|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3036-5019 |
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: 1111.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3036 VKIKDLMRNITKFTEDLRSFFHISEETIHSILEANISHSKVLSSVLTIALSG-KCDEEILHLLLTFPESEKSWFVTRELC 3114
Cdd:TIGR01257 151 IRIRDILKDEEALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAYGVPDLELKDiACSEALLERFIIFSQRRGAQTVRDALC 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3115 SLPGSQVFSLLVMMGQNLNLRNL--IYKTLIPSEANGL-LKSLLDVVASLSSilaRAQhaleylpEFLHTFKITALL--D 3189
Cdd:TIGR01257 231 SLSQGTLQWIEDTLYANVDFFKLfhVLPTLLDSRSQGInLRSWGGILSDMSP---RIQ-------EFIHRPSVQDLLwvT 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3190 MPDFQQVSSKgqtrssAFASFQSVMK-LLCKDQESFLSNSNMFinlprvnELLEDNKEKFNIPHDST------------- 3255
Cdd:TIGR01257 301 RPLLQNGGPE------TFTQLMGILSdLLCGYPEGGGSRVFSF-------NWYEDNNYKAFLGIDSTrkdpiysydkrtt 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3256 PFCLKLYQEILQSPNGALVWSFLKPVLHGKILYTPNSPEINEVIQKANYTFYFVDKIKVLSETFLKIS-KLFQGSGNGQM 3334
Cdd:TIGR01257 368 SFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGpQIWYFFDKSTQ 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3335 FNQLQDALRNKFIRNFVESQLHID---------------MDKLTEDLQTYGrmLDKMFNHVEaghfRFLggMLAN-LSSC 3398
Cdd:TIGR01257 448 MTMIRDTLQNPTVKDFINRQLGEEgitaeavlnflyngpREKQADDMTNFD--WRDIFNITD----RFL--RLANqYLEC 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3399 VVLDRFQAVETVDTLETKAHELMQQNSFLASIIFNSslrhrhIRSAPHKLPPHVTYTIRTNVLYSMRTDMIKNPSWKFHP 3478
Cdd:TIGR01257 520 LVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPD------MYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGP 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3479 QNLPAGGFKYNYI-FVPLQDMIERAIIVVQTgQESLEPTTQAQAAPYPCHTSDLFLNNVGFFFPLIMMLTWMVAVASMVR 3557
Cdd:TIGR01257 594 RADPVEDFRYIWGgFAYLQDMVEQGITRSQM-QAEPPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVK 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3558 KLVYEREIQIEEYMRMMGLHPTIHFLSWFLENMATLALSSAALAVILKMSGIFMHSDAFIIFLYLLDFGVSAVMMSYFLS 3637
Cdd:TIGR01257 673 SIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLS 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3638 VFFNQANTAALCTSLGYMISFLPYVVLLVLHNQLSFAIQTLLCLLSTTAFGQGVFFITFLEGQEEGIQWGNMYRAPEPGG 3717
Cdd:TIGR01257 753 TFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGD 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3718 -MTFGWVCWMILFDAILYFLGGWYFSNLVPGTFGLGKPWYFPFTASYW--KSICGLMERRRCSLSSGLFFFNEDFGN-KG 3793
Cdd:TIGR01257 833 eFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWlgGEGCSTREERALEKTEPLTEEMEDPEHpEG 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3794 LSQQNGPGEMEGGNPGVALISVTKEYEDH-KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGK 3872
Cdd:TIGR01257 913 INDSFFERELPGLVPGVCVKNLVKIFEPSgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK 992
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3873 NLQTDLSKVREELGVCPQQDVLLDNLTVREHLMLFASIKAPWWttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKL 3952
Cdd:TIGR01257 993 DIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW--EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKL 1070
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3953 SIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNC 1150
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4033 YGQGLTLTLSKQ--------------------------PSILETQEPK-----DVARVTSLIQIYIPQAFLKDSCGGELT 4081
Cdd:TIGR01257 1151 FGTGFYLTLVRKmkniqsqrggcegtcsctskgfstrcPARVDEITPEqvldgDVNELMDLVYHHVPEAKLVECIGQELI 1230
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4082 YTIP-KDADRTCFKGLCQALDQNLQHLHLTGYGISDTTLEEVFLMLLQDTNKKSYITPDNKVEPQNERPVGPLS------ 4154
Cdd:TIGR01257 1231 FLLPnKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKRENANLRHPCSgpteka 1310
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4155 ------PHNVSP--LSTPPEGA-LPEPIG-------GCQLLLGQAVALLRKRLLHTLRAWKSTTSDLLLPVLFVALAMGL 4218
Cdd:TIGR01257 1311 gqtpqaSHTCSPgqPAAHPEGQpPPEPEDpgvplntGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALML 1390
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4219 FMVQPLAITYPPLKLTPGHYETAETyFFSSGNHGPD----LTHVLLRKFRDQDPVCADAFR-----MNSSSW-------- 4281
Cdd:TIGR01257 1391 SIIIPPFGEYPALTLHPWMYGQQYT-FFSMDEPNSEhlevLADVLLNKPGFGNRCLKEEWLpeypcGNSTPWktpsvspn 1469
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4282 -----HRDPYSGPESQDSCGCL---------KCPNKSAG--APSLTNCLGHTLLNLSGYDVEEYL------LVPSA---- 4335
Cdd:TIGR01257 1470 ithlfQKQKWTAAHPSPSCRCStrekltmlpECPEGAGGlpPPQRTQRSTEILQDLTDRNISDFLvktypaLIRSSlksk 1549
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4336 ----KPRLGGWSFGGQIP-------------NDAEDVKTNTSKPRTLA------------------KVWYNQKGFHSLPS 4380
Cdd:TIGR01257 1550 fwvnEQRYGGISIGGKLPaipitgealvgflSDLGQMMNVSGGPVTREaskempdflkhletedniKVWFNNKGWHALVS 1629
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4381 YLNHLNNLILWHHLPANAvDWRQYGITLYSHPYG--GALLNEDRILESIRQCGVALCIVLGFSILSASIGSSVVRDRVTG 4458
Cdd:TIGR01257 1630 FLNVAHNAILRASLPKDR-DPEEYGITVISQPLNltKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNK 1708
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4459 AKRLQHISGLGHRTYWLINFLYDMLFYLVSVCLCVAVIGAFQLTAFTFRENLAATALLLALFGYAMIPWMYLMSRIFSSS 4538
Cdd:TIGR01257 1709 AKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVP 1788
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4539 DVAFISYISLNFIFGLCTMLMTTmprLLAIISKAQNLQKIYNVLKWAFTIFPQFCLGQGLIELCYNQIKYDLTHNFGIDS 4618
Cdd:TIGR01257 1789 STAYVALSCANLFIGINSSAITF---VLELFENNRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEH 1865
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4619 YVSPFEMNFLGWIFVELTLQGT--FLLLLRLMLHGDLLRWprdhsvlqdIVKPAK------DIDVETEQMRVLEGRTGGD 4690
Cdd:TIGR01257 1866 SANPFQWDLIGKNLVAMAVEGVvyFLLTLLIQHHFFLSRW---------IAEPAKepifdeDDDVAEERQRIISGGNKTD 1936
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytvirtpqgdmvDLASAGK 4770
Cdd:TIGR01257 1937 ILRLNELTKVYS---GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG------------DATVAGK 2001
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AgIL---------IGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLS 4841
Cdd:TIGR01257 2002 S-ILtnisdvhqnMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLS 2080
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4842 TALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNR 4921
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4922 FGDGY--TVKVWLHKEGSQP--SAVSDCLKLHFPGIQFKGQRLNLLEYHVQKSweCLADLFKVLENNKSLLNIEHYSISQ 4997
Cdd:TIGR01257 2161 FGDGYivTMKIKSPKDDLLPdlNPVEQFFQGNFPGSVQRERHYNMLQFQVSSS--SLARIFQLLISHKDSLLIEEYSVTQ 2238
|
2170 2180
....*....|....*....|..
