------LALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAY 1031
Cdd:PRK13546 3 VSVNIKNVTKeyriYRTNKermkdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1032 IDGwdiltDIKKIRQNIGFTPQhnvlfdlLTVREHLEFFARLKGAADEtidiEIERMLDDLMLTNKRDNY----STELSG 1107
Cdd:PRK13546 83 RNG-----EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRK----EIKAMTPKIIEFSELGEFiyqpVKKYSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1108 GMKRKLSIAIAFCANSKTVILDEP-TAGVDPFARRSIwDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK13546 147 GMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCL-DKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 2041616051 1186 TSMFLKRKYAEgynLIVEF--TSVSDEEELKTHSDEN 1220
Cdd:PRK13546 226 ELDDVLPKYEA---FLNDFkkKSKAEQKEFRNKLDES 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1983-2182 |
1.46e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.26 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1983 GKKFTAVNNICAGVKQGECFGLLGINGSGKSTTF-------KMLTGEI-----------PLTS---GNAYVMEHsvlkdi 2041
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMnclfgvdKRAGGEIrlngkdisprsPLDAvkkGMAYITES------ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2042 dgvHRNLGYCPQFDALDNLLTARE-HLYFYARLRGI----KQQNIPYISGCLLKRLGLTLwaDRPVRQYSGGNKRKLSTA 2116
Cdd:PRK09700 347 ---RRDNGFFPNFSIAQNMAISRSlKDGGYKGAMGLfhevDEQRTAENQRELLALKCHSV--NQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2117 IALIGNPSVIFMDEPTTGMDVRAKRFlwdcILTLTRK---EHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAE----IYKVMRQladDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1930-2183 |
1.46e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1930 IADRI---RR------KPPKIVSIEE------DDDVAAERQRlynDPNNTSHDVLRMTDLiKVYGwqfGKKFTAVNNICA 1994
Cdd:COG3845 207 IADRVtvlRRgkvvgtVDTAETSEEElaelmvGREVLLRVEK---APAEPGEVVLEVENL-SVRD---DRGVPALKDVSL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1995 GVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDIDG------VHRNLGY----------CPQFDALD 2058
Cdd:COG3845 280 EVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG----EDITGlsprerRRLGVAYipedrlgrglVPDMSVAE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLLtarehlyfyarLRGIKQQniPYISGCLLKRLGLTLWADR--------------PVRQYSGGNKRKLSTAIALIGNPS 2124
Cdd:COG3845 356 NLI-----------LGRYRRP--PFSRGGFLDRKAIRAFAEElieefdvrtpgpdtPARSLSGGNQQKVILARELSRDPK 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2125 VIFMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGEF 2183
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
990-1181 |
1.58e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 990 KNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI--LTDIKKIRQNIGFTP----QHNVLFDL--- 1060
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPedrqSSGLYLDApla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 -----LTVREhLEFFarLKGAADETIdieIERMLDDLMLT-NKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:PRK15439 360 wnvcaLTHNR-RGFW--IKPARENAV---LERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 1135 VDPFARRSIWDLLLKY-KQGRTII-ISTHFmDEADLLGDRIAIISSGEL 1181
Cdd:PRK15439 434 VDVSARNDIYQLIRSIaAQNVAVLfISSDL-EEIEQMADRVLVMHQGEI 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
976-1180 |
2.05e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 976 IINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI---------LTDIKKIRQ 1046
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1047 NIGFTPQHNVLFDLLTVREHLE-FFARLKGAADETIDIEIERMLDdlmlTNKRDNYSTeLSGGMKRKLSIAIAFCANSKT 1125
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKgMFVDQDKMYRDTKAIFDELDID----IDPRAKVAT-LSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1126 VILDEPTAGVDPFARRSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
985-1161 |
2.28e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.50 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 985 NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGftpqHNVLFDL-LTV 1063
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG----HNLGLKLeMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1064 REHLEFFARLKGAAdETIDIEIERM-LDDLMltnkrDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRS 1142
Cdd:PRK13541 88 FENLKFWSEIYNSA-ETLYAAIHYFkLHDLL-----DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|
gi 2041616051 1143 IWDLL-LKYKQGRTIIISTH 1161
Cdd:PRK13541 162 LNNLIvMKANSGGIVLLSSH 181
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
989-1161 |
2.32e-09 |
|
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: 63.01 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPpTSGTAYIDG--WDILTdIKKIRQNIGFTPQHNVLFDLlTVREH 1066
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvsWNSVT-LQTWRKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1067 LEFFARLKgaadetiDIEIERMLDDLMLTNKRDNYSTEL-----------SGGMKRKLSIAIAFCANSKTVILDEPTAGV 1135
Cdd:TIGR01271 1312 LDPYEQWS-------DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180
....*....|....*....|....*.
gi 2041616051 1136 DPFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
988-1181 |
2.48e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.57 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGW-----DILTDIKKIRqnIGFTPQHNVLFDLLT 1062
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIR--MIFQDPSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1063 VREHLEFFARL----KGAADETIDIEIERMLDdlMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPF 1138
Cdd:PRK15112 106 ISQILDFPLRLntdlEPEQREKQIIETLRQVG--LLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2041616051 1139 ARRSIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIAIISSGEL 1181
Cdd:PRK15112 184 MRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
992-1161 |
2.73e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 992 LSVKFYQNQITSFLGRNGAGKSTTWSILTGLIpPTSGTAYIDGWDILT----DIKKIRQNigFTPQHNVLFdLLTVREHL 1067
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAY--LSQQQTPPF-AMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1068 EFFaRLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFC-------ANSKTVILDEPTAGVDpFAR 1140
Cdd:PRK03695 91 TLH-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLD-VAQ 168
|
170 180
....*....|....*....|...
gi 2041616051 1141 RSIWDLLLKY--KQGRTIIISTH 1161
Cdd:PRK03695 169 QAALDRLLSElcQQGIAVVMSSH 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
970-1182 |
3.40e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLCKYYNNKLALK---NLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIP-PTSGTAYIDG--WDILTDIKK 1043
Cdd:PRK13549 256 GEVILEVRNLTAWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1044 IRQNIGFTP----QHNVLFDL-------LTVREHLEFFARLKGAADE-TIDIEIERM---LDDLMLTNKRdnysteLSGG 1108
Cdd:PRK13549 336 IAQGIAMVPedrkRDGIVPVMgvgknitLAALDRFTGGSRIDDAAELkTILESIQRLkvkTASPELAIAR------LSGG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1109 MKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEADLLGDRIAIISSGELR 1182
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
989-1136 |
3.43e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI----LTDIKKirqNIGFTPQHNVLFDlLTVR 1064
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskfgLMDLRK---VLGIIPQAPVLFS-GTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1065 EHLEFFARLKGAadetiDI--EIERM-LDDLMLTNKR----------DNYSTelsgGMKRKLSIAIAFCANSKTVILDEP 1131
Cdd:PLN03130 1331 FNLDPFNEHNDA-----DLweSLERAhLKDVIRRNSLgldaevseagENFSV----GQRQLLSLARALLRRSKILVLDEA 1401
|
....*
gi 2041616051 1132 TAGVD 1136
Cdd:PLN03130 1402 TAAVD 1406
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1996-2137 |
3.62e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.73 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNayvmehsVLKDIDGVhrnlGYCPQFDALDNLLTAREHLYFYARLRG 2075
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-------IEIELDTV----SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2076 ikqqNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDV 2137
Cdd:cd03237 91 ----THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
988-1185 |
4.30e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGW--DILTD--IKKIRQNIGFT---------PQH 1054
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTLSPgkLQALRRDIQFIfqdpyasldPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLtvrEHLEFFARLKG-AADETIDIEIERMLddlMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PRK10261 419 TVGDSIM---EPLRVHGLLPGkAAAARVAWLLERVG---LLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 1134 GVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1976-2136 |
4.39e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1976 KVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLT-GEIPlTSGNAYVMEHSV-------LKDIDGVHRN 2047
Cdd:COG4161 10 CFYG-----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNlLETP-DSGQLNIAGHQFdfsqkpsEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2048 LGYC-------PQFDALDNLLTA--------REHlyfyARLRGIKqqnipyisgcLLKRLGLTLWADRPVRQYSGGNKRK 2112
Cdd:COG4161 84 VGMVfqqynlwPHLTVMENLIEApckvlglsKEQ----AREKAMK----------LLARLRLTDKADRFPLHLSGGQQQR 149
|
170 180
....*....|....*....|....
gi 2041616051 2113 LSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALD 173
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
984-1225 |
4.68e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 984 NNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIdgwdiltdikkIRQNIGFTPQHNVLFDLlTV 1063
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1064 REHLEFFARLKGAADETIdIEIERMLDDLMLTNKRDnySTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:PLN03130 696 RDNILFGSPFDPERYERA-IDVTALQHDLDLLPGGD--LTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1137 PFARRSIWDLLLKYK-QGRTIIIST---HFMDEAdllgDRIAIISSGELRCVGT------SMFLKRKYAEGYNLIVEFTS 1206
Cdd:PLN03130 773 AHVGRQVFDKCIKDElRGKTRVLVTnqlHFLSQV----DRIILVHEGMIKEEGTyeelsnNGPLFQKLMENAGKMEEYVE 848
|
250
....*....|....*....
gi 2041616051 1207 VSDEEELKTHSDENVMNNN 1225
Cdd:PLN03130 849 ENGEEEDDQTSSKPVANGN 867
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1006-1161 |
4.72e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1006 GRNGAGKSTTWSILTGLIPP---TSGTAYIDGWDILT----DIKKIRqnigfTPQHNVLF-DLLT-------VREHL-EF 1069
Cdd:PRK09473 49 GESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNlpekELNKLR-----AEQISMIFqDPMTslnpymrVGEQLmEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1070 FARLKGAADETIDIEIERMLDDLML--TNKRDN-YSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDL 1146
Cdd:PRK09473 124 LMLHKGMSKAEAFEESVRMLDAVKMpeARKRMKmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTL 203
|
170
....*....|....*..
gi 2041616051 1147 L--LKYKQGRTIIISTH 1161
Cdd:PRK09473 204 LneLKREFNTAIIMITH 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1988-2167 |
5.13e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.76 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSV--------LKDIDGVHRN-----LGYCPQF 2054
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnfeklRKHIGIVFQNpdnqfVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2055 D---ALDNlltareHLYFYARLRGIKQQnipyisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEP 2131
Cdd:PRK13648 104 DvafGLEN------HAVPYDEMHRRVSE--------ALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2041616051 2132 TTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEE 2167
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1988-2166 |
5.48e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSV-LKDIDGVHRNLGYCPQfDALDNLL--TAR 2064
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGLVFQ-DPDDQVFssTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 EHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLW 2144
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180
....*....|....*....|..
gi 2041616051 2145 DcILTLTRKEHKSVIITSHSME 2166
Cdd:PRK13647 179 E-ILDRLHNQGKTVIVATHDVD 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1996-2163 |
5.73e-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: 61.34 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLKDIDgvhrnLGYCPQFDALDNLLTAREHlyfyarLRG 2075
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDLK-----ISYKPQYISPDYDGTVEEF------LRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2076 IKQQNIP--YISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDV-------RA-KRFlwd 2145
Cdd:COG1245 425 ANTDDFGssYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlavaKAiRRF--- 501
|
170
....*....|....*...