gi 116292744 4998 TTLEQVFVNFATEQLQTPCFPV 5019
Cdd:TIGR01257 2239 TTLDQVFVNFAKQQTETYDLPL 2260
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4692-4919 |
5.13e-92 |
|
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: 298.65 E-value: 5.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4692 MVLCNLSKSYRSvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqgDMVDLASAGKA 4771
Cdd:cd03263 1 LQIRNLTKTYKK---GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN----GYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GILIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPD 4851
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLWQTItQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIK 4919
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLI-LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3815-4030 |
9.71e-92 |
|
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: 297.88 E-value: 9.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYE-DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDV 3893
Cdd:cd03263 6 LTKTYKkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 LLDNLTVREHLMLFASIKAPwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:cd03263 86 LFDELTVREHLRFYARLKGL--PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3974 VDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLK 4030
Cdd:cd03263 164 LDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3815-4033 |
5.69e-79 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 261.92 E-value: 5.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDVL 3894
Cdd:COG1131 6 LTKRYGD-KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGV 3974
Cdd:COG1131 85 YPDLTVRENLRFFARLYG--LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3975 DPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETY 4033
Cdd:COG1131 163 DPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4696-4922 |
1.82e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 251.91 E-value: 1.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYtvIRTPQGDMVDLASAGKAgiLI 4775
Cdd:COG1131 5 GLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE--VRVLGEDVARDPAEVRR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLL 4855
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4856 DEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNRF 4922
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3810-4020 |
3.40e-59 |
|
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: 202.63 E-value: 3.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYeDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCP 3889
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDVLLDNLTVREHLMLfasikapwwttkelqqqvnktldeveltqhqhkpagvlSGGMKRKLSIGIAFMGMSKTVVLDE 3969
Cdd:cd03230 80 EEPSLYENLTVRENLKL--------------------------------------SGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3970 PSSGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3812-4035 |
7.64e-59 |
|
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: 204.71 E-value: 7.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3812 LISVTKEYeDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQ 3891
Cdd:COG4555 4 VENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLDNLTVREHLMLFASIKAPWwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLF--DEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3972 SGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETYGQ 4035
Cdd:COG4555 161 NGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4696-4919 |
9.26e-55 |
|
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: 191.81 E-value: 9.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSG------YTVIRTPqgdmvdlasaG 4769
Cdd:cd03265 5 NLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvagHDVVREP----------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGILIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGK 4849
Cdd:cd03265 70 EVRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4850 PDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIK 4919
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3815-4030 |
5.92e-54 |
|
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: 189.50 E-value: 5.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHkVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDVL 3894
Cdd:cd03265 6 LVKKYGDF-EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFASIKA-PWwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:cd03265 85 DDELTGWENLYIHARLYGvPG---AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3974 VDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLK 4030
Cdd:cd03265 162 LDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
3817-4126 |
3.55e-52 |
|
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: 187.60 E-value: 3.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3817 KEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDVLLD 3896
Cdd:TIGR01188 1 KVYGDFK-AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 NLTVREHLMLFASIKA-PWWttkELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVD 3975
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGlPKD---EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3976 PCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETYGqGLTLTlskqpsiLETQEPK 4054
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLE-------SRPRDIQ 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4055 DVARVTSLIQIYIPQAFLKDSC----GGELTYTIPkDADRTCFKGLcQALDQNlqHLHLTGYGISDTTLEEVFLML 4126
Cdd:TIGR01188 229 SLKVEVSMLIAELGETGLGLLAvtvdSDRIKILVP-DGDETVPEIV-EAAIRN--GIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4696-4907 |
1.03e-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: 181.44 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPQGDMVDLASAGKAgiLI 4775
Cdd:cd03230 5 NLSKRY-----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG--EIKVLGKDIKKEPEEVKR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYycrlrgipkqyipevaadlvrrlhleshvdkpvatySGGTRRKLSTALALVGKPDILLL 4855
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4856 DEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4691-4924 |
1.85e-50 |
|
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: 180.44 E-value: 1.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSVFggkttAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAG- 4769
Cdd:COG4555 1 MIEVENLSKKYGKVP-----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-----DGEDVRKEPr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGILIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGK 4849
Cdd:COG4555 71 EARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4850 PDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNRFGD 4924
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3812-4131 |
3.19e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 176.07 E-value: 3.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3812 LISVTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqtDLSKVR------EEL 3885
Cdd:COG4152 4 LKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL--DPEDRRrigylpEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3886 GvcpqqdvLLDNLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:COG4152 81 G-------LYPKMKVGEQLVYLARLKG--LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETYG-QGLTLTLSK 4043
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGrNTLRLEADG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4044 QPSILetqepKDVARVTSLiqiyipqaflkDSCGGELTYTIPKDADRTcfkglcQALDQNLQHLHLTGYGISDTTLEEVF 4123
Cdd:COG4152 232 DAGWL-----RALPGVTVV-----------EEDGDGAELKLEDGADAQ------ELLRALLARGPVREFEEVRPSLNEIF 289
|
....*...
gi 116292744 4124 LMLLQDTN 4131
Cdd:COG4152 290 IEVVGEKA 297
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3810-4029 |
3.56e-46 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 167.51 E-value: 3.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVC 3888
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PQQ-DVLLDNLTVREHLMLfasikAP---WWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSI-GIAFMGmSK 3963
Cdd:COG1122 81 FQNpDDQLFAPTVEEDVAF-----GPenlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIaGVLAME-PE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3964 TVVLDEPSSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3810-4021 |
1.55e-45 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 165.06 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYeDHKVAVQELTLTFhRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCP 3889
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDVLLDNLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDE 3969
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKG--IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3970 PSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3815-4021 |
8.29e-45 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 162.77 E-value: 8.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQtDLSKVREELGVCPQQDVL 3894
Cdd:cd03268 6 LTKTYGKKRV-LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIEAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFASIKApwwttkELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGV 3974
Cdd:cd03268 84 YPNLTARENLRLLARLLG------IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3975 DPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:cd03268 158 DPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3810-4023 |
1.32e-44 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 162.45 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDlskVREELGVCP 3889
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDVLLDNLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDE 3969
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKG--LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3970 PSSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCY 4023
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4696-4910 |
6.63e-44 |
|
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: 160.44 E-value: 6.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGeCFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDlASAGKAGI-- 4773
Cdd:cd03264 5 NLTKRY-----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI-----DGQD-VLKQPQKLrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 LIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDIL 4853
Cdd:cd03264 73 RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4854 LLDEPSSGMDPcSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFR 4910
Cdd:cd03264 153 IVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4696-4907 |
7.27e-44 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 160.14 E-value: 7.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLAsagkAGILI 4775
Cdd:cd03269 5 NVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF---DGKPLDIA----ARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLL 4855
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4856 DEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4696-4908 |
1.01e-43 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 159.69 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPQGDMVDLASA-GKAGIL 4774
Cdd:cd03268 5 DLTKTY-----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG--EITFDGKSYQKNIEAlRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 IGYcPqqdALDELLTGWEHLQYYCRLRGIPKQYIPEVaadlVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILL 4854
Cdd:cd03268 78 IEA-P---GFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4855 LDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGS 4908
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4691-4907 |
1.21e-42 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 157.14 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSVfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGK 4770
Cdd:cd03266 1 MITADALTKRFRDV-KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-----DGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGIL-IGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGK 4849
Cdd:cd03266 75 EARRrLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4850 PDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4691-5011 |
1.32e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 159.89 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVirTPQGDMVDLASAGK 4770
Cdd:COG4152 1 MLELKGLTKRF-----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG-EV--LWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 agilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:COG4152 73 ----IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNRFGdgyTVKV 4930
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG---RNTL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4931 WLHKEGSQPSAvsdclkLHFPGI---QFKGQRLNL-LEYHVQKSweclaDLFKVLennKSLLNIEHYSISQTTLEQVFVN 5006
Cdd:COG4152 226 RLEADGDAGWL------RALPGVtvvEEDGDGAELkLEDGADAQ-----ELLRAL---LARGPVREFEEVRPSLNEIFIE 291
|
....*
gi 116292744 5007 FATEQ 5011
Cdd:COG4152 292 VVGEK 296
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4694-4916 |
2.81e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 160.38 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfGGKTTaVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSG-YTVIRTPQGDMVDLASAGkag 4772
Cdd:PRK13536 44 LAGVSKSY----GDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGkITVLGVPVPARARLARAR--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4773 ilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDI 4852
Cdd:PRK13536 116 --IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4853 LLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQ 4916
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3815-4006 |
9.05e-42 |
|
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: 154.17 E-value: 9.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDVL 3894
Cdd:COG4133 8 LSCRRGERLL-FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFASIKAPWWTTKELQQqvnkTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGV 3974
Cdd:COG4133 87 KPELTVRENLRFWAALYGLRADREAIDE----ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|...
gi 116292744 3975 DPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAE 4006
Cdd:COG4133 163 DAAGVALLAELIAAHLArGGAVLLTTHQPLELA 195
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3821-4039 |
6.61e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.94 E-value: 6.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQtdlsKVREELGVCPQQDVLLDN--L 3898
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIGYVPQRAEVDWDfpI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3899 TVREHLM--LFASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDP 3976
Cdd:COG1121 93 TVRDVVLmgRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3977 CSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLrCYAPPAD------LKETYGQGLTL 4039
Cdd:COG1121 173 ATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEvltpenLSRAYGGPVAL 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3803-4015 |
1.87e-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: 152.17 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3803 MEGGNPGVALISVTKEY---EDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtDLS 3879
Cdd:COG1116 1 MSAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK----PVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3880 KVREELGVCPQQDVLLDNLTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFM 3959
Cdd:COG1116 77 GPGPDRGVVFQEPALLPWLTVLDNVAL--GLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3960 GMSKTVVLDEPSSGVDPCSRRSLWDILLKY--REGRTIIFTTHHLDEAEMLSDHVAVL 4015
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3824-4020 |
2.28e-40 |
|
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: 152.12 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3824 VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLsKVRE--ELGVC-----PQqdvLLD 3896
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGL-PPHRiaRLGIArtfqnPR---LFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 NLTVREHLML----------FASIKAPWWTTK---ELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSK 3963
Cdd:COG0411 93 ELTVLENVLVaaharlgrglLAALLRLPRARReerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3964 TVVLDEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4696-4916 |
4.80e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 152.65 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPqGDMVDlASAGKAGILI 4775
Cdd:PRK13537 12 NVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAG--SISLC-GEPVP-SRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLL 4855
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4856 DEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQ 4916
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3815-4034 |
4.81e-40 |
|
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: 150.96 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT----DLSKVreeLGVCPQ 3890
Cdd:COG1120 7 LSVGYGGRPV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsrrELARR---IAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREHLML--FASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:COG1120 83 EPPAPFGLTVRELVALgrYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3969 EPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPAD------LKETYG 4034
Cdd:COG1120 163 EPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvltpelLEEVYG 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4691-4889 |
5.12e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 149.17 E-value: 5.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLASAGK 4770
Cdd:COG4133 2 MLEAENLSCRR-----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAG-EVLWNGEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AgilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQyiPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:COG4133 76 R---LAYLGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSH 4889
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3815-4015 |
9.61e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 148.77 E-value: 9.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYED---HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtDLSKVREELGVCPQQ 3891
Cdd:cd03293 6 VSKTYGGgggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE----PVTGPGPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLDNLTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:cd03293 82 DALLPWLTVLDNVAL--GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116292744 3972 SGVDPCSRRSLWDILLK--YREGRTIIFTTHHLDEAEMLSDHVAVL 4015
Cdd:cd03293 160 SALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3815-4032 |
4.48e-39 |
|
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: 147.65 E-value: 4.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL----QTDLSKVREELGVCPQ 3890
Cdd:cd03261 6 LTKSFGGRTV-LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTV--------REHLMLFASikapwwttkELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMS 3962
Cdd:cd03261 85 SGALFDSLTVfenvafplREHTRLSEE---------EIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3963 KTVVLDEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3815-4032 |
6.25e-39 |
|
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: 147.43 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT----DLSKVREELGVCPQ 3890
Cdd:COG1127 11 LTKSFGDRVV-LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELRRRIGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTV--------REHLMLfasikapwwTTKELQQQVNKTLDEVELTQHQHK-PAGvLSGGMKRKlsIGIAfmgm 3961
Cdd:COG1127 90 GGALFDSLTVfenvafplREHTDL---------SEAEIRELVLEKLELVGLPGAADKmPSE-LSGGMRKR--VALA---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3962 sKTVVL-------DEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:COG1127 154 -RALALdpeillyDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3815-4019 |
1.52e-38 |
|
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: 144.92 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQQ- 3891
Cdd:cd03225 5 LSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLVFQNp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLDNLTVRE-------HLMLfasikapwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKT 3964
Cdd:cd03225 85 DDQFFGPTVEEevafgleNLGL---------PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3965 VVLDEPSSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3824-4028 |
1.74e-38 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 145.66 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3824 VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCP--QQDVLLDNLTVR 3901
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtfQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3902 EHLML--------FASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:cd03219 94 ENVMVaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3974 VDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPAD 4028
Cdd:cd03219 174 LNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3814-4021 |
5.38e-38 |
|
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: 143.66 E-value: 5.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYED---HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQ 3890
Cdd:cd03266 6 ALTKRFRDvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEP 3970
Cdd:cd03266 86 STGLYDRLTARENLEYFAGLYG--LKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3971 SSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3810-4029 |
1.23e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.90 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCP 3889
Cdd:PRK13536 42 IDLAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDVLLDNLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDE 3969
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFG--MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3970 PSSGVDPCSRRSLWDIL--LKYReGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13536 199 PTTGLDPHARHLIWERLrsLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4691-4918 |
4.97e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 4.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYtvIRtpqgdmVDLASAGK 4770
Cdd:COG1121 6 AIELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT--VR------LFGKPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGILIGYCPQQDALDEL--LTGWE----HLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTAL 4844
Cdd:COG1121 73 ARRRIGYVPQRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4845 ALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFrCLGPPQHI 4918
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3815-4020 |
7.59e-37 |
|
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: 140.35 E-value: 7.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGVCPQQDVL 3894
Cdd:cd03259 6 LSKTYGS-VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLmLFAsIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGV 3974
Cdd:cd03259 84 FPHLTVAENI-AFG-LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3975 DPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03259 162 DAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3815-4032 |
7.60e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 143.41 E-value: 7.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDVL 3894
Cdd:PRK13537 13 VEKRYGDKLV-VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGV 3974
Cdd:PRK13537 92 DPDFTVRENLLVFGRYFG--LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3975 DPCSRRSLWDIL--LKYReGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:PRK13537 170 DPQARHLMWERLrsLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3815-4019 |
2.08e-36 |
|
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: 136.99 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQqdv 3893
Cdd:cd00267 5 LSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 lldnltvrehlmlfasikapwwttkelqqqvnktldeveltqhqhkpagvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 116292744 3974 VDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:cd00267 111 LDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3825-4031 |
2.94e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 138.72 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLS---KVREELGVCPQQDVLLDNLTVR 3901
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPpheRARAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3902 EHLMLFASIKAPwwttkelqQQVNKTLDEV-----ELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDP 3976
Cdd:cd03224 94 ENLLLGAYARRR--------AKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3977 CSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:cd03224 166 KIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4694-4918 |
3.68e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 139.00 E-value: 3.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYRsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTV----IRTPQGDMVDLASag 4769
Cdd:COG1122 3 LENLSFSYP----GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG-EVlvdgKDITKKNLRELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGILIgycpqQDALDELL--TGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALV 4847
Cdd:COG1122 76 KVGLVF-----QNPDDQLFapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4848 GKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3815-4029 |
5.53e-36 |
|
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: 146.59 E-value: 5.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYE----DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT----DLSKVREELG 3886
Cdd:COG1123 266 LSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRELRRRVQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3887 VCPQQ-DVLLD-NLTVREHLMlFASIKAPWWTTKELQQQVNKTLDEVEL-TQHQHKPAGVLSGGMKRKLSIGIAFMGMSK 3963
Cdd:COG1123 346 MVFQDpYSSLNpRMTVGDIIA-EPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPK 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3964 TVVLDEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:COG1123 425 LLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3814-4029 |
6.13e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 138.59 E-value: 6.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKN-LQTDLSKVREELGVCPQQD 3892
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3893 VLLDNLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVEL--TQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEP 3970
Cdd:cd03295 85 GLFPHMTVEENIALVPKLLK--WPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3971 SSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4696-4907 |
1.11e-35 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 136.83 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGY-TVIRTPQGDMVDLASAGKAGIL 4774
Cdd:cd03225 4 NLSFSYP---DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 IgycpqQDALDELL--TGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDI 4852
Cdd:cd03225 81 F-----QNPDDQFFgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4853 LLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
3826-3972 |
3.22e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 133.16 E-value: 3.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3826 VQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQ-TDLSKVREELGVCPQQDVLLDNLTVREHL 3904
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3905 MLFASIKApwWTTKELQQQVNKTLDEVELT----QHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSS 3972
Cdd:pfam00005 81 RLGLLLKG--LSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3821-4015 |
5.64e-35 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 134.97 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNlqtdLSKVREELGVCPQQ-DVLLD-NL 3898
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP----LEKERKRIGYVPQRrSIDRDfPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3899 TVREHLM--LFASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDP 3976
Cdd:cd03235 86 SVRDVVLmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 116292744 3977 CSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVL 4015
Cdd:cd03235 166 KTQEDIYELLRELRrEGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3815-4019 |
7.07e-35 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 132.89 E-value: 7.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQD 3892
Cdd:cd03228 6 VSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3893 VLLdNLTVREhlmlfasikapwwttkelqqqvNktldeveltqhqhkpagVLSGGMKRKLSIGIAFMGMSKTVVLDEPSS 3972
Cdd:cd03228 86 FLF-SGTIRE----------------------N-----------------ILSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 116292744 3973 GVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGR 4019
Cdd:cd03228 126 ALDPETEALILEALRALAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3812-4019 |
3.09e-34 |
|
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: 131.54 E-value: 3.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3812 LISVTKEYeDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT---DLSKVREELGVC 3888
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PQQDVLLDNLTVREHLMLfasikapwwttkelqqqvnktldeveltqhqhkpagVLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:cd03229 82 FQDFALFPHLTVLENIAL------------------------------------GLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3969 EPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:cd03229 126 EPTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4692-4907 |
3.70e-34 |
|
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: 132.64 E-value: 3.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4692 MVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKA 4771
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-----DGRDVTGVPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GILIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPD 4851
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLwqtiTQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03259 151 LLLLDEPLSALDAKLREEL----REELKElqrelGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4694-4920 |
9.28e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 131.90 E-value: 9.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpQGDMVDLASAGKAGI 4773
Cdd:cd03218 3 AENLSKRY-----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD--GQDITKLPMHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 LIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDIL 4853
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4854 LLDEPSSGMDPCSKRYLwQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKN 4920
Cdd:cd03218 156 LLDEPFAGVDPIAVQDI-QKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3825-4031 |
4.07e-33 |
|
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: 130.49 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLS---KVREELGVCPQQDVLLDNLTVR 3901
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLPphrIARLGIGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3902 EHLMLFASIKAPwwttkelQQQVNKTLDEV-----ELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDP 3976
Cdd:COG0410 97 ENLLLGAYARRD-------RAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3977 CSRRSLWDIL--LKyREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:COG0410 170 LIVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3805-4034 |
5.13e-33 |
|
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: 138.35 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3805 GGNPGVALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVRE 3883
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3884 ELGVCPQQDVLLdNLTVREHLmLFASIKAPwwttkelQQQVNKTLDEVELTQH-QHKPAGV----------LSGGMKRKL 3952
Cdd:COG4988 412 QIAWVPQNPYLF-AGTIRENL-RLGRPDAS-------DEELEAALEAAGLDEFvAALPDGLdtplgeggrgLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3953 SIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEmLSDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLAK 561
|
..