gi 2041616051 2146 ciltlTRKEHKSVIITSH 2163
Cdd:COG1245 502 -----AENRGKTAMVVDH 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1996-2137 |
5.97e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLKDIDgvhrnLGYCPQFDALDNLLTAREHlyfyarLRG 2075
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-------EVDPELK-----ISYKPQYIKPDYDGTVEDL------LRS 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2076 IKQQ-NIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDV 2137
Cdd:PRK13409 424 ITDDlGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1988-2197 |
6.40e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.99 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLkdIDGvhRNLgycPQFD--ALDN---LLT 2062
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQG-------EIL--LNG--QPI---ADYSeaALRQaisVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2063 AREHLyFYARLRGIKQQNIPYIS-------------GCLLKRL-GLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:PRK11160 421 QRVHL-FSATLRDNLLLAAPNASdealievlqqvglEKLLEDDkGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2129 DEPTTGMDVRAKRFlwdcILTLTRK--EHKSVIITSH---SMEECEVLCnrlsIMVAGEFKCFGSVQHLKAKFG 2197
Cdd:PRK11160 500 DEPTEGLDAETERQ----ILELLAEhaQNKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQELLAQQG 565
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1969-2166 |
6.47e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNA-YVMEHSV---------- 2037
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKnkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2038 --------------LKDIDGVHRNLGYCPQFdALDNLL--TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTL-WADR 2100
Cdd:PRK13651 83 vleklviqktrfkkIKKIKEIRRRVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2101 PVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDcILTLTRKEHKSVIITSHSME 2166
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQGKTIILVTHDLD 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
930-1174 |
7.56e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.72 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 930 NKIR-KRTEYLINLEKNQSENTNELDNRVKQRSasiesysdGEVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRN 1008
Cdd:TIGR03719 286 SKARlARYEELLSQEFQKRNETAEIYIPPGPRL--------GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPN 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1009 GAGKSTTWSILTGLIPPTSGT---------AYIDgwdiltdikkirQNigftpqhnvlfdlltvREHLEffarlkgaADE 1079
Cdd:TIGR03719 358 GAGKSTLFRMITGQEQPDSGTieigetvklAYVD------------QS----------------RDALD--------PNK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1080 TIDIEIERMLDDLMLTNK---------RDNYS--------TELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRS 1142
Cdd:TIGR03719 402 TVWEEISGGLDIIKLGKReipsrayvgRFNFKgsdqqkkvGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
250 260 270
....*....|....*....|....*....|....*
gi 2041616051 1143 IWDLLLKYKqGRTIIIStH---FMdeadllgDRIA 1174
Cdd:TIGR03719 482 LEEALLNFA-GCAVVIS-HdrwFL-------DRIA 507
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1988-2164 |
7.98e-09 |
|
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: 60.84 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLK-DIDGVHRNLGYCPQ----FDA--LDNL 2060
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQdahlFDTtvRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2061 LTAR-----EHLYfyARLRGIKQQNipyisgcLLKRL--GLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:TIGR02868 430 RLARpdatdEELW--AALERVGLAD-------WLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|.
gi 2041616051 2134 GMDVRAKRFLWDCILTLTrkEHKSVIITSHS 2164
Cdd:TIGR02868 501 HLDAETADELLEDLLAAL--SGRTVVLITHH 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1958-2153 |
8.62e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1958 YNDPNNTSHDVLRMTDL---IKVYGwqfgKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIP---LTSGNAY 2031
Cdd:TIGR00956 749 KDMEKESGEDIFHWRNLtyeVKIKK----EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRL 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2032 VMEHSVLKDIdgvHRNLGYCPQFDALDNLLTAREHLYFYARLR-----GIKQQN--IPYIsgclLKRLGLTLWADRPVRQ 2104
Cdd:TIGR00956 825 VNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpksvSKSEKMeyVEEV----IKLLEMESYADAVVGV 897
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2105 YSGG----NKRKLSTAIALIGNP-SVIFMDEPTTGMDVRAKrflWdCILTLTRK 2153
Cdd:TIGR00956 898 PGEGlnveQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTA---W-SICKLMRK 947
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1982-2181 |
8.81e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1982 FGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL---KDIDGVHRNLGYC-PQFdal 2057
Cdd:PRK09493 11 FGPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVfQQF--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2058 dNL---LTAREHLYFYA-RLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:PRK09493 87 -YLfphLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2134 GMDVRakrfLWDCILTLTR---KEHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK09493 166 ALDPE----LRHEVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2004-2139 |
8.86e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.40 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2004 LLGINGSGKSTTFKMLTGEipLTSGnaYVmEHSVL-----KDIDGVHRNLGYCPQFDALDNLLTAREHLYFYARLR---- 2074
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGR--KTGG--YI-EGDIRisgfpKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRlpke 985
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2075 GIKQQNIPYISGCL----LKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:PLN03140 986 VSKEEKMMFVDEVMelveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
974-1180 |
9.88e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIP--PTSGTAYIDGWDIL-TDIKKI-RQNIG 1049
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKaSNIRDTeRAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDLLTVREHLeFFAR---LKGA--ADETIDIEIERMLDDLMLTNKRDNYST-ELSGGMKRKLSIAIAFCANS 1123
Cdd:TIGR02633 82 IIHQELTLVPELSVAENI-FLGNeitLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1124 KTVILDEPTAGVDPFARRSIWDLLLKYKQ-GRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1978-2181 |
1.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.60 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1978 YGWQFGKKFT--AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVME-----HSVLKDIDGVHRNLGY 2050
Cdd:PRK13649 10 YTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitsTSKNKDIKQIRKKVGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2051 CPQFdALDNLL--TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLT--LWADRPVrQYSGGNKRKLSTAIALIGNPSVI 2126
Cdd:PRK13649 90 VFQF-PESQLFeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISesLFEKNPF-ELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2127 FMDEPTTGMDVRAKRFLwdciLTLTRKEHKS---VIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK13649 168 VLDEPTAGLDPKGRKEL----MTLFKKLHQSgmtIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1983-2200 |
1.26e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1983 GKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGE-----IPLTSGNAY--VMEHSVLKDIDGvhrNLGYCPQFD 2055
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNtdgfhIGVEGVITYdgITPEEIKKHYRG---DVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2056 ALDNLLTAREHLYFYARLRGI--------KQQNIPYISGCLLKRLGL-----TLWADRPVRQYSGGNKRKLSTAIALIGN 2122
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCKTPqnrpdgvsREEYAKHIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2123 PSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHS-MEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGD-GY 2200
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQcSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKmGF 307
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1996-2182 |
1.28e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL--KDIDGVHRNLGYCPQ---FDALDNLLTAREHLYFY 2070
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDAIRAGIMLCPEdrkAEGIIPVHSVADNINIS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2071 ARLRGIKqqnipyiSGCLL-------------KRLGL-TLWADRPVRQYSGGNKRK------LSTAIalignpSVIFMDE 2130
Cdd:PRK11288 356 ARRHHLR-------AGCLInnrweaenadrfiRSLNIkTPSREQLIMNLSGGNQQKailgrwLSEDM------KVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2131 PTTGMDVRAKRFLWDCILTLTrKEHKSVIITSHSMEECEVLCNRLSIM----VAGE 2182
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMregrIAGE 477
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1968-2188 |
1.38e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.19 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwqfGKkfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGNAYVMEhsvlKDIDGV-- 2044
Cdd:PRK09452 14 LVELRGISKSFD---GK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETP-DSGRIMLDG----QDITHVpa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 -HRNLGYCPQFDALDNLLTAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNP 2123
Cdd:PRK09452 84 eNRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2124 SVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGS 2188
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1968-2192 |
1.48e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLiKVYgwqFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKML------------TGEIPLTSGNAYVMEH 2035
Cdd:PRK14239 5 ILQVSDL-SVY---YNKK-KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2036 SVL---KDIDGVHRNLGYCPqfdaldnlLTAREHLYFYARLRGIKQQNIpyISGCLLKRL-GLTLWADRPVRQY------ 2105
Cdd:PRK14239 80 DTVdlrKEIGMVFQQPNPFP--------MSIYENVVYGLRLKGIKDKQV--LDEAVEKSLkGASIWDEVKDRLHdsalgl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2106 SGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtrKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKC 2185
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
....*..
gi 2041616051 2186 FGSVQHL 2192
Cdd:PRK14239 228 YNDTKQM 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
988-1180 |
1.52e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdiLTDIKKIRQNIGFTPQHNV----------- 1056
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK---MLLRRRSRQVIELSEQSAAqmrhvrgadma 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1057 ---------LFDLLTVREHLEFFARL-KGAADETIDIEIERMLDDLMLTNKR---DNYSTELSGGMKRKLSIAIAFCANS 1123
Cdd:PRK10261 108 mifqepmtsLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1124 KTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1996-2166 |
1.88e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 56.71 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYvmehsvlkdidgVHRNLGYCPQFDALDNlltarehlyfyARLRg 2075
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS------------VPGSIAYVSQEPWIQN-----------GTIR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2076 ikqQNI----PY--------ISGCLLKR-L--------------GLTLwadrpvrqySGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:cd03250 84 ---ENIlfgkPFdeeryekvIKACALEPdLeilpdgdlteigekGINL---------SGGQKQRISLARAVYSDADIYLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 2041616051 2129 DEPTTGMDVRAKRFLWD-CILTLTRKeHKSVIITSHSME 2166
Cdd:cd03250 152 DDPLSAVDAHVGRHIFEnCILGLLLN-NKTRILVTHQLQ 189
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1989-2187 |
1.99e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 59.38 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYvmehsvlkdIDGVH----------RNLGYCPQ----F 2054
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR---------LDGADlsqwdreelgRHIGYLPQdvelF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2055 DAldnllTAREHLyfyARLRGIKQQNIpyI-----SGC--LLKRL-----------GLTLwadrpvrqySGGNKRKLSTA 2116
Cdd:COG4618 419 DG-----TIAENI---ARFGDADPEKV--VaaaklAGVheMILRLpdgydtrigegGARL---------SGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2117 IALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMeecEVL--CNRLSIMVAGEFKCFG 2187
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1981-2138 |
2.83e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 57.09 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSvLKDIDGVH--RNLGYCPQFDALD 2058
Cdd:PRK13548 11 RLGGR-TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSPAElaRRRAVLPQHSSLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLLTARE--------HLYFYARLRGIKQQnipyisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALI------GNPS 2124
Cdd:PRK13548 89 FPFTVEEvvamgrapHGLSRAEDDALVAA--------ALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170
....*....|....
gi 2041616051 2125 VIFMDEPTTGMDVR 2138
Cdd:PRK13548 161 WLLLDEPTSALDLA 174
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1987-2216 |
2.88e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 58.70 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLKDIDGVH--------RNLGYCPQFDALD 2058
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAG-------TVLVAGDDVEalsaraasRRVASVPQDTSLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLLTARE--------HLYFYARL-----RGIKQQnipyisgclLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSV 2125
Cdd:PRK09536 90 FEFDVRQvvemgrtpHRSRFDTWtetdrAAVERA---------MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2126 IFMDEPTTGMDV-RAKRflwdcILTLTRK---EHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFG------SVQHLKAK 2195
Cdd:PRK09536 161 LLLDEPTASLDInHQVR-----TLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAA 235
|
250 260
....*....|....*....|.
gi 2041616051 2196 FgDGYTIIlRTNAVADIDTLT 2216
Cdd:PRK09536 236 F-DARTAV-GTDPATGAPTVT 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1988-2182 |
2.93e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKML-------TGEIPLTSGNAYVMEHSVLKdidGVHRNLGYCPQ--FDALD 2058
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALlrlvesqGGEIIFNGQRIDTLSPGKLQ---ALRRDIQFIFQdpYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLLTA----REHLYFYARLRG-IKQQNIPYisgcLLKRLGLT---LWadRPVRQYSGGNKRKLSTAIALIGNPSVIFMDE 2130
Cdd:PRK10261 416 PRQTVgdsiMEPLRVHGLLPGkAAAARVAW----LLERVGLLpehAW--RYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2131 PTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1006-1179 |
3.00e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 56.67 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1006 GRNGAGKSTTWSILTGLIPPTSGTAYI---DGW-DILT----DIKKIRQN-IGFTPQH-NVL-----FDLltVREHLeff 1070
Cdd:COG4778 44 GPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvDLAQasprEILALRRRtIGYVSQFlRVIprvsaLDV--VAEPL--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1071 aRLKGAADETIDIEIERMLDDLMLTNKR-DNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLK 1149
Cdd:COG4778 119 -LERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE 197
|
170 180 190
....*....|....*....|....*....|....
gi 2041616051 1150 YK-QGRTII-IsthFMDEA--DLLGDRIAIISSG 1179
Cdd:COG4778 198 AKaRGTAIIgI---FHDEEvrEAVADRVVDVTPF 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1982-2182 |
3.27e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.95 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1982 FGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNayVMEHSvlKDIDG-----VHRNLGYCPQFDA 2056
Cdd:PRK11231 12 YGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGT--VFLGD--KPISMlssrqLARRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2057 LDNLLTARE--------HLYFYARLRGIKQQNIPYIsgclLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:PRK11231 87 TPEGITVRElvaygrspWLSLWGRLSAEDNARVNQA----MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2041616051 2129 DEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
989-1179 |
3.37e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIltdikkirqniGFTPQHNVLFDLLTVREHLE 1068
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-----------QFGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1069 FFARLKGAAdetidieiermLDDLMLTNKRdnYStELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDP-FARR--SIWD 1145
Cdd:COG2401 115 AVELLNAVG-----------LSDAVLWLRR--FK-ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAKRvaRNLQ 180
|
170 180 190
....*....|....*....|....*....|....*
gi 2041616051 1146 LLLKyKQGRTIIISTHFMD-EADLLGDRIAIISSG 1179
Cdd:COG2401 181 KLAR-RAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
989-1181 |
4.27e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDI----LTDIKKIrqnIGFTPQHNVLFDlLTVR 1064
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVakfgLTDLRRV---LSIIPQSPVLFS-GTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1065 EHLEFFArlkgaadETIDIEIERMLDDLMLTNKRDNYSTEL-----------SGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PLN03232 1328 FNIDPFS-------EHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 1134 GV----DPFARRSIWDlllKYKQGRTIIISTHFMDEADLlgDRIAIISSGEL 1181
Cdd:PLN03232 1401 SVdvrtDSLIQRTIRE---EFKSCTMLVIAHRLNTIIDC--DKILVLSSGQV 1447
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1988-2195 |
4.84e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.95 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL-----KDIDGVHRNLGYCPQFDaldnllt 2062
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKPLRKKVGIVFQFP------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2063 arEHLYFYARLR----------GIKQQNIPYISGCLLKRLGLT--LWADRPVrQYSGGNKRKLSTAIALIGNPSVIFMDE 2130
Cdd:PRK13634 95 --EHQLFEETVEkdicfgpmnfGVSEEDAKQKAREMIELVGLPeeLLARSPF-ELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2131 PTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAK 2195
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1979-2167 |
5.52e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.88 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1979 GWQFGKKfTAVNNICAGVKQGEcFGLL-GINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHR-NLGYCPQFDA 2056
Cdd:PRK10247 14 GYLAGDA-KILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRqQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2057 L--DnllTAREHLYFYARLRGIKQQNIPYISGclLKRLGL---TLwaDRPVRQYSGGNKRKlstaIALIGN----PSVIF 2127
Cdd:PRK10247 92 LfgD---TVYDNLIFPWQIRNQQPDPAIFLDD--LERFALpdtIL--TKNIAELSGGEKQR----ISLIRNlqfmPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2041616051 2128 MDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEE 2167
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1001-1167 |
5.58e-08 |
|
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: 55.31 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1001 ITSFLGRNGAGKSTTWS----ILTGLIPPTSgtayiDGWDILTDIkkIRQN-------IGFTpqhNVLFDLLTVREHLEF 1069
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPNS-----KGGAHDPKL--IREGevraqvkLAFE---NANGKKYTITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1070 FarlkgaaDETIDIEIERMLDDLMLTNKRdnysteLSGGMKRKLSIAI------AFCANSKTVILDEPTAGVDPFARR-S 1142
Cdd:cd03240 94 L-------ENVIFCHQGESNWPLLDMRGR------CSGGEKVLASLIIrlalaeTFGSNCGILALDEPTTNLDEENIEeS 160
|
170 180 190
....*....|....*....|....*....|
gi 2041616051 1143 IWDLLLKYKQ--GRTIIISTH---FMDEAD 1167
Cdd:cd03240 161 LAEIIEERKSqkNFQLIVITHdeeLVDAAD 190
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
970-1161 |
6.08e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.80 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGtayidgwDI------LTDIK- 1042
Cdd:PRK10789 312 GELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-------DIrfhdipLTKLQl 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1043 -KIRQNIGFTPQHNVLF-DllTV------------REHLEFFARLKGAADetidieiermlDDLMLTnkrDNYSTE---- 1104
Cdd:PRK10789 385 dSWRSRLAVVSQTPFLFsD--TVannialgrpdatQQEIEHVARLASVHD-----------DILRLP---QGYDTEvger 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1105 ---LSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:PRK10789 449 gvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1989-2232 |
6.22e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKML--------TGEI-----PLT---------SGNAYVMEHsvlkdidgvHR 2046
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypgrwEGEIfidgkPVKirnpqqaiaQGIAMVPED---------RK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 NLGYCPQFDALDNL-LTAREHLYFYARLRGIKQQNIPYISgclLKRLGL-TLWADRPVRQYSGGNKRKLSTAIALIGNPS 2124
Cdd:PRK13549 349 RDGIVPVMGVGKNItLAALDRFTGGSRIDDAAELKTILES---IQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2125 VIFMDEPTTGMDVRAKRFLWDCILTLTrKEHKSVIITSHSMEECEVLCNRLSIMVAGEfkcfgsvqhLKAKFgdgytiil 2204
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVLGLSDRVLVMHEGK---------LKGDL-------- 487
|
250 260
....*....|....*....|....*...
gi 2041616051 2205 rtnavaDIDTLTQyiiEHLPEATLKEKH 2232
Cdd:PRK13549 488 ------INHNLTQ---EQVMEAALRSEH 506
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1968-2132 |
6.62e-08 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 55.77 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL---KDIDGV 2044
Cdd:COG1126 1 MIEIENLHKSFG-----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 HRNLGYCPQ-FdaldNL---LTAREHLyFYA--RLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIA 2118
Cdd:COG1126 76 RRKVGMVFQqF----NLfphLTVLENV-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170
....*....|....
gi 2041616051 2119 LIGNPSVIFMDEPT 2132
Cdd:COG1126 151 LAMEPKVMLFDEPT 164
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1982-2192 |
6.78e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1982 FGKKfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGNAYVMEHSVLK------DIDGVHRNLGYCPQF 2054
Cdd:PRK11432 16 FGSN-TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKP-TEGQIFIDGEDVTHrsiqqrDICMVFQSYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2055 DALDNLltarehlyFYarlrGIKQQNIPyiSGCLLKRLGLTL-------WADRPVRQYSGGNKRKLSTAIALIGNPSVIF 2127
Cdd:PRK11432 94 SLGENV--------GY----GLKMLGVP--KEERKQRVKEALelvdlagFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2128 MDEPTTGMDVRAKRFLWDCIltltRKEHKSVIITS----HSMEECEVLCNRLSIMVAGEFKCFGSVQHL 2192
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKI----RELQQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1962-2214 |
7.49e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1962 NNTSHDVLRMTDLIKVYGWQFGKkFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-----------------EI- 2023
Cdd:PRK09473 6 QQQADALLDVKDLRVTFSTPDGD-VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaangriggsatfngrEIl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2024 ---------------------PLTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNLLTArehlyfyarlrgIKqqnIP 2082
Cdd:PRK09473 85 nlpekelnklraeqismifqdPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDA------------VK---MP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2083 YISgcllKRLGLTlwadrPvRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITS 2162
Cdd:PRK09473 150 EAR----KRMKMY-----P-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMIT 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2163 HSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGDGYTIILrTNAVADIDT 2214
Cdd:PRK09473 220 HDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGL-LNAVPRLDA 270
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1965-2192 |
7.55e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1965 SHDVLRMTDLiKVYGWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKML------------TGEIPLTSGNAYV 2032
Cdd:PRK10261 9 ARDVLAVENL-NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALmrlleqagglvqCDKMLLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2033 ME-----HSVLKDIDGVHRNLGYCPQFDALDNLLTAREHLYFYARL--------------RGIKQQNIPYISGCLlkrlg 2093
Cdd:PRK10261 88 IElseqsAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLhqgasreeamveakRMLDQVRIPEAQTIL----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2094 ltlwaDRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCN 2173
Cdd:PRK10261 163 -----SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIAD 237
|
250
....*....|....*....
gi 2041616051 2174 RLSIMVAGEFKCFGSVQHL 2192
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQI 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
970-1181 |
7.69e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 970 GEVGVEIINLC-KYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL-TDIKKIRQN 1047
Cdd:COG3845 254 GEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITgLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1048 -IGFTP---QHNVLFDLLTVREHL--------EF----FARLKGAADETIDIeIERMldDLMLTNKRDNYSTeLSGGMKR 1111
Cdd:COG3845 334 gVAYIPedrLGRGLVPDMSVAENLilgryrrpPFsrggFLDRKAIRAFAEEL-IEEF--DVRTPGPDTPARS-LSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1112 KLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYK-QGRTII-ISthfmdeADL-----LGDRIAIISSGEL 1181
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLlIS------EDLdeilaLSDRIAVMYEGRI 480
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
989-1152 |
7.94e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.85 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT----DIKKIRQNI---------GFTPQHN 1055
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDIqmvfqdsisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1056 VLFdllTVREHLEFFARLKGAADETIDIEIERMLD-DLMLTNKRdnySTELSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:PRK10419 108 VRE---IIREPLRHLLSLDKAERLARASEMLRAVDlDDSVLDKR---PPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170
....*....|....*...