gi 116292744 4033 YG 4034
Cdd:COG4988 562 NG 563
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3815-4020 |
1.79e-32 |
|
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: 127.99 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQEL---TLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQ----TDLSKVR-EELG 3886
Cdd:cd03255 6 LSKTYGGGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklseKELAAFRrRHIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3887 VCPQQDVLLDNLTVREHLML---FASIKApwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSK 3963
Cdd:cd03255 86 FVFQSFNLLPDLTALENVELpllLAGVPK-----KERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3964 TVVLDEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMlSDHVAVLQQGRL 4020
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4696-4918 |
2.59e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.42 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGKAGILI 4775
Cdd:COG1123 9 DLSVRYP---GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQqDALDEL--LTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDIL 4853
Cdd:COG1123 86 GMVFQ-DPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4854 LLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4690-4922 |
3.55e-32 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.89 E-value: 3.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4690 DMMVLCNLSKSYR-----------SVFGGKTT------AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGy 4752
Cdd:COG1134 3 SMIEVENVSKSYRlyhepsrslkeLLLRRRRTrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4753 TVIRTpqgdmvdlasaGKAGILIGYcpqQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATY 4832
Cdd:COG1134 82 RVEVN-----------GRVSALLEL---GAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4833 SGGTRRKLSTALALVGKPDILLLDEPSSGMDP-----CSKRylwqtITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkkCLAR-----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|....*
gi 116292744 4908 SFRCLGPPQHIKNRF 4922
Cdd:COG1134 223 RLVMDGDPEEVIAAY 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3806-4035 |
5.77e-32 |
|
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: 135.28 E-value: 5.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3806 GNPGVALISVTKEYEDHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVRE 3883
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3884 ELGVCPQQDVLLDNlTVREHLmLFASIKApwwTTKELQQqvnkTLDEVELTQH-QHKPAGV----------LSGGMKRKL 3952
Cdd:COG4987 410 RIAVVPQRPHLFDT-TLRENL-RLARPDA---TDEELWA----ALERVGLGDWlAALPDGLdtwlgeggrrLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3953 SIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLsDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQ 559
|
...
gi 116292744 4033 YGQ 4035
Cdd:COG4987 560 NGR 562
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3825-4021 |
6.29e-32 |
|
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: 126.36 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVreelGVCPQQDVLLDNLTVREH 3903
Cdd:TIGR03740 15 AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtRKDLHKI----GSLIESPPLYENLTAREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3904 LMLFASIKA-PwwttkelQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSL 3982
Cdd:TIGR03740 91 LKVHTTLLGlP-------DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQEL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 116292744 3983 WDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:TIGR03740 164 RELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3815-4031 |
7.93e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 126.91 E-value: 7.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT----DLSKVREELGVCPQ 3890
Cdd:cd03256 6 LSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIGMIFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREH-LMLFASIKAPWWT-----TKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKT 3964
Cdd:cd03256 86 QFNLIERLSVLENvLSGRLGRRSTWRSlfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3965 VVLDEPSSGVDPCSRRSLWDILLKY--REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:cd03256 166 ILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4711-5030 |
1.03e-31 |
|
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: 138.22 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLASAGKAgilIGYCPQQDALDELLTG 4790
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSG-TVLVGGKDIETNLDAVRQS---LGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4791 WEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYL 4870
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4871 WQTITQeVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNRFGDGYTVKVW-----LHKEGSQPSAVSDC 4945
Cdd:TIGR01257 1101 WDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVrkmknIQSQRGGCEGTCSC 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4946 LKLHF------------PGIQFKG---QRLNLLEYHV--QKSWECL------------------ADLFKVLENNKSLLNI 4990
Cdd:TIGR01257 1180 TSKGFstrcparvdeitPEQVLDGdvnELMDLVYHHVpeAKLVECIgqelifllpnknfkqrayASLFRELEETLADLGL 1259
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 116292744 4991 EHYSISQTTLEQVFVNFATEQLQTPCFPVDS----PSTDAQHPC 5030
Cdd:TIGR01257 1260 SSFGISDTPLEEIFLKVTEDADSGSLFAGGAqqkrENANLRHPC 1303
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4691-4918 |
1.93e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 125.93 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGK 4770
Cdd:COG1120 1 MLEAENLSVGY-----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL-----DGRDLASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGI--LIGYCPQQDALDELLTGWE--------HLQYYCRLRgiPKQYipEVAADLVRRLHLESHVDKPVATYSGGTRRKL 4840
Cdd:COG1120 71 RELarRIAYVPQEPPAPFGLTVRElvalgrypHLGLFGRPS--AEDR--EAVEEALERTGLEHLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4841 STALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4694-4907 |
2.24e-31 |
|
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: 122.35 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLASAGKAGI 4773
Cdd:cd00267 2 IENLSFRY-----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG-EILIDGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 liGYCPQqdaldelltgwehlqyycrlrgipkqyipevaadlvrrlhleshvdkpvatYSGGTRRKLSTALALVGKPDIL 4853
Cdd:cd00267 76 --GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4854 LLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
4712-4860 |
2.68e-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: 121.99 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGKAgilIGYCPQQDALDELLTGW 4791
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE---IGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4792 EHLQYYCRLRGIPKQYIPEVAADLVRRLHLE----SHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSS 4860
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4696-4920 |
4.92e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 125.15 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSyrsvFGGkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVI---RtpqgDMVDLASAG--K 4770
Cdd:COG0411 9 GLTKR----FGG-LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSG-RILfdgR----DITGLPPHRiaR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGI-----LIGYCPQQDALDELLTGWEH------LQYYCRLRGIPKQY--IPEVAADLVRRLHLESHVDKPVATYSGGTR 4837
Cdd:COG0411 79 LGIartfqNPRLFPELTVLENVLVAAHArlgrglLAALLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4838 RKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTItQEVRD--GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPP 4915
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELI-RRLRDerGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*
gi 116292744 4916 QHIKN 4920
Cdd:COG0411 238 AEVRA 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3815-4033 |
8.86e-31 |
|
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: 123.42 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGknlqTDLSKV----REELGVC-- 3888
Cdd:cd03218 6 LSKRYGKRKV-VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG----QDITKLpmhkRARLGIGyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PQQDVLLDNLTVREHLMLFASIKAPwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGL--SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3969 EPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL------KETY 4033
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIaanelvRKVY 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4696-4920 |
1.31e-30 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 122.93 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSyrsvFGGkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVI--------RTPQgdmvDLAS 4767
Cdd:cd03219 5 GLTKR----FGG-LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSG-SVLfdgeditgLPPH----EIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4768 AG------KAGILigycPQQDALDELLTGWE-HLQYYCRLRGIPKQY--IPEVAADLVRRLHLESHVDKPVATYSGGTRR 4838
Cdd:cd03219 75 LGigrtfqIPRLF----PELTVLENVMVAAQaRTGSGLLLARARREEreARERAEELLERVGLADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4839 KLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
..
gi 116292744 4919 KN 4920
Cdd:cd03219 231 RN 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4696-4913 |
2.70e-30 |
|
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: 121.87 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRS-----------------VFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTp 4758
Cdd:cd03220 5 NVSKSYPTykggssslkklgilgrkGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG-TVTVR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4759 qGDMVDLASAGkAGiligycpqqdaLDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRR 4838
Cdd:cd03220 83 -GRVSSLLGLG-GG-----------FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4839 KLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLG 4913
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3821-4020 |
9.84e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 118.69 E-value: 9.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQqdvlldnlt 3899
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3900 vrehlmlfasikapwwttkelqqqvnkTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSR 3979
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 116292744 3980 RSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03214 134 IELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4696-4904 |
1.33e-29 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 119.50 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSG-----YTVIRTPQGDmvdlasagk 4770
Cdd:cd03293 5 NVSKTYGGG-GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGevlvdGEPVTGPGPD--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 agilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:cd03293 75 ----RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLWQTITQEVR-DGCAAVLTSHSMEECEALCTRLAIM 4904
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4696-4927 |
2.08e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.56 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRtpqgDMVDLASAGKAGIL- 4774
Cdd:COG1123 265 NLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSG-SILF----DGKDLTKLSRRSLRe 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 ----IGYCPQ--QDALDELLTGWEHLQYYCRLRGI-PKQYIPEVAADLVRRLHL-ESHVDKPVATYSGGTRRKLSTALAL 4846
Cdd:COG1123 340 lrrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4847 VGKPDILLLDEPSSGMDPCSKRylwqTITQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNR 4921
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQA----QILNLLRDlqrelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
....*.
gi 116292744 4922 FGDGYT 4927
Cdd:COG1123 496 PQHPYT 501
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3810-4020 |
4.45e-29 |
|
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: 118.45 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHK---VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT----DLSKVR 3882
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3883 EELGVCPQQDVLLDNLTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMS 3962
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVAL--PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3963 KTVVLDEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3810-4020 |
4.63e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.23 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT----DLSKVREEL 3885
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3886 GVCPQQDVLLDNLTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVAL--PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4691-4918 |
4.90e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.59 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVL--CNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPQGDMVDL--- 4765
Cdd:COG1137 1 MMTLeaENLVKSY-----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG--RIFLDGEDITHLpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4766 --ASAGkagilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTA 4843
Cdd:COG1137 74 krARLG-----IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4844 LALVGKPDILLLDEPSSGMDPCSKRYLwQTITQEVRDGCAAVL-TSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADI-QKIIRHLKERGIGVLiTDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4691-4922 |
5.01e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.13 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqG-DMVDLAsAG 4769
Cdd:COG3842 5 ALELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD---GrDVTGLP-PE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTR-RklsTALA--L 4846
Cdd:COG3842 76 KRN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VALAraL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4847 VGKPDILLLDEPSSGMDPCSKRYLWqtitQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI--- 4918
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMR----EELRRlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIyer 226
|
....*
gi 116292744 4919 -KNRF 4922
Cdd:COG3842 227 pATRF 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4696-4907 |
5.97e-29 |
|
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: 117.59 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQG-DMVDLASAGKAGIL 4774
Cdd:cd03255 5 NLSKTYGGG-GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV---DGtDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 ---IGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPD 4851
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEEcEALCTRLAIMVDG 4907
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDG 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3815-4029 |
1.05e-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: 124.25 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKV-AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPT---SGTITINGKNLQTDLSKVR-EELGVCP 3889
Cdd:COG1123 10 LSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgRRIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQ-DVLLDNLTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:COG1123 90 QDpMTQLNPVTVGDQIAE--ALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3969 EPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:COG1123 168 EPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3817-4020 |
1.57e-28 |
|
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: 116.60 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3817 KEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPP---TSGTITINGKNLQTDLskVREELGVCPQQDV 3893
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQ--FQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 LLDNLTVREHLMLFASIKAPWWTTKELQQQVNKT--LDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3972 SGVDPCSRRSLWDILLKY-REGRTIIFTTHHlDEAEM--LSDHVAVLQQGRL 4020
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3810-4031 |
3.22e-28 |
|
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: 116.18 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYeDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGVCP 3889
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDVLLDNLTVREHLMLFASIKAPwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDE 3969
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKL--PKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3970 PSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:cd03300 157 PLGALDLKLRKDMQLELkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4691-4908 |
4.48e-28 |
|
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: 115.61 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYR-SVFGGKT-TAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTpQGDMVDLASA 4768
Cdd:COG4778 4 LLEVENLSKTFTlHLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRH-DGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4769 GKAGIL------IGYC-------PQQDALD---ELLtgwehlqyycRLRGIPKQYIPEVAADLVRRLHLESHV-DKPVAT 4831
Cdd:COG4778 83 SPREILalrrrtIGYVsqflrviPRVSALDvvaEPL----------LERGVDREEARARARELLARLNLPERLwDLPPAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4832 YSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGS 4908
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3805-4020 |
4.53e-28 |
|
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: 116.97 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3805 GGNPGVALISVTKEY---EDHK-----VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT 3876
Cdd:cd03294 11 GKNPQKAFKLLAKGKskeEILKktgqtVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3877 ----DLSKVR-EELGVCPQQDVLLDNLTVREHLMLFASIKAPwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRK 3951
Cdd:cd03294 91 msrkELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGV--PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3952 LSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKY--REGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03294 169 VGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3815-4020 |
6.46e-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: 6.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHK---VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL----QTDLSKVREELGV 3887
Cdd:cd03257 7 LSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3888 CPqQDVL--LD-NLTVREHLMLFASIKAPWWTTKELQQQVNKTLDEVELTQ-------HQhkpagvLSGGMKRKLSIGIA 3957
Cdd:cd03257 87 VF-QDPMssLNpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevlnrypHE------LSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3958 FMGMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3817-4029 |
6.71e-28 |
|
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: 115.45 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3817 KEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDL---SKVREELGVCPQQDV 3893
Cdd:TIGR04406 9 KSYKKRKV-VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLpmhERARLGIGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 LLDNLTVREHLMLFASIKaPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:TIGR04406 87 IFRKLTVEENIMAVLEIR-KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3974 VDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4696-4904 |
1.00e-27 |
|
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: 114.17 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRtpqgdmVDLASAGKAGILI 4775
Cdd:cd03235 4 DLTVSY-----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSG--SIR------VFGKPLEKERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQ---------DALDELLTGWehLQYYCRLRGIPKQYIPEV--AADLVRRLHLEshvDKPVATYSGGTRRKLSTAL 4844
Cdd:cd03235 71 GYVPQRrsidrdfpiSVRDVVLMGL--YGHKGLFRRLSKADKAKVdeALERVGLSELA---DRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4845 ALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIM 4904
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3808-4029 |
1.01e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3808 PGVALISVTKEYEDHkVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGV 3887
Cdd:COG3842 4 PALELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3888 CPQQDVLLDNLTVREHLMlFaSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGG------------MKRKLsig 3955
Cdd:COG3842 82 VFQDYALFPHLTVAENVA-F-GLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvalaralaPEPRV--- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3956 iafmgmsktVVLDEPSSGVDPCSRRSLWDILLKY--REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:COG3842 157 ---------LLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4696-4906 |
1.22e-27 |
|
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: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYR-------------SVFGGKT---TAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVI--RT 4757
Cdd:cd03267 5 NLSKSYRvyskepgligslkSLFKRKYrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVagLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4758 PQGDMVDLASagKAGILIGycpQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTR 4837
Cdd:cd03267 85 PWKRRKKFLR--RIGVVFG---QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4838 RKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLaIMVD 4906
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRV-LVID 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
3817-4021 |
1.48e-27 |
|
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: 113.54 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3817 KEYEDHKVAVQeLTLTFhrdQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGK-----NLQTDLSKVREELGVCPQQ 3891
Cdd:cd03297 8 KRLPDFTLKID-FDLNE---EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLDNLTVREHLMLFASIKAPwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRN----REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3972 SGVDpcsrRSLWDILLKYREGR------TIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:cd03297 160 SALD----RALRLQLLPELKQIkknlniPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4691-4930 |
2.73e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 115.95 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYR-----SVFGG-----------KTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTV 4754
Cdd:COG4586 1 IIEVENLSKTYRvyekePGLKGalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4755 I--RTPQGDMVDLASagKAGILIGycpQQDAL--DelLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVA 4830
Cdd:COG4586 81 VlgYVPFKRRKEFAR--RIGVVFG---QRSQLwwD--LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4831 TYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLaIMVD-GS 4908
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRV-IVIDhGR 232
|
250 260
....*....|....*....|..