gi 2041616051 1135 VDPFARRSIWDLLLKYKQ 1152
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQ 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1997-2136 |
9.20e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.41 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1997 KQGECFGLLGINGSGKSTTFKMLT-GEIPlTSGNAYVMEHSV-------LKDIDGVHRNLGYC-------PQFDALDNLL 2061
Cdd:PRK11124 26 PQGETLVLLGPSGAGKSSLLRVLNlLEMP-RSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVfqqynlwPHLTVQQNLI 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 2062 TARehlyfyARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:PRK11124 105 EAP------CRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1996-2163 |
1.12e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.45 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGE-IPltsgnayvmehsvlkdidgvhrNLG-YC--PQFDALDNLLTAREHLYFYA 2071
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKlKP----------------------NLGkFDdpPDWDEILDEFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2072 RLRG------IKQQNIPYI-------SGCLLKR-------------LGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSV 2125
Cdd:cd03236 81 KLLEgdvkviVKPQYVDLIpkavkgkVGELLKKkdergkldelvdqLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2041616051 2126 IFMDEPTTGMDVRaKRFLWDCILTLTRKEHKSVIITSH 2163
Cdd:cd03236 161 YFFDEPSSYLDIK-QRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
937-1167 |
1.31e-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: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 937 EYLINLEKNQS---------ENTNELDNRVKQRSAS-IESYSDGEVGVEIINLCkYYNNKLALKNLSVKFYQNQITSFLG 1006
Cdd:PRK10790 296 EPLIELTTQQSmlqqavvagERVFELMDGPRQQYGNdDRPLQSGRIDIDNVSFA-YRDDNLVLQNINLSVPSRGFVALVG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1007 RNGAGKSTTWSILTGLIPPTSGTAYIDGWDILT-DIKKIRQNIGFTPQHNV-----LFDLLTV-REHLEffARLKGAAdE 1079
Cdd:PRK10790 375 HTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQQDPVvladtFLANVTLgRDISE--EQVWQAL-E 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1080 TIDI-EIERMLDDLMLTNKRDNYSTeLSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIII 1158
Cdd:PRK10790 452 TVQLaELARSLPDGLYTPLGEQGNN-LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV 530
|
250
....*....|..
gi 2041616051 1159 STHFMD---EAD 1167
Cdd:PRK10790 531 IAHRLStivEAD 542
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
988-1180 |
1.34e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKIRQN--IGFTPQHNVLFDLLTVRE 1065
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEagIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1066 HLeFFARLKGAADETID-----IEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFAR 1140
Cdd:PRK10762 99 NI-FLGREFVNRFGRIDwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 1141 RSIWDLLLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGE 1180
Cdd:PRK10762 178 ESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1958-2137 |
1.41e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1958 YNDPNNTSHDVLRMTDLIKVYGWQfgkkfTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmEHSV 2037
Cdd:PRK10636 302 FRAPESLPNPLLKMEKVSAGYGDR-----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-----EIGL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2038 LKDIdgvhrNLGYCPQFDaLDNLLTAREHLYFYARL--RGIKQQNIPYISGCLLKRLGLTlwadRPVRQYSGGNKRKLST 2115
Cdd:PRK10636 372 AKGI-----KLGYFAQHQ-LEFLRADESPLQHLARLapQELEQKLRDYLGGFGFQGDKVT----EETRRFSGGEKARLVL 441
|
170 180
....*....|....*....|..
gi 2041616051 2116 AIALIGNPSVIFMDEPTTGMDV 2137
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDL 463
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1000-1176 |
1.43e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1000 QITSFLGRNGAGKSTTWSILTG-LIPPTSGTAYIDGWD----------ILTDIKKIRQN---IGFTPQHnvlFDLL---- 1061
Cdd:PRK13409 100 KVTGILGPNGIGKTTAVKILSGeLIPNLGDYEEEPSWDevlkrfrgteLQNYFKKLYNGeikVVHKPQY---VDLIpkvf 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1062 --TVREHLEfFARLKGAADETID-IEIERMLDdlmltnkRDnySTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPF 1138
Cdd:PRK13409 177 kgKVRELLK-KVDERGKLDEVVErLGLENILD-------RD--ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2041616051 1139 ARRSIWDLLLKYKQGRTIIISTHfmDEA--DLLGDRIAII 1176
Cdd:PRK13409 247 QRLNVARLIRELAEGKYVLVVEH--DLAvlDYLADNVHIA 284
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
936-1226 |
1.60e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 936 TEYLINLEKnqsenTNELdNRVKQRSASIESYSDGEV-----GVEIINLCKYYNNKLAL---KNLSVKFYQNQITSFLGR 1007
Cdd:PTZ00265 346 TEYMKSLEA-----TNSL-YEIINRKPLVENNDDGKKlkdikKIQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1008 NGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDI--KKIRQNIGFTPQHNVLF----------------DLLTVREHLE- 1068
Cdd:PTZ00265 420 SGCGKSTILKLIERLYDPTEGDIIINDSHNLKDInlKWWRSKIGVVSQDPLLFsnsiknnikyslyslkDLEALSNYYNe 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1069 ------------FFARLKGAAD--------------------------ETIDIEIERMLDDLM--LTNKRDNY----STE 1104
Cdd:PTZ00265 500 dgndsqenknkrNSCRAKCAGDlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVsaLPDKYETLvgsnASK 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1105 LSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHFMDEADlLGDRIAIISSGElr 1182
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRLSTIR-YANTIFVLSNRE-- 656
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2041616051 1183 cvgtsmflKRKYAEGYNLIVEFTSVSDEEELKTHSDENVMNNNS 1226
Cdd:PTZ00265 657 --------RGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNN 692
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1996-2175 |
1.89e-07 |
|
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: 54.04 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGnayvmehSVLkdIDGVhrNLGYCPQFDA------LDNLLTAreHLY 2068
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGfETP-QSG-------RVL--INGV--DVTAAPPADRpvsmlfQENNLFA--HLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2069 FYA----------RLRGIKQQNIPYIsgclLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVR 2138
Cdd:cd03298 87 VEQnvglglspglKLTAEDRQAIEVA----LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2041616051 2139 AKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRL 2175
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRV 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1996-2163 |
1.93e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAY-------VMEH---SVL---------KDIDGVHRnlgycPQF-D 2055
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdeVLKRfrgTELqnyfkklynGEIKVVHK-----PQYvD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2056 ALDNLL--TAREHLyfyARL--RGIKQQnipyisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEP 2131
Cdd:PRK13409 171 LIPKVFkgKVRELL---KKVdeRGKLDE--------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 2041616051 2132 TTGMDVRAKRFLWDCILTLTRKehKSVIITSH 2163
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEG--KYVLVVEH 269
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
987-1181 |
2.06e-07 |
|
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: 56.23 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVKFYQNQIT-------SF----------LGRNGAGKS-TTWSILtGLIPP----TSGTAYIDGWDILT----D 1040
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveavkgvSFdiaagetlalVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGlserE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1041 IKKIRQN-IGF---------TPqhnvlfdLLTV----REHLEFFARLKGAA--DETIDI-------EIERMLDDlmltnk 1097
Cdd:COG4172 86 LRRIRGNrIAMifqepmtslNP-------LHTIgkqiAEVLRLHRGLSGAAarARALELlervgipDPERRLDA------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1098 rdnYSTELSGGMKRKLSIAIAfCANS-KTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTHfmdeaDL-----L 1169
Cdd:COG4172 153 ---YPHQLSGGQRQRVMIAMA-LANEpDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITH-----DLgvvrrF 223
|
250
....*....|..
gi 2041616051 1170 GDRIAIISSGEL 1181
Cdd:COG4172 224 ADRVAVMRQGEI 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1988-2169 |
2.23e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.81 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTG-----EIPLTSGNAYVMEHSVlKDIDGVHRNLGYCpqFDALDNLL- 2061
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPNSKITVDGITLTA-KTVWDIREKVGIV--FQNPDNQFv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 --TAREHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:PRK13640 99 gaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190
....*....|....*....|....*....|
gi 2041616051 2140 KRFLWDCILTLTRKEHKSVIITSHSMEECE 2169
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEAN 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
984-1159 |
2.32e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.54 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 984 NNKLALKNLSVKFYQNQ---ITsflGRNGAGKSTTWSILTGLIPPTSGTayidgWDILTDikkirQNIGFTPQHNvLFDL 1060
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDrllIT---GPSGTGKSSLFRALAGLWPWGSGR-----IGMPEG-----EDLLFLPQRP-YLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 LTVREHLeffarlkgaadetidieiermlddlmltnkrdNY--STELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPF 1138
Cdd:cd03223 78 GTLREQL--------------------------------IYpwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|.
gi 2041616051 1139 ARRSIWDLLlkyKQGRTIIIS 1159
Cdd:cd03223 126 SEDRLYQLL---KELGITVIS 143
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
987-1184 |
3.18e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 987 LALKNLSVKFYQNQIT-----------------SFLGRNGAGKS-TTWSILTGLipPTSGTAYIDGwDIL---------- 1038
Cdd:PRK15134 6 LAIENLSVAFRQQQTVrtvvndvslqieagetlALVGESGSGKSvTALSILRLL--PSPPVVYPSG-DIRfhgesllhas 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1039 -TDIKKIRQN----------IGFTPQHNV---LFDLLTVreHleffarlKGAADETIDIEIERMLDDLMLTN--KRDN-Y 1101
Cdd:PRK15134 83 eQTLRGVRGNkiamifqepmVSLNPLHTLekqLYEVLSL--H-------RGMRREAARGEILNCLDRVGIRQaaKRLTdY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1102 STELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIISSG 1179
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
....*
gi 2041616051 1180 elRCV 1184
Cdd:PRK15134 234 --RCV 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
991-1181 |
3.22e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 991 NLSVKfyQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDG--WDILTDIKKIRQNIGFTPQ---HNVLFDLLTVRE 1065
Cdd:PRK11288 273 SFSVR--AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1066 HLEFFARLK----------GAADETIDIEIERMLddlMLTNKRDNYSTELSGGMKRK------LSIAIafcansKTVILD 1129
Cdd:PRK11288 351 NINISARRHhlragclinnRWEAENADRFIRSLN---IKTPSREQLIMNLSGGNQQKailgrwLSEDM------KVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1130 EPTAGVDPFARRSIWDLLLKY-KQGRTII-ISThfmDEADLLG--DRIAIISSGEL 1181
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELaAQGVAVLfVSS---DLPEVLGvaDRIVVMREGRI 474
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1988-2188 |
3.26e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.22 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV--MEHSVLKDIDGVHRNLGYCPQFDALDNL-LTAR 2064
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgIDTGDFSKLQGIRKLVGIVFQNPETQFVgRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2065 EHLYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLW 2144
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2041616051 2145 DCILTLTRKeHKSVIITSHSMEECEVlCNRLSIMVAGEFKCFGS 2188
Cdd:PRK13644 177 ERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1996-2137 |
3.53e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGN-------------------------AYVME------------HSVL 2038
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdlivarlqqdpprnvegtvyDFVAEgieeqaeylkryHDIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2039 KDI--DGVHRNLGycpQFDALDNLLtarEHL---YFYARlrgIKQqnipyisgcLLKRLGLTlwADRPVRQYSGGNKRKL 2113
Cdd:PRK11147 106 HLVetDPSEKNLN---ELAKLQEQL---DHHnlwQLENR---INE---------VLAQLGLD--PDAALSSLSGGWLRKA 165
|
170 180
....*....|....*....|....