gi 116292744 4909 FRCLGPPQHIKNRFGDGYTVKV 4930
Cdd:COG4586 233 IIYDGSLEELKERFGPYKTIVL 254
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4713-4907 |
3.49e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.22 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4713 HGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVI-----RTpQGDMVDLASagkagiLIGYCPQQDALdel 4787
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG-EIYldgkpLS-AMPPPEWRR------QVAYVPQEPAL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4788 ltgW-----EHLQYYCRLRGipKQYIPEVAADLVRRLHLESHV-DKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSG 4861
Cdd:COG4619 86 ---WggtvrDNLPFPFQLRE--RKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 116292744 4862 MDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG4619 161 LDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4687-4904 |
5.90e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 113.26 E-value: 5.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4687 TGGDMMVLCNLSKSYRSVfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVirtpqgdMVDLA 4766
Cdd:COG1116 3 AAAPALELRGVSKRFPTG-GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSG-EV-------LVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4767 SAGKAGILIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALAL 4846
Cdd:COG1116 74 PVTGPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4847 VGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIM 4904
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3810-4020 |
7.72e-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: 109.83 E-value: 7.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVcp 3889
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 qqdvlldnLTVrehlmlfasikapwwttkelqqqvnktldeveltqHQhkpagvLSGGMKRKLSIGIAFMGMSKTVVLDE 3969
Cdd:cd03216 78 --------AMV-----------------------------------YQ------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3970 PSSGVDPCSRRSLWDIL--LKyREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03216 109 PTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4691-4907 |
7.91e-27 |
|
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: 111.90 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSVfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGK 4770
Cdd:cd03258 1 MIELKNVSKVFGDT-GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-----DGTDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGIL-----IGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALA 4845
Cdd:cd03258 75 KELRkarrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4846 LVGKPDILLLDEPSSGMDPCSKRY---LWQTITQEVrdGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSilaLLRDINREL--GLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3810-4040 |
8.12e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 112.49 E-value: 8.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSG-TITINGKNL-QTDLSKVREELG- 3886
Cdd:COG1119 4 LELRNVTVRRGGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3887 VCPQ-QDVLLDNLTVREHLM--LFASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSK 3963
Cdd:COG1119 83 VSPAlQLRFPRDETVLDVVLsgFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3964 TVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDE--AEMlsDHVAVLQQGRLRCYAPPAD------LKETY 4033
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEEipPGI--THVLLLKDGRVVAAGPKEEvltsenLSEAF 240
|
....*..
gi 116292744 4034 GQGLTLT 4040
Cdd:COG1119 241 GLPVEVE 247
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4691-4920 |
1.36e-26 |
|
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: 111.61 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSyrsvFGGKTtaVH-GISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAG 4769
Cdd:COG1127 5 MIEVRNLTKS----FGDRV--VLdGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-----DGQDITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGIL-----IGYCPQQDALDELLTGWEHLQYYCR-LRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTA 4843
Cdd:COG1127 74 EKELYelrrrIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4844 LALVGKPDILLLDEPSSGMDPCSKRYLWQTItQEVRD--GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKN 4920
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELI-RELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4696-4935 |
1.74e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.52 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSvfggkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGKAGIli 4775
Cdd:PRK10895 8 NLAKAYKG-----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYYCRLR-GIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILL 4854
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4855 LDEPSSGMDPCSKRYLwQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIknrFGDGYTVKVWLH 4933
Cdd:PRK10895 161 LDEPFAGVDPISVIDI-KRIIEHLRDsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI---LQDEHVKRVYLG 236
|
..
gi 116292744 4934 KE 4935
Cdd:PRK10895 237 ED 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4696-4907 |
3.08e-26 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 110.29 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRsVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRtpqgDMVDLASAGKAGIL- 4774
Cdd:cd03257 6 NLSVSFP-TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSG-SIIF----DGKDLLKLSRRLRKi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 ----IGYCPQ--QDALDELLTGWEHLQ--YYCRLRGIPKQYIPEVAADLVRRLHL-ESHVDKPVATYSGGTRRKLSTALA 4845
Cdd:cd03257 80 rrkeIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4846 LVGKPDILLLDEPSSGMDPCSKRYLWQTItQEVRD--GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLL-KKLQEelGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3808-4020 |
3.92e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 116.28 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3808 PGVALISVTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlQTDLSKVRE--EL 3885
Cdd:COG3845 4 PALELRGITKRFGG-VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK--PVRIRSPRDaiAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3886 GV--CPQQDVLLDNLTVREHLML-FASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMS 3962
Cdd:COG3845 81 GIgmVHQHFMLVPNLTVAENIVLgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3963 KTVVLDEPSSGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3814-4026 |
4.27e-26 |
|
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: 109.96 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFP-----PTSGTITINGKN---LQTDLSKVREEL 3885
Cdd:cd03260 5 DLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiydLDVDVLELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3886 GVCPQQDVLLDnLTVREHLMLfasikAPW----WTTKELQQQVNKTLDEVELTQ--HQHKPAGVLSGGMKRKLSIGIAFM 3959
Cdd:cd03260 84 GMVFQKPNPFP-GSIYDNVAY-----GLRlhgiKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3960 GMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPP 4026
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4696-4920 |
6.08e-26 |
|
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: 109.06 E-value: 6.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRtpQG-DMVDLASAGKAGIL 4774
Cdd:cd03224 5 NLNAGY-----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSG-SIRF--DGrDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 IGYCPQQDALDELLTGWEHLQ--YYCRLRGIPKQYIPEVAA---DLVRRLHleshvdKPVATYSGGTRRKLSTALALVGK 4849
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLlgAYARRRAKRKARLERVYElfpRLKERRK------QLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4850 PDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKN 4920
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4691-4927 |
7.13e-26 |
|
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: 109.89 E-value: 7.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSVFGGKTtAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIR-TPQGDMVDLASAG 4769
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVP-VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGILigycpQQD---ALDELLTGWEHLQYYCRLRGIPkqYIPEVAADLVRRLHL-ESHVDKPVATYSGGTRRKLSTALA 4845
Cdd:COG1124 80 RVQMV-----FQDpyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4846 LVGKPDILLLDEPSSGMDPCSK----RYLwQTITQEvrDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNR 4921
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQaeilNLL-KDLREE--RGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
....*.
gi 116292744 4922 FGDGYT 4927
Cdd:COG1124 230 PKHPYT 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4703-4908 |
1.17e-25 |
|
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: 109.40 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4703 SVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVI----RTPQGDMVDLASagkagiLIGYC 4778
Cdd:COG1119 10 TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgeRRGGEDVWELRK------RIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4779 ---------PQQDALDELLTGwehlqYYCRLrGIPKQYIPE---VAADLVRRLHLESHVDKPVATYSGGTRRKLSTALAL 4846
Cdd:COG1119 84 spalqlrfpRDETVLDVVLSG-----FFDSI-GLYREPTDEqreRARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4847 VGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDG-CAAVLTSHSMEECEALCTRLAIMVDGS 4908
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
4707-4893 |
1.20e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.32 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPqgdmvdlasagkaGILIGYCPQQDALDE 4786
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-TVRRAG-------------GARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4787 LL---------TG-WEHLQYYCRLRGIPKQyipeVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLD 4856
Cdd:NF040873 69 SLpltvrdlvaMGrWARRGLWRRLTRDDRA----AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 116292744 4857 EPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEE 4893
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3815-4029 |
1.56e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 108.58 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLS---KVREELGVCPQQ 3891
Cdd:COG1137 9 LVKSYGKRTV-VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPmhkRARLGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLDNLTVREHLMLFASIKAPwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:COG1137 87 ASIFRKLTVEDNILAVLELRKL--SKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3972 SGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:COG1137 165 AGVDPIAVADIQKIIRHLKErGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3806-4023 |
1.58e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3806 GNPGVALISVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITInGKNLQtdlskvreeL 3885
Cdd:COG0488 312 GKKVLELEGLSKSYGDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3886 GVCPQ-QDVLLDNLTVREHLmlfasikapwwttkelqQQVNKTLDEVELTQ----------HQHKPAGVLSGGMKRKLSI 3954
Cdd:COG0488 381 GYFDQhQEELDPDKTVLDEL-----------------RDGAPGGTEQEVRGylgrflfsgdDAFKPVGVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3955 GIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYrEGrTIIFTTH--HLDEAemLSDHVAVLQQGRLRCY 4023
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdrYFLDR--VATRILEFEDGGVREY 510
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4696-4913 |
1.62e-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: 106.37 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGILI 4775
Cdd:cd03214 4 NLSVGY-----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---DGKDLASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQqdALDelLTGWEHLqyycrlrgipkqyipevaadlvrrlhleshVDKPVATYSGGTRRKLSTALALVGKPDILLL 4855
Cdd:cd03214 76 AYVPQ--ALE--LLGLAHL------------------------------ADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4856 DEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLG 4913
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4696-4858 |
1.69e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPqgdmvdlasagkaGILI 4775
Cdd:COG0488 3 NLSKSF-----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-EVSIPK-------------GLRI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEH-LQYYCRLRGIPKQY------IPEVAADLVR--RLH----------LESHV----------- 4825
Cdd:COG0488 64 GYLPQEPPLDDDLTVLDTvLDGDAELRALEAELeeleakLAEPDEDLERlaELQeefealggweAEARAeeilsglgfpe 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 116292744 4826 ---DKPVATYSGGTRRKLSTALALVGKPDILLLDEP 4858
Cdd:COG0488 144 edlDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3819-4034 |
2.95e-25 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 115.32 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQDVLLd 3896
Cdd:COG2274 483 YPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLF- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 NLTVREHLMLFASiKAPwwttkelQQQVNKTLDEVELTQ--HQHkPAG----------VLSGGMKRKLSIGIAFMGMSKT 3964
Cdd:COG2274 562 SGTIRENITLGDP-DAT-------DEEIIEAARLAGLHDfiEAL-PMGydtvvgeggsNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3965 VVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEmLSDHVAVLQQGRLRCYAPPADLKETYG 4034
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3825-4020 |
4.11e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 107.51 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGknlqTDLSKVRE----ELGVCP--QQDVLLDNL 3898
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGG----TDLTGLDEheiaRLGIGRkfQKPTVFEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3899 TVREHLMLFASIKAPWWT------TKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSS 3972
Cdd:COG4674 101 TVFENLELALKGDRGVFAslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3973 GVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:COG4674 181 GMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3815-4020 |
5.05e-25 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 106.07 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL---QTDLSKVREELGVCPQQ 3891
Cdd:cd03262 6 LHKSFGDFHV-LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGMVFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLDNLTVREHLMLfASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:cd03262 85 FNLFPHLTVLENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 116292744 3972 SGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03262 164 SALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3802-4020 |
7.62e-25 |
|
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: 106.65 E-value: 7.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3802 EMEGGNPGVALISVTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKV 3881
Cdd:cd03267 14 SKEPGLIGSLKSLFKRKYRE-VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3882 REELG-VCPQQDVLLDNLTVREHLMLFASI----KApwwttkELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGI 3956
Cdd:cd03267 93 LRRIGvVFGQKTQLWWDLPVIDSFYLLAAIydlpPA------RFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3957 AFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGR--TIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4663-4910 |
8.30e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.47 E-value: 8.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4663 LQDIVKPAKDIDVEteqMRVLEG-RTGGDMMVLCNLSKSYrsvfGGKTtAVHGISLGIPRGECFGLLGVNGAGKSTTFKI 4741
Cdd:COG0488 289 LEREEPPRRDKTVE---IRFPPPeRLGKKVLELEGLSKSY----GDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4742 LNGETPPSSGyTVIRtpqgdmvdlasaGKaGILIGYCPQ-QDALDELLTGWEHLQyycrlRGIPKQYIPEVaadlvrRLH 4820
Cdd:COG0488 361 LAGELEPDSG-TVKL------------GE-TVKIGYFDQhQEELDPDKTVLDELR-----DGAPGGTEQEV------RGY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4821 LES------HVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYL------WqtitqevrDGCaAVLTS 4888
Cdd:COG0488 416 LGRflfsgdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALeealddF--------PGT-VLLVS 486
|
250 260
....*....|....*....|..
gi 116292744 4889 HSMEECEALCTRLAIMVDGSFR 4910
Cdd:COG0488 487 HDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4696-4920 |
8.55e-25 |
|
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: 106.43 E-value: 8.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSyrsvFGGKTtaVH-GISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGIL 4774
Cdd:cd03261 5 GLTKS----FGGRT--VLkGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-----DGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 -----IGYCPQQDALDELLTGWEHLQYYCRLRGI-PKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVG 4848
Cdd:cd03261 74 rlrrrMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4849 KPDILLLDEPSSGMDPCSKRYLWQTItQEVRD--GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKN 4920
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLI-RSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4676-4918 |
9.82e-25 |
|
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: 112.20 E-value: 9.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4676 ETEQMRVLEgrTGGDMMVLCNLSKSYRSVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVI 4755
Cdd:TIGR03269 266 EVEKECEVE--VGEPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4756 RTPQG--DMVDLASAGKA------GIL---IGYCPQQDALDELL--TGWEHLQYYCRLRGIpkqYIPEVAAdlVRRLHLE 4822
Cdd:TIGR03269 344 RVGDEwvDMTKPGPDGRGrakryiGILhqeYDLYPHRTVLDNLTeaIGLELPDELARMKAV---ITLKMVG--FDEEKAE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4823 SHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRL 4901
Cdd:TIGR03269 419 EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRA 498
|
250
....*....|....*..
gi 116292744 4902 AIMVDGSFRCLGPPQHI 4918
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEI 515
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3824-4029 |
1.07e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3824 VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGV-CPQQDV-LLDNLTVR 3901
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIaIIHQELnLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3902 EHLMLFASIKAPWWT-TKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRR 3980
Cdd:COG1129 98 ENIFLGREPRRGGLIdWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3981 SLWDIL--LKyREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:COG1129 178 RLFRIIrrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4692-4913 |
1.31e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 105.03 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4692 MVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPQGDMVDLASAGKA 4771
Cdd:cd03301 1 VELENVTKRF-----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG--RIYIGGRDVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 gilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPD 4851
Cdd:cd03301 74 ---IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLG 4913
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
3826-4018 |
1.34e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 105.63 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3826 VQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQtdlskvreELG----VCPQQDVLLDNLTVR 3901
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT--------EPGpdrmVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3902 EHLMLFASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRS 3981
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 116292744 3982 LWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:TIGR01184 153 LQEELMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3810-4020 |
2.13e-24 |
|
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: 104.41 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL----QTDLSKVREEL 3885
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3886 GVCPQQDVLLDNLTVREHLMLFASI--KAPwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSK 3963
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVtgVPP----REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3964 TVVLDEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3826-4020 |
2.51e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.40 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3826 VQELTLTFHRDQITALLGTNGAGKTTIISMLMGL--FPPTSGTITINGKNLqtDLSKVREELGVCPQQDVLLDNLTVREH 3903
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3904 LMLFASIKapwwttkelqqqvnktldeveltqhqhkpagVLSGGMKRKLSIGIAfMGMSKTVV-LDEPSSGVDPCSRRSL 3982
Cdd:cd03213 103 LMFAAKLR-------------------------------GLSGGERKRVSIALE-LVSNPSLLfLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 116292744 3983 WDILLKYR-EGRTIIFTTHHL-DEAEMLSDHVAVLQQGRL 4020
Cdd:cd03213 151 MSLLRRLAdTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4696-4922 |
2.58e-24 |
|
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: 104.63 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPqgDMVDLAsAGKAGIli 4775
Cdd:cd03300 5 NVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK--DITNLP-PHKRPV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLL 4855
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4856 DEPSSGMDpcskRYLWQTITQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI----KNRF 4922
Cdd:cd03300 155 DEPLGALD----LKLRKDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRF 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3814-4029 |
3.93e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.59 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINgknlQTDLS------KVREELGV 3887
Cdd:PRK10895 8 NLAKAYKGRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID----DEDISllplhaRARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3888 CPQQDVLLDNLTVREHLMLFASIKAPwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVL 3967
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDD-LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3968 DEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4710-4923 |
4.96e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.14 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4710 TAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqGDMVDlasagkAGIL-----IGYCPQQDAL 4784
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLF---GQPVD------AGDIatrrrVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4785 DELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDP 4864
Cdd:NF033858 351 YGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4865 CSKRYLWQTITQEVR-DGCAAVLTSHSMEECEaLCTRLAIMVDGsfRCL--GPPQHIKNRFG 4923
Cdd:NF033858 431 VARDMFWRLLIELSReDGVTIFISTHFMNEAE-RCDRISLMHAG--RVLasDTPAALVAARG 489
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4696-4918 |
6.53e-24 |
|
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: 103.92 E-value: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIR---TPQGDMVDLASAgkag 4772
Cdd:cd03295 5 NVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgedIREQDPVELRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4773 ilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLE--SHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:cd03295 77 --IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLWQ---TITQEVrdGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEefkRLQQEL--GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3840-4020 |
8.75e-24 |
|
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: 103.18 E-value: 8.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3840 ALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGVCPQQDVLLDNLTVREHLMLfaSIKAPWWTTKE 3919
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAY--GLKKRKVDKKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3920 LQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYRE--GRTIIF 3997
Cdd:cd03299 106 IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLH 185
|
170 180
....*....|....*....|...