gi 2041616051 2114 STAIALIGNPSVIFMDEPTTGMDV 2137
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
946-1180 |
3.67e-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: 55.56 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 946 QSENTNELDNRVKQRSASIESYSDGEVGVEIINLCKYYNNKlalkNLSV---KFYQNQITSFLGRNGAGKSTTWSILTGL 1022
Cdd:COG1245 314 PEENVRIRDEPIEFEVHAPRREKEEETLVEYPDLTKSYGGF----SLEVeggEIREGEVLGIVGPNGIGKTTFAKILAGV 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1023 IPPTSGtayidgwDILTDIKkirqnIGFTPQH-NVLFDLlTVREHLEffarlkGAADETID--IEIERMLDDLMLTNKRD 1099
Cdd:COG1245 390 LKPDEG-------EVDEDLK-----ISYKPQYiSPDYDG-TVEEFLR------SANTDDFGssYYKTEIIKPLGLEKLLD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1100 NYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKY--KQGRTIIISTHFMDEADLLGDRIaIIS 1177
Cdd:COG1245 451 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaeNRGKTAMVVDHDIYLIDYISDRL-MVF 529
|
...
gi 2041616051 1178 SGE 1180
Cdd:COG1245 530 EGE 532
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1984-2181 |
4.03e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.60 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1984 KKF---TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLT------------GEIPLTSGNAYVMEHSVLKDIDG----V 2044
Cdd:PRK11264 11 KKFhgqTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARSLSQQKGLIRQLRQhvgfV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 HRNLGYCPQFDALDNLL--------TAREHLYFYARLrgikqqnipyisgcLLKRLGLTLWADRPVRQYSGGNKRKLSTA 2116
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIegpvivkgEPKEEATARARE--------------LLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2117 IALIGNPSVIFMDEPTTGMDVRakrfLWDCILTLTR---KEHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPE----LVGEVLNTIRqlaQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1989-2163 |
4.17e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLKDIDGVHRNLGYCPQFDALDNLLTAREHLY 2068
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2069 FYARLrgiKQQNIPYISGCLLKRLGLTLwaDRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAkrflwdcIL 2148
Cdd:PRK13540 97 YDIHF---SPGAVGITELCRLFSLEHLI--DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS-------LL 164
|
170 180
....*....|....*....|.
gi 2041616051 2149 TLTRK--EHK----SVIITSH 2163
Cdd:PRK13540 165 TIITKiqEHRakggAVLLTSH 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
965-1136 |
4.34e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 965 ESYSDGEVGVEIINLCKYYNN-KLALKNLSVkfYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGtayidgwDILTDIKk 1043
Cdd:PRK13409 332 RDESERETLVEYPDLTKKLGDfSLEVEGGEI--YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-------EVDPELK- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1044 irqnIGFTPQH-NVLFDlLTVRehlEFFARLKGAADET-IDIEIER--MLDDLMltnkrDNYSTELSGGMKRKLSIAIAF 1119
Cdd:PRK13409 402 ----ISYKPQYiKPDYD-GTVE---DLLRSITDDLGSSyYKSEIIKplQLERLL-----DKNVKDLSGGELQRVAIAACL 468
|
170
....*....|....*..
gi 2041616051 1120 CANSKTVILDEPTAGVD 1136
Cdd:PRK13409 469 SRDADLYLLDEPSAHLD 485
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
989-1161 |
4.37e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGliPPTSGtaYIDGwDI-LTDIKKIRQNI----GFTPQHNVLFDLLTV 1063
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIrISGFPKKQETFarisGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1064 REHLEFFARLKGAADETIDiEIERMLDDLM----LTNKRDNYS-----TELSGGMKRKLSIAIAFCANSKTVILDEPTAG 1134
Cdd:PLN03140 971 RESLIYSAFLRLPKEVSKE-EKMMFVDEVMelveLDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190
....*....|....*....|....*....|.
gi 2041616051 1135 VDPFA----RRSIWDLLlkyKQGRTIIISTH 1161
Cdd:PLN03140 1050 LDARAaaivMRTVRNTV---DTGRTVVCTIH 1077
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1982-2182 |
6.54e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.98 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1982 FGKK---FTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPL---TSGNAYVMEHSVLKDIDGVHR--------- 2046
Cdd:PRK11022 13 FGDEsapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgrVMAEKLEFNGQDLQRISEKERrnlvgaeva 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2047 ----------NLGYCPQFDALDNLLTAREHLYFYARLRGIKqqnipyisgcLLKRLGLTLWADR----PvRQYSGGNKRK 2112
Cdd:PRK11022 93 mifqdpmtslNPCYTVGFQIMEAIKVHQGGNKKTRRQRAID----------LLNQVGIPDPASRldvyP-HQLSGGMSQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2113 LSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
988-1161 |
6.66e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.59 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIP-PTSGTA---YIDGWDILTDIKKIRQNI--------------G 1049
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAeklEFNGQDLQRISEKERRNLvgaevamifqdpmtS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1050 FTPQHNVLFDLL-TVREHleffarlKGAADETidiEIERMLDDLML------TNKRDNYSTELSGGMKRKLSIAIAFCAN 1122
Cdd:PRK11022 102 LNPCYTVGFQIMeAIKVH-------QGGNKKT---RRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 1123 SKTVILDEPTAGVDPFARRSIWDLLLKYKQGR--TIIISTH 1161
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITH 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1987-2201 |
7.81e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKML------TGEI-----PLTSGNAYVMeHSVLKDIDGVHR--NLGYCPQ 2053
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALlrlinsQGEIwfdgqPLHNLNRRQL-LPVRHRIQVVFQdpNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2054 FDALDNLltaREHLYFYARLRGIKQQNIPYISgcLLKRLGLtlwaDRPVRQ-----YSGGNKRKLSTAIALIGNPSVIFM 2128
Cdd:PRK15134 379 LNVLQII---EEGLRVHQPTLSAAQREQQVIA--VMEEVGL----DPETRHrypaeFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2129 DEPTTGMD--VRAKrflwdcILTLTRK---EHK-SVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHLKAKFGDGYT 2201
Cdd:PRK15134 450 DEPTSSLDktVQAQ------ILALLKSlqqKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1996-2163 |
8.90e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 52.38 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGeIP---LTSGNAYVMEHSVLK-------------------DIDGVhrnlgycpq 2053
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMG-HPkyeVTSGSILLDGEDILElspderaragiflafqypvEIPGV--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2054 fdALDNLLTA------REHLYFYARLRGIKQqnipyisgcLLKRLGLTL-WADRPVRQ-YSGGNKRKLSTAIALIGNPSV 2125
Cdd:COG0396 93 --SVSNFLRTalnarrGEELSAREFLKLLKE---------KMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 2041616051 2126 IFMDEPTTGMDVRAKRFLWDCILTLtRKEHKSVIITSH 2163
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITH 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1969-2167 |
9.17e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1969 LRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYV----MEHSVLKDidgV 2044
Cdd:PRK10253 8 LRGEQLTLGYG-----KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehIQHYASKE---V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2045 HRNLGYCPQFDALDNLLTARE--------HLYFYARLRGIKQQNIpyisGCLLKRLGLTLWADRPVRQYSGGNKRKLSTA 2116
Cdd:PRK10253 80 ARRIGLLAQNATTPGDITVQElvargrypHQPLFTRWRKEDEEAV----TKAMQATGITHLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2117 IALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEE 2167
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQ 206
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
2004-2189 |
1.23e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.95 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2004 LLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHsVLKDID-GVH-----RNLGYC-------PQFDALDNLL-----TARE 2065
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDAEkGIClppekRRIGYVfqdarlfPHYKVRGNLRygmakSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2066 HLYFYARLRGIKQqnipyisgcLLKRLGLTLwadrpvrqySGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWD 2145
Cdd:PRK11144 108 QFDKIVALLGIEP---------LLDRYPGSL---------SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2041616051 2146 CILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSV 2189
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1000-1136 |
1.28e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1000 QITSFLGRNGAGKSTTWSILTG-----LIPPTSGTAYiDGWDiLTDIKK-IRQNIGFTPQHNVLFDLLTVREHLEFFARL 1073
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIASntdgfHIGVEGVITY-DGIT-PEEIKKhYRGDVVYNAETDVHFPHLTVGETLDFAARC 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 1074 KGAAD--ETIDIE--IERMLDDLML---------TNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:TIGR00956 166 KTPQNrpDGVSREeyAKHIADVYMAtyglshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
974-1136 |
1.67e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 974 VEIINLCKYYNNKL--ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL-TDIKKIRQNIGF 1050
Cdd:TIGR00957 1285 VEFRNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1051 TPQHNVLFDlLTVREHLEFFARLkgaADETIDIEIE-RMLDDLM--LTNKRDNYSTE----LSGGMKRKLSIAIAFCANS 1123
Cdd:TIGR00957 1365 IPQDPVLFS-GSLRMNLDPFSQY---SDEEVWWALElAHLKTFVsaLPDKLDHECAEggenLSVGQRQLVCLARALLRKT 1440
|
170
....*....|...
gi 2041616051 1124 KTVILDEPTAGVD 1136
Cdd:TIGR00957 1441 KILVLDEATAAVD 1453
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1971-2163 |
1.68e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.57 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1971 MTDLIKVYG----WQFGKKFTAV-NNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlKDIDGvh 2045
Cdd:PRK10535 1 MTALLELKDirrsYPSGEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-ATLDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2046 rnlgycpqfDALDNLltAREHLYF----YARLRGIK-QQN--IPYI------------SGCLLKRLGLTLWADRPVRQYS 2106
Cdd:PRK10535 78 ---------DALAQL--RREHFGFifqrYHLLSHLTaAQNveVPAVyaglerkqrllrAQELLQRLGLEDRVEYQPSQLS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 2107 GGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWdCILTLTRKEHKSVIITSH 2163
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM-AILHQLRDRGHTVIIVTH 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
978-1166 |
1.79e-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: 53.02 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 978 NLCKYYN-NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDgwdilTDIKkirqnIGFTPQHNV 1056
Cdd:TIGR03719 9 RVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-----PGIK-----VGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1057 LFDLLTVREHLEF-FARLKGAADE-----------------------------------TIDIEIERMLDDLMLTNKrDN 1100
Cdd:TIGR03719 79 LDPTKTVRENVEEgVAEIKDALDRfneisakyaepdadfdklaaeqaelqeiidaadawDLDSQLEIAMDALRCPPW-DA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1101 YSTELSGGMKRKlsiaIAFCA----NSKTVILDEPTAGVDpfARRSIW--DLLLKYKQgrTIIISTH---FMDEA 1166
Cdd:TIGR03719 158 DVTKLSGGERRR----VALCRlllsKPDMLLLDEPTNHLD--AESVAWleRHLQEYPG--TVVAVTHdryFLDNV 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2106-2181 |
1.90e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2106 SGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEhKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD-KGIIIISSEMPELLGITDRILVMSNG 467
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
988-1179 |
2.00e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPptSGTaYiDGwDILTD-----IKKIRQN----IGFTPQHNVLF 1058
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGS-Y-EG-EILFDgevcrFKDIRDSealgIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1059 DLLTVREHLeFF----ARlKGAAD--ETIdIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPT 1132
Cdd:NF040905 91 PYLSIAENI-FLgnerAK-RGVIDwnETN-RRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2041616051 1133 AGVDPFARRSIWDLLLKYK-QGRT-IIIStHFMDEADLLGDRIAIISSG 1179
Cdd:NF040905 168 AALNEEDSAALLDLLLELKaQGITsIIIS-HKLNEIRRVADSITVLRDG 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1980-2166 |
2.70e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.79 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1980 WQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAY----VMEHSVLKDIDGVHR-NLGYCPQF 2054
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRySVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2055 DALDNLlTAREHLYFYARLRgiKQQNIPYISGC-------LLKRLGLTLWADRPVrQYSGGNKRKLSTAIALIGNPSVIF 2127
Cdd:cd03290 88 PWLLNA-TVEENITFGSPFN--KQRYKAVTDACslqpdidLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2041616051 2128 MDEPTTGMDVR-AKRFLWDCILTLTRKEHKSVIITSHSME 2166
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1105-1176 |
2.82e-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: 49.67 E-value: 2.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 1105 LSGGMKRKLSIAIAF----CANSKTVILDEPTAGVDPFARRSIWDLLLK-YKQGRTIIISTHFMDEADLLgDRIAII 1176
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELA-DKLIHI 153
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
970-1033 |
3.14e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 3.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 970 GEVGVEIINLCKYYNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGT---------AYID 1033
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTikigetvklAYVD 393
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1987-2192 |
3.39e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1987 TAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVME-----HSVL--KDIDGVHRNLGYCPQ------ 2053
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllggRSIFnyRDVLEFRRRVGMLFQrpnpfp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2054 FDALDNLLTA-REH-LYFYARLRGIKQQNIPYIS--GCLLKRLgltlwADRPVRqYSGGNKRKLSTAIALIGNPSVIFMD 2129
Cdd:PRK14271 115 MSIMDNVLAGvRAHkLVPRKEFRGVAQARLTEVGlwDAVKDRL-----SDSPFR-LSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2130 EPTTGMDVRAKRFLWDCILTLTrkEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSVQHL 2192
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
986-1161 |
3.64e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 986 KLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDgwdiltdikkirQNIGFTPQHNVLFDLlTVRE 1065
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RSIAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1066 HLEFF-----ARLKGAadetidIEIERMLDDLMLTNKrdNYSTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTA 1133
Cdd:PTZ00243 740 NILFFdeedaARLADA------VRVSQLEADLAQLGG--GLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180
....*....|....*....|....*....
gi 2041616051 1134 GVDP-FARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:PTZ00243 812 ALDAhVGERVVEECFLGALAGKTRVLATH 840
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1005-1161 |
3.73e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.44 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1005 LGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdiltdikkiRQNIGFTPQHNvLFDLLTVREHL-------EFFARlkGAA 1077
Cdd:TIGR00954 484 CGPNGCGKSSLFRILGELWPVYGGRLTKPA----------KGKLFYVPQRP-YMTLGTLRDQIiypdsseDMKRR--GLS 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1078 DEtidiEIERMLDDLMLTN--KRD-------NYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLL 1148
Cdd:TIGR00954 551 DK----DLEQILDNVQLTHilEREggwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR 626
|
170
....*....|...
gi 2041616051 1149 KYkqGRTIIISTH 1161
Cdd:TIGR00954 627 EF--GITLFSVSH 637
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1001-1185 |
3.74e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1001 ITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwDILTDI-KKI-----RQNIGFTPQHNVLFDLLTVREHLEFFARLK 1074
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLFDAeKGIclppeKRRIGYVFQDARLFPHYKVRGNLRYGMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1075 GAA--DETID-IEIERMLDDLMLTnkrdnysteLSGGMKRKLSIAIAFCANSKTVILDEPTAGVD-PFARRsiwdlLLKY 1150
Cdd:PRK11144 105 MVAqfDKIVAlLGIEPLLDRYPGS---------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE-----LLPY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2041616051 1151 -----KQGRT-IIISTHFMDEADLLGDRIAIISSGELRCVG 1185
Cdd:PRK11144 171 lerlaREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
961-1181 |
4.92e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.29 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 961 SASIESYSD-GEVG----VEIINLCKYYNNKL--ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYID 1033
Cdd:cd03288 2 IASISGSSNsGLVGlggeIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1034 GWDILT-DIKKIRQNIGFTPQHNVLFDlLTVREHLEffARLKGAAD---ETIDI-EIERMLD------DLMLTNKRDNYS 1102
Cdd:cd03288 82 GIDISKlPLHTLRSRLSIILQDPILFS-GSIRFNLD--PECKCTDDrlwEALEIaQLKNMVKslpgglDAVVTEGGENFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1103 TelsgGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDEAdLLGDRIAIISSGEL 1181
Cdd:cd03288 159 V----GQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGIL 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1996-2164 |
5.44e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKST---TFKML---------TGEIPLTSGNAYVmehsvlKDIDG--VHRNLGYCPQFDALDNLL 2061
Cdd:PRK14267 27 IPQNGVFALMGPSGCGKSTllrTFNRLlelneearvEGEVRLFGRNIYS------PDVDPieVRREVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 TAREHLYFYARLRGI--KQQNIPYISGCLLKRLglTLWADRPVR------QYSGGNKRKLSTAIALIGNPSVIFMDEPTT 2133
Cdd:PRK14267 101 TIYDNVAIGVKLNGLvkSKKELDERVEWALKKA--ALWDEVKDRlndypsNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190
....*....|....*....|....*....|.
gi 2041616051 2134 GMDVRAKRFLWDCILTLtrKEHKSVIITSHS 2164
Cdd:PRK14267 179 NIDPVGTAKIEELLFEL--KKEYTIVLVTHS 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1985-2135 |
5.55e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1985 KFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEhsvlKDIDG------VHRNLGYCPQFDALD 2058
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDITDwqtakiMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLLTAREHLY---FYARlRGIKQQNIPYISGcLLKRLgltlwADRPVRQ---YSGGNKRKLSTAIALIGNPSVIFMDEPT 2132
Cdd:PRK11614 93 SRMTVEENLAmggFFAE-RDQFQERIKWVYE-LFPRL-----HERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
...
gi 2041616051 2133 TGM 2135
Cdd:PRK11614 166 LGL 168
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1989-2197 |
5.79e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIP--LTSGNAYV-----MEHSVLKDIDG--VHRNLGYCPQ------ 2053
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVtgdvtLNGEPLAAIDAprLARLRAVLPQaaqpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2054 -FDALDNLLTARehlYFYARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIAL---------IGNP 2123
Cdd:PRK13547 97 aFSAREIVLLGR---YPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2124 SVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGEFKCFGSV------QHLKAKFG 2197
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPadvltpAHIARCYG 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1996-2163 |
5.84e-06 |
|
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: 49.45 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTG----EIplTSGNAYvmehsvLKDIDgvhrnlgycpqfdaLDNLLT---AREHLY 2068
Cdd:cd03217 23 IKKGEVHALMGPNGSGKSTLAKTIMGhpkyEV--TEGEIL------FKGED--------------ITDLPPeerARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2069 fyarlrgIKQQNIPYISGCllkRLGLTLwadRPVRQ-YSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCI 2147
Cdd:cd03217 81 -------LAFQYPPEIPGV---KNADFL---RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI 147
|
170
....*....|....*.
gi 2041616051 2148 LTLtRKEHKSVIITSH 2163
Cdd:cd03217 148 NKL-REEGKSVLIITH 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
917-1186 |
5.89e-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: 51.83 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 917 FPFTKTYWfgYD----VNKIR--------KRTEY--------LINLEKNQSENTNELDNRVKQRSASiESYSDGEVGVEI 976
Cdd:TIGR01271 355 FPGAIQTW--YDslgaITKIQdflckeeyKTLEYnlttteveMVNVTASWDEGIGELFEKIKQNNKA-RKQPNGDDGLFF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 977 INLCKYYNNklALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGtayidgwdiltdikKIRQN--IGFTPQH 1054
Cdd:TIGR01271 432 SNFSLYVTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--------------KIKHSgrISFSPQT 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDlLTVREHLEFFArlkgAADE---TIDIEIERMLDDLMLTNKRDNY-----STELSGGMKRKLSIAIAFCANSKTV 1126
Cdd:TIGR01271 496 SWIMP-GTIKDNIIFGL----SYDEyryTSVIKACQLEEDIALFPEKDKTvlgegGITLSGGQRARISLARAVYKDADLY 570
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 1127 ILDEPTAGVDPFARRSIWD-LLLKYKQGRTIIISTHFMDEADlLGDRIAIISSGELRCVGT 1186
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFEsCLCKLMSNKTRILVTSKLEHLK-KADKILLLHEGVCYFYGT 630
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1997-2163 |
8.91e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1997 KQGECFGLLGINGSGKSTTFKMLTGE-IPltsgnayvmehsvlkdidgvhrNLGycpqfdALDNLLTARE---------- 2065
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElKP----------------------NLG------DYDEEPSWDEvlkrfrgtel 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2066 HLYFYARLRG-----IKQQNIPYIS-------GCLLKR-------------LGLTLWADRPVRQYSGGNKRKLSTAIALI 2120
Cdd:COG1245 149 QDYFKKLANGeikvaHKPQYVDLIPkvfkgtvRELLEKvdergkldelaekLGLENILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2041616051 2121 GNPSVIFMDEPTTGMDVRAKRFLWDCILTLTrKEHKSVIITSH 2163
Cdd:COG1245 229 RDADFYFFDEPSSYLDIYQRLNVARLIRELA-EEGKYVLVVEH 270
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1989-2167 |
1.19e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.44 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVL-----KDIDGVHRNLGYCPQFDalDNLL-- 2061
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKKLRKKVSLVFQFP--EAQLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2062 -TAREHLYFYARLRGIKQQNIPYISGCLLKRLGL-TLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:PRK13641 101 nTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180
....*....|....*....|....*...
gi 2041616051 2140 KRFLWDCILTLTRKEHkSVIITSHSMEE 2167
Cdd:PRK13641 181 RKEMMQLFKDYQKAGH-TVILVTHNMDD 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1951-2182 |
1.75e-05 |
|
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: 50.07 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1951 AAERQRLYNDPNNTSHDVLRMTDLiKVY-----GWqFGKK---FTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGE 2022
Cdd:COG4172 258 AAEPRGDPRPVPPDAPPLLEARDL-KVWfpikrGL-FRRTvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2023 IPlTSGNAYVMEHsvlkDIDGVH--------RNLgycpQ------FDALDNLLTAR----EHLYFY-------ARLRGIK 2077
Cdd:COG4172 336 IP-SEGEIRFDGQ----DLDGLSrralrplrRRM----QvvfqdpFGSLSPRMTVGqiiaEGLRVHgpglsaaERRARVA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2078 QqnipyisgcLLKRLGLTL-WADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD--VRAKrflwdcILTLTR-- 2152
Cdd:COG4172 407 E---------ALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsVQAQ------ILDLLRdl 471
|
250 260 270
....*....|....*....|....*....|..
gi 2041616051 2153 -KEHK-SVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:COG4172 472 qREHGlAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1981-2163 |
2.34e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKK--FtavNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGN-----------------AYvMEHSVlkdI 2041
Cdd:PRK15064 10 QFGAKplF---ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNvsldpnerlgklrqdqfAF-EEFTV---L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2042 DGV---HRNLGYCPQ-FDALDNLLTAREHLYF--------YARLRGikqqnipYIS----GCLLKRLGLtlwadrPVRQY 2105
Cdd:PRK15064 83 DTVimgHTELWEVKQeRDRIYALPEMSEEDGMkvadlevkFAEMDG-------YTAearaGELLLGVGI------PEEQH 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2106 SG-------GNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDcILTltrkEHKS-VIITSH 2163
Cdd:PRK15064 150 YGlmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLED-VLN----ERNStMIIISH 210
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1996-2182 |
2.34e-05 |
|
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: 47.18 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAyvmehsvlkDIDGVhrNLGYCPQFDALdnlltarehlyfyarlrg 2075
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND---------EWDGI--TPVYKPQYIDL------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2076 ikqqnipyisgcllkrlgltlwadrpvrqySGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEH 2155
Cdd:cd03222 73 ------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....*..
gi 2041616051 2156 KSVIITSHSMEECEVLCNRLsIMVAGE 2182
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRI-HVFEGE 148
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1027-1161 |
2.36e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1027 SGTAYIDGWDILT-DIKKIRQNIGFTPQHNVLFDLlTVREHLEFfarlkGAADETIDiEIERM-----LDDLM--LTNKR 1098
Cdd:PTZ00265 1276 SGKILLDGVDICDyNLKDLRNLFSIVSQEPMLFNM-SIYENIKF-----GKEDATRE-DVKRAckfaaIDEFIesLPNKY 1348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 1099 DN----YSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLL--LKYKQGRTIIISTH 1161
Cdd:PTZ00265 1349 DTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAH 1417
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1988-2176 |
3.04e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.39 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1988 AVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLkdIDGV----------HRNLGYCPQ---- 2053
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG-------RIL--IDGVdirdltleslRRQIGVVPQdtfl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2054 FDA--LDNLLTAREH-----LYFYARLRGIKQqnipyisgcLLKRL-----------GLTLwadrpvrqySGGNKRKLST 2115
Cdd:COG1132 426 FSGtiRENIRYGRPDatdeeVEEAAKAAQAHE---------FIEALpdgydtvvgerGVNL---------SGGQRQRIAI 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2116 AIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRkeHKSVIITSHsmeecevlcnRLS 2176
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH----------RLS 536
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2103-2196 |
3.09e-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: 49.03 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2103 RQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGE 246
|
90
....*....|....
gi 2041616051 2183 FKCFGSVQHLKAKF 2196
Cdd:TIGR03269 247 IKEEGTPDEVVAVF 260
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
968-1181 |
3.19e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.07 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 968 SDGEVGVEIINLCKY-YNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTsGTAYIDGWDILT-DIKKIR 1045
Cdd:PRK11174 344 SNDPVTIEAEDLEILsPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRElDPESWR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1046 QNIGFTPQHNVLFDLlTVREHLeffarLKG---AADETIDIEIER-----MLDDLML---TNKRDNySTELSGGMKRKLS 1114
Cdd:PRK11174 423 KHLSWVGQNPQLPHG-TLRDNV-----LLGnpdASDEQLQQALENawvseFLPLLPQgldTPIGDQ-AAGLSVGQAQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1115 IAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTHFMDeaDLLG-DRIAIISSGEL 1181
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQwDQIWVMQDGQI 561
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
985-1152 |
3.23e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 985 NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPpTSGTAYIDG-----WD------ILTDIKKIRQ--NIGFT 1051
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGqplhnLNrrqllpVRHRIQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLfdlLTVREHLEFFARLKGAA---DETIDIEIERMLDdlmlTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVIL 1128
Cdd:PRK15134 377 PRLNVL---QIIEEGLRVHQPTLSAAqreQQVIAVMEEVGLD----PETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180
....*....|....*....|....
gi 2041616051 1129 DEPTAGVDPFARRSIWDLLLKYKQ 1152
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQ 473
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2106-2183 |
3.62e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 3.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2106 SGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTrKEHKSVIITSHSMEECEVLCNRLSIMVAGEF 2183
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1981-2181 |
3.96e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1981 QFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTT----FKML--------TGEIPLTSGNAYVMEHSVLKDIDGVHRNL 2048
Cdd:PRK15134 17 QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLpsppvvypSGDIRFHGESLLHASEQTLRGVRGNKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2049 GYCPQFDALDNLLTAREHLYFYARL-RGIKQQNI-PYISGCLlKRLGLTLWADR----PvRQYSGGNKRKLSTAIALIGN 2122
Cdd:PRK15134 97 IFQEPMVSLNPLHTLEKQLYEVLSLhRGMRREAArGEILNCL-DRVGIRQAAKRltdyP-HQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2123 PSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
983-1159 |
5.27e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 983 YNNKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDgwdiltdiKKIRqnIGFTPQHNVLFdLLT 1062
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA--------KGIK--LGYFAQHQLEF-LRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1063 VREHLEFFARLkgAADETidieiERMLDDLM-----LTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDP 1137
Cdd:PRK10636 391 DESPLQHLARL--APQEL-----EQKLRDYLggfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
170 180
....*....|....*....|..
gi 2041616051 1138 FARRSIWDLLLKYkQGRTIIIS 1159
Cdd:PRK10636 464 DMRQALTEALIDF-EGALVVVS 484
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1990-2136 |
5.66e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.72 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1990 NNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlKDIDGVHRNLGYCPQFDALDNLLTAREHLYF 2069
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2070 YARLRGIK----QQNIPYISGCLlkRLGLTLwaDRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:PRK11000 99 GLKLAGAKkeeiNQRVNQVAEVL--QLAHLL--DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
988-1136 |
6.27e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.78 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIL----TDIKKIRQNIGFTPQhNVLFDL--- 1060
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQ-DPLASLnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1061 LTV----REHLEFFaRLKGAADETIDIEIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVD 1136
Cdd:PRK15079 115 MTIgeiiAEPLRTY-HPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
989-1167 |
8.73e-05 |
|
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: 46.17 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAY-----IDGWDILTDIKKIRQNIGFTPQHNVLFDLlTV 1063
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknESEPSFEATRSRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1064 REHLEFFA-----RLKGAADETI---DIEIERMLDDLMLTNKRDNysteLSGGMKRKLSIAIAFCANSKTVILDEPTAGV 1135
Cdd:cd03290 96 EENITFGSpfnkqRYKAVTDACSlqpDIDLLPFGDQTEIGERGIN----LSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 2041616051 1136 D-PFARRSIWDLLLKYKQG--RTIIISTH---FMDEAD 1167
Cdd:cd03290 172 DiHLSDHLMQEGILKFLQDdkRTLVLVTHklqYLPHAD 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1968-2182 |
8.96e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.71 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1968 VLRMTDLIKVY----GWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSvLKDIDG 2043
Cdd:PRK15112 4 LLEVRNLSKTFryrtGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP-LHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2044 VHRNLGYCPQFDALDNLLTAREH--------------LYFYARLRGIKQQnipyisgclLKRLGLtlwadRPVRQY---- 2105
Cdd:PRK15112 83 SYRSQRIRMIFQDPSTSLNPRQRisqildfplrlntdLEPEQREKQIIET---------LRQVGL-----LPDHASyyph 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2106 --SGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAGE 2182
Cdd:PRK15112 149 mlAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
989-1238 |
9.75e-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: 48.02 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 989 LKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGwdiltdikkirqNIGFTPQHNVLFDLlTVREHLE 1068
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQAWIQND-SLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1069 FFARLKGAADETIdIEIERMLDDLMLTNKRDNysTE-------LSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARR 1141
Cdd:TIGR00957 721 FGKALNEKYYQQV-LEACALLPDLEILPSGDR--TEigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1142 SIWDLLLKYK---QGRTIIISTH---FMDEADLlgdrIAIISSGELRCVGT-SMFLKRKYAegynlIVEF--TSVSDEEE 1212
Cdd:TIGR00957 798 HIFEHVIGPEgvlKNKTRILVTHgisYLPQVDV----IIVMSGGKISEMGSyQELLQRDGA-----FAEFlrTYAPDEQQ 868
|
250 260
....*....|....*....|....*.
gi 2041616051 1213 LktHSDENVMNNNSTIDDNASKLVNS 1238
Cdd:TIGR00957 869 G--HLEDSWTALVSGEGKEAKLIENG 892
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1099-1181 |
1.15e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 46.82 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1099 DNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAII 1176
Cdd:COG4170 153 NSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWADTITVL 232
|
....*
gi 2041616051 1177 SSGEL 1181
Cdd:COG4170 233 YCGQT 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2106-2237 |
1.31e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2106 SGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEECE------VLCNR----- 2174
Cdd:PTZ00265 581 SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRyantifVLSNRergst 660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616051 2175 LSIMVAGEFKCFGSVQHlKAKFGDGYTIILRTNAVADIDTLTQYIIEHLPEATLKEKHNKVIH 2237
Cdd:PTZ00265 661 VDVDIIGEDPTKDNKEN-NNKNNKDDNNNNNNNNNNKINNAGSYIIEQGTHDALMKNKNGIYY 722
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1960-2180 |
1.50e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.93 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1960 DPNNTSHDVLRMTDLIKVYGwqfgkKFTAVNNICAGVKQGECFGLLGINGSGKST---TFKMLTGEIP--LTSGNAYVME 2034
Cdd:PRK14243 2 STLNGTETVLRTENLNVYYG-----SFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPgfRVEGKVTFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2035 HSVL-KDID--GVHRNLGYCPQ----FDAldnllTAREHLYFYARLRGIKQQNIPYISGCL------------LKRLGLT 2095
Cdd:PRK14243 77 KNLYaPDVDpvEVRRRIGMVFQkpnpFPK-----SIYDNIAYGARINGYKGDMDELVERSLrqaalwdevkdkLKQSGLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2096 LwadrpvrqySGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLtrKEHKSVIITSHSMEEcevlCNRL 2175
Cdd:PRK14243 152 L---------SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQ----AARV 216
|
....*
gi 2041616051 2176 SIMVA 2180
Cdd:PRK14243 217 SDMTA 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
973-1188 |
1.81e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.38 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 973 GVEIINLCKYYNNKL-ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDIlTDIKKIRQNIGFT 1051
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1052 PQHNVLFDLLTVREHLEFFARLKGAADETID---------IEIERMLDdlmltnKRDNystELSGGMKRKLSIAIAFCAN 1122
Cdd:PRK11650 82 FQNYALYPHMSVRENMAYGLKIRGMPKAEIEervaeaariLELEPLLD------RKPR---ELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1123 SKTVILDEPTAGVDpfAR-RSIWDLLLKYKQGR---TIIISTHFMDEADLLGDRIAIISSGELRCVGTSM 1188
Cdd:PRK11650 153 PAVFLFDEPLSNLD--AKlRVQMRLEIQRLHRRlktTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1989-2181 |
2.04e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.46 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1989 VNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIP----------LTSGNAYVMEHSVLKDIDGVHRNlgycPQfDALD 2058
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqtagrvLLDGKPVAPCALRGRKIATIMQN----PR-SAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2059 NLLTAREHLYFYARLRGiKQQNIPYISGCLlKRLGLtlwaDRPVR-------QYSGGNKRKLSTAIALIGNPSVIFMDEP 2131
Cdd:PRK10418 94 PLHTMHTHARETCLALG-KPADDATLTAAL-EAVGL----ENAARvlklypfEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2132 TTGMDVRAK-RFLwDCILTLTRKEHKSVIITSHSMEECEVLCNRLSIMVAG 2181
Cdd:PRK10418 168 TTDLDVVAQaRIL-DLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2106-2167 |
2.19e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.41 E-value: 2.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2106 SGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSHSMEE 2167
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQ 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1992-2163 |
2.68e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 44.83 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1992 ICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPlTSGNAYVMEHSvLKDIDG----VHRnlGYCPQFDALDNLLTAREHL 2067
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRP-LSDWSAaelaRHR--AYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2068 YFYARLRGIKQQNIPYISgCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALI-----GNPS--VIFMDEPTTGMDVRAK 2140
Cdd:COG4138 91 ALHQPAGASSEAVEQLLA-QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAQQ 169
|
170 180
....*....|....*....|....*.
gi 2041616051 2141 RFLwdciLTLTRKEHK---SVIITSH 2163
Cdd:COG4138 170 AAL----DRLLRELCQqgiTVVMSSH 191
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
988-1161 |
2.69e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 45.34 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFyqNQITSFLGRNGAGKSTTWSILTGL-------IPPTSGTAYIDGWDILTDIKKIRQNIGFTPQ------H 1054
Cdd:COG4938 11 PFKEAELEL--KPLTLLIGPNGSGKSTLIQALLLLlqsnfiyLPAERSGPARLYPSLVRELSDLGSRGEYTADflaeleN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLTVREHLEFFARLKGAADETIDIEIERMLDDLMLTNKRDNYS---TELSGGMKRKLSIAIA-FCANSK--TVIL 1128
Cdd:COG4938 89 LEILDDKSKELLEQVEEWLEKIFPGKVEVDASSDLVRLVFRPSGNGKRiplSNVGSGVSELLPILLAlLSAAKPgsLLII 168
|
170 180 190
....*....|....*....|....*....|....
gi 2041616051 1129 DEPTAGVDPFARRSIWDLLLK-YKQGRTIIISTH 1161
Cdd:COG4938 169 EEPEAHLHPKAQSALAELLAElANSGVQVIIETH 202
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
988-1251 |
2.83e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 988 ALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDGWDILTDIKKirqniGFTPQhnvlfdlLTVREHL 1067
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS-----GLNGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1068 EFFARLKGAADETIDiEIERMLDDLMLTNKRDNYSTE-LSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDL 1146
Cdd:PRK13545 107 ELKGLMMGLTKEKIK-EIIPEIIEFADIGKFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1147 LLKYK-QGRTIIISTHFMDEADLLGDRIAIISSGELRCVGTSMFLKRKYAEgynLIVEFTSVSDEEELKTHSDENVMNNN 1225
Cdd:PRK13545 186 MNEFKeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE---FLKKYNQMSVEERKDFREEQISQFQH 262
|
250 260
....*....|....*....|....*.
gi 2041616051 1226 STIDDNASKLVNSSNIELRTISRNNK 1251
Cdd:PRK13545 263 GLLQEDQTGRERKRKKGKKTSRKFKK 288
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1105-1179 |
3.42e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 3.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 1105 LSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKY-KQGRTIIISTHFMDEadLLG--DRIAIISSG 1179
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPE--LLGitDRILVMSNG 467
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1996-2169 |
4.40e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 45.48 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGnayvmehSVLkdIDGV----------HRNLGycpqfdaldnlLTARE 2065
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG-------QVL--LDGVplvqydhhylHRQVA-----------LVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2066 HLYFyarlRGIKQQNIPYisgcllkrlGLTLWADRPVR----------------------------QYSGGNKRKLSTAI 2117
Cdd:TIGR00958 564 PVLF----SGSVRENIAY---------GLTDTPDEEIMaaakaanahdfimefpngydtevgekgsQLSGGQKQRIAIAR 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2041616051 2118 ALIGNPSVIFMDEPTTGMDVRAKRFLWDciltLTRKEHKSVIITSHSMEECE 2169
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRLSTVE 678
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1100-1180 |
5.79e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1100 NYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQ--GRTIIISTHFMDEADLLGDRIAIIS 1177
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQWADKINVLY 233
|
...
gi 2041616051 1178 SGE 1180
Cdd:PRK15093 234 CGQ 236
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1957-2136 |
6.85e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1957 LYNDPNNTSHDVLRMtdlikvYGWQFGK--KFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLT---SG--- 2028
Cdd:PLN03140 153 LPNAARNIAESALGM------LGINLAKktKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGeit 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2029 -NAYVMEHSVLKdidgvhRNLGYCPQFDALDNLLTAREHLYFYARLRGI--------------KQQNI------------ 2081
Cdd:PLN03140 227 yNGYRLNEFVPR------KTSAYISQNDVHVGVMTVKETLDFSARCQGVgtrydllselarreKDAGIfpeaevdlfmka 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616051 2082 --------PYISGCLLKRLGL-----TLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:PLN03140 301 tamegvksSLITDYTLKILGLdickdTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLD 368
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2003-2136 |
7.41e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.54 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2003 GLLGINGSGKSTTFKMLTGeipltsgnayvmehsVLKDIDGVHR-----NLGYCPQFDALDNLLTAREHLY--------- 2068
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAG---------------VDKDFNGEARpqpgiKVGYLPQEPQLDPTKTVRENVEegvaeikda 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2069 ------FYARL------------RGIKQQNIpyISGC----LLKRLGLTLWA------DRPVRQYSGGNKRKLSTAIALI 2120
Cdd:TIGR03719 100 ldrfneISAKYaepdadfdklaaEQAELQEI--IDAAdawdLDSQLEIAMDAlrcppwDADVTKLSGGERRRVALCRLLL 177
|
170
....*....|....*.
gi 2041616051 2121 GNPSVIFMDEPTTGMD 2136
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLD 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1996-2136 |
1.33e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.55 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTG-EIPlTSGNAYVMEHSVLK----DIDGVHRNLGYCPQFDALDNLLTAREHLYFY 2070
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLICGiERP-SAGKIWFSGHDITRlknrEVPFLRRQIGMIFQDHHLLMDRTVYDNVAIP 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2071 ARLRGIKQQNIPYISGCLLKRLGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMD 2136
Cdd:PRK10908 104 LIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2101-2166 |
1.39e-03 |
|
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: 43.15 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2101 PVRQYSGGNKRKLSTAIALI---GNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKsVIITSHSME 2166
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQ-LILTTHSPL 300
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2004-2139 |
1.65e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2004 LLGINGSGKSTTFKMLTGEIPLTSGN---------AYVMEHSVlkdidgvhrnlgycpqfDALDnlLTAREHLYFYARLR 2074
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTvfrsakvrmAVFSQHHV-----------------DGLD--LSSNPLLYMMRCFP 600
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041616051 2075 GIKQQNIPyisgCLLKRLGLT-LWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRA 2139
Cdd:PLN03073 601 GVPEQKLR----AHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1978-2163 |
1.89e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1978 YGWQFGKKFTAVNNICAGVKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVlkdidgvhrnlGYCPQFDAL 2057
Cdd:PLN03232 622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSV-----------AYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2058 DNLlTAREHLYFYARL------RGIK----QQNIPYISGCLLKRLGltlwaDRPVrQYSGGNKRKLSTAIALIGNPSVIF 2127
Cdd:PLN03232 691 FNA-TVRENILFGSDFeserywRAIDvtalQHDLDLLPGRDLTEIG-----ERGV-NISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190
....*....|....*....|....*....|....*.
gi 2041616051 2128 MDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSH 2163
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ 799
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2093-2166 |
1.93e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616051 2093 GLTLWAD---RPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAkrFLWdcILTLTRKEHKSVIITSHSME 2166
Cdd:PLN03073 330 GLSFTPEmqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA--VLW--LETYLLKWPKTFIVVSHARE 402
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1996-2221 |
2.05e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1996 VKQGECFGLLGINGSGKSTTFKMLTGEIPLTSGNAYVMEHSVLK-DIDGVHRNLGYCPQFDALD------NLLTAREH-- 2066
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFsgtvrfNIDPFSEHnd 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2067 -----LYFYARLRGIKQQNiPYisgcllkrlGLTLWADRPVRQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKR 2141
Cdd:PLN03232 1339 adlweALERAHIKDVIDRN-PF---------GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 2142 FLWDCIltltRKEHKS--VIITSHSMEECeVLCNRLSIMVAGEFKCFGSVQHLKAKFGDGYTIILRTNAVADIDTLTQYI 2219
Cdd:PLN03232 1409 LIQRTI----REEFKSctMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQYLSNLV 1483
|
..
gi 2041616051 2220 IE 2221
Cdd:PLN03232 1484 FE 1485
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
998-1130 |
2.48e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 998 QNQITSFLGRNGAGKSTT-WSILTGLIPPTSGTAYIDGWDILTDIKKIRQNIGFTPQHNVLFDLLTVRehlEFFARLKGA 1076
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLaRALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR---LALALARKL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2041616051 1077 ADETIDI-EIERMLDDLMLTNKRDNYSTELSGGMKRKLSIAIaFCANSKTVILDE 1130
Cdd:smart00382 78 KPDVLILdEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV-ILTTNDEKDLGP 131
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1006-1159 |
2.93e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 42.87 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1006 GRNGAGKSTTWSILTGLIPPTSGTAYI-DGWDILtdikkirqnigFTPQHNVLFdLLTVREHLeffarLKGAADETI-DI 1083
Cdd:COG4178 396 GPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL-----------FLPQRPYLP-LGTLREAL-----LYPATAEAFsDA 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1084 EIERMLDDLMLT------NKRDNYSTELSGGMKRKLSIAIAFCANSKTVILDEPTAGVDPFARRSIWDLLLKYKQGrTII 1157
Cdd:COG4178 459 ELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG-TTV 537
|
..
gi 2041616051 1158 IS 1159
Cdd:COG4178 538 IS 539
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2103-2163 |
3.27e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 3.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616051 2103 RQYSGGNKRKLSTAIALIGNPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHKSVIITSH 2163
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1055-1161 |
5.48e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1055 NVLFDLLtvREHLEFFAR----LKGAADETIDIEIERMLDD---LMLT---NKRDNYSTELSGGMKRKLSIAIAFCANS- 1123
Cdd:COG4637 201 AVLATLR--ETHPERFERileaLRDAFPGFEDIEVEPDEDGrvlLEFRekgLDRPFPARELSDGTLRFLALLAALLSPRp 278
|
90 100 110
....*....|....*....|....*....|....*....
gi 2041616051 1124 -KTVILDEPTAGVDPFARRSIWDLLLKYKQGRTIIISTH 1161
Cdd:COG4637 279 pPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
2100-2165 |
5.72e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 5.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616051 2100 RPVRQYSGGNKRKLSTAIALIG---NPSVIFMDEPTTGMDVRAKRFLWDCILTLTRKEHkSVIITSHSM 2165
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNM 872
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
981-1164 |
9.22e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 981 KYYN-NKLALKNLSVKFYQNQITSFLGRNGAGKSTTWSILTGLIPPTSGTAYIDgwdilTDIKkirqnIGFTPQHNVLFD 1059
Cdd:PRK11819 14 KVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-----PGIK-----VGYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1060 LLTVREHLEF-FARLKGAADE-----------------------------------TIDIEIERMLDDLMLTNKrDNYST 1103
Cdd:PRK11819 84 EKTVRENVEEgVAEVKAALDRfneiyaayaepdadfdalaaeqgelqeiidaadawDLDSQLEIAMDALRCPPW-DAKVT 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616051 1104 ELSGGMKRKlsiaIAFC----ANSKTVILDEPTAGVDpfARRSIW--DLLLKYKqGrTIIISTH---FMD 1164
Cdd:PRK11819 163 KLSGGERRR----VALCrlllEKPDMLLLDEPTNHLD--AESVAWleQFLHDYP-G-TVVAVTHdryFLD 224
|
|
| |