gi 116292744 3998 TTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03299 186 VTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3810-4021 |
1.54e-23 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 101.95 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGVCP 3889
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDVLLDNLTVREHlMLFA--SIKAPwwtTKELQQQVNKTLDEVELTQH-QHKPAGvLSGGMKRKLSIGIAFMGMSKTVV 3966
Cdd:cd03301 79 QNYALYPHMTVYDN-IAFGlkLRKVP---KDEIDERVREVAELLQIEHLlDRKPKQ-LSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3967 LDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3819-4020 |
1.81e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKV-REELGVCPQQDVLLDN 3897
Cdd:PRK11231 12 YGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3898 LTVREhlmLFASIKAPW---W--TTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKlsigiAFMGM-----SKTVVL 3967
Cdd:PRK11231 91 ITVRE---LVAYGRSPWlslWgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQR-----AFLAMvlaqdTPVVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3968 DEPSSGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3799-4020 |
1.83e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 108.71 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3799 GPGEMEGGNPGVALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-D 3877
Cdd:COG1132 329 GAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlT 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3878 LSKVREELGVCPqQDVLLDNLTVREHLmLFASIKApwwttkelqqqvnkTLDEVE----LTQ-H---QHKPAGV------ 3943
Cdd:COG1132 409 LESLRRQIGVVP-QDTFLFSGTIRENI-RYGRPDA--------------TDEEVEeaakAAQaHefiEALPDGYdtvvge 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3944 ----LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGR 4019
Cdd:COG1132 473 rgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGR 551
|
.
gi 116292744 4020 L 4020
Cdd:COG1132 552 I 552
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4696-4907 |
1.88e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 100.34 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGIL- 4774
Cdd:cd03229 5 NVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-----DGEDLTDLEDELPPl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 ---IGYCPQQDALDELLTGWEHLQYycrlrgipkqyipevaadlvrRLhleshvdkpvatySGGTRRKLSTALALVGKPD 4851
Cdd:cd03229 75 rrrIGMVFQDFALFPHLTVLENIAL---------------------GL-------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLwQTITQEVRD--GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03229 121 VLLLDEPTSALDPITRREV-RALLKSLQAqlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3808-4015 |
2.03e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 108.14 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3808 PGVALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELG 3886
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3887 VCPQQDVLLDNlTVREHLMLfasiKAPWWTTKELQQQVNKT-LDEV--ELTQHQHKPAG----VLSGGMKRKLSIGIAFM 3959
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRL----ARPDASDAEIREALERAgLDEFvaALPQGLDTPIGeggaGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3960 GMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEmLSDHVAVL 4015
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3815-4020 |
2.20e-23 |
|
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: 101.92 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPqQDV 3893
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrDISRKSLRSMIGVVL-QDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 LLDNLTVREHLMLFASIkapwwTTKELQQQVNKTL---DEVE-LT---QHQHKPAG-VLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:cd03254 87 FLFSGTIMENIRLGRPN-----ATDEEVIEAAKEAgahDFIMkLPngyDTVLGENGgNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGRL 4020
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4691-4907 |
2.32e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.66 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSvFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSG-YTVirtpqgDMVDLASAG 4769
Cdd:COG1136 4 LLELRNLTKSYGT-GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGeVLI------DGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGI------LIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTA 4843
Cdd:COG1136 77 ERELarlrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4844 LALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSmEECEALCTRLAIMVDG 4907
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDG 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4694-4907 |
2.68e-23 |
|
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: 102.26 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGI 4773
Cdd:cd03256 3 VENLSKTY----PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI-----DGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 L-----IGY-------CPQQDALDELLTGweHLQYYCRLRGIPKQYIPE---VAADLVRRLHLESHVDKPVATYSGGTRR 4838
Cdd:cd03256 74 RqlrrqIGMifqqfnlIERLSVLENVLSG--RLGRRSTWRSLFGLFPKEekqRALAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4839 KLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4696-4918 |
3.02e-23 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 101.49 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNG-----ETPPSSGyTV------IRTPQGDMVD 4764
Cdd:cd03260 5 DLNVYY-----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEG-EVlldgkdIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4765 LASAgkagilIGYCPQQDALDELlTGWEHLQYYCRLRGI-PKQYIPEVAADLVRRLHLESHV-DKPVATY-SGGTRRKLS 4841
Cdd:cd03260 79 LRRR------VGMVFQKPNPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVkDRLHALGlSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4842 TALALVGKPDILLLDEPSSGMDPCSKRYLWQTITqEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIA-ELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3815-4122 |
3.41e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.01 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVcpqqdV- 3893
Cdd:COG4586 28 FRREYRE-VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGV-----Vf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 -----LLDNLTVREHLMLFASI-KAPwwttkelQQQVNKTLDEV----ELTQHQHKPAgvlsggmkRKLSIG------IA 3957
Cdd:COG4586 102 gqrsqLWWDLPAIDSFRLLKAIyRIP-------DAEYKKRLDELvellDLGELLDTPV--------RQLSLGqrmrceLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3958 fmgMS-----KTVVLDEPSSGVDPCSRRSLWDILLKY--REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLK 4030
Cdd:COG4586 167 ---AAllhrpKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4031 ETYGQGLTLTlskqpsiLETQEPKDVARVTSLIQIyipqaflKDSCGGELTYTIPKDADrtcfkgLCQALDQNLQHLHLT 4110
Cdd:COG4586 244 ERFGPYKTIV-------LELAEPVPPLELPRGGEV-------IEREGNRVRLEVDPRES------LAEVLARLLARYPVR 303
|
330
....*....|..
gi 116292744 4111 GYGISDTTLEEV 4122
Cdd:COG4586 304 DLTIEEPPIEEV 315
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3819-4055 |
3.47e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL---QTDLSKVREELGVCPQQ-DVL 3894
Cdd:PRK13636 15 YSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFA-SIKAPwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:PRK13636 95 LFSASVYQDVSFGAvNLKLP---EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3974 VDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL--KETYGQGLTLTLSKQPSILE 4049
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVfaEKEMLRKVNLRLPRIGHLME 251
|
....*.
gi 116292744 4050 TQEPKD 4055
Cdd:PRK13636 252 ILKEKD 257
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4696-4907 |
3.50e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.04 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAgkagili 4775
Cdd:cd03216 5 GITKRF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV---DGKEVSFASP------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 gycpqQDALDelltgwehlqyycrlRGIpkqyipevaaDLVRRLhleshvdkpvatySGGTRRKLSTALALVGKPDILLL 4855
Cdd:cd03216 70 -----RDARR---------------AGI----------AMVYQL-------------SVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4856 DEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3825-4020 |
4.04e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.49 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKV-REELGVCPQQDVLLDNLTVRE 3902
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTAKImREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3903 HLML---FASikapwwtTKELQQQVNKTLDEV-ELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCS 3978
Cdd:PRK11614 100 NLAMggfFAE-------RDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 116292744 3979 RRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11614 173 IQQIFDTIEQLReQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3810-4020 |
7.85e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 103.23 E-value: 7.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHK---VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT----DLSKVR 3882
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3883 EELGVCPQQDVLLDNLTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHK-PAGvLSGGMKRKlsIGIA-FMG 3960
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVAL--PLEIAGVPKAEIRKRVAELLELVGLSDKADAyPSQ-LSGGQKQR--VGIArALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3961 MSKTVVL-DEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHhldeaEM-----LSDHVAVLQQGRL 4020
Cdd:COG1135 157 NNPKVLLcDEATSALDPETTRSILDLLKDINRelGLTIVLITH-----EMdvvrrICDRVAVLENGRI 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4696-4921 |
8.67e-23 |
|
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: 100.49 E-value: 8.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVFggkttaVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYtvIRTPQGDMVDLaSAGKAGIli 4775
Cdd:cd03299 5 NLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGK--ILLNGKDITNL-PPEKRDI-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLL 4855
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4856 DEPSSGMDPCSK---RYLWQTITQEVrdGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNR 4921
Cdd:cd03299 154 DEPFSALDVRTKeklREELKKIRKEF--GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3815-4018 |
9.21e-23 |
|
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: 99.25 E-value: 9.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQtdlSKVREELGVCPQQDVl 3894
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNL---TVREHLMLfaSIKApwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:cd03226 81 DYQLftdSVREELLL--GLKE----LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3972 SGVDPCSRRSLWDILLK-YREGRTIIFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:cd03226 155 SGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4691-4922 |
9.41e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 103.23 E-value: 9.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGK 4770
Cdd:COG3839 3 SLELENVSKSY-----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI---GGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGIliGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:COG3839 75 RNI--AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4851 DILLLDEPSSGMDPCSKrylWQTITqEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI----KNR 4921
Cdd:COG3839 153 KVFLLDEPLSNLDAKLR---VEMRA-EIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELydrpANL 228
|
.
gi 116292744 4922 F 4922
Cdd:COG3839 229 F 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3810-4020 |
1.00e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.97 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKV-AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGV 3887
Cdd:cd03245 3 IEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3888 CPqQDVLLDNLTVREHLMLFasikAPWWTTKELQQQVNKT-LDevELTQHQhkPAGV----------LSGGMKRKLSIGI 3956
Cdd:cd03245 83 VP-QDVTLFYGTLRDNITLG----APLADDERILRAAELAgVT--DFVNKH--PNGLdlqigergrgLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3957 AFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLdeaEMLS--DHVAVLQQGRL 4020
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP---SLLDlvDRIIVMDSGRI 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3819-4029 |
1.02e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.24 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqtDLSK-----VREELGVC---PQ 3890
Cdd:PRK13638 11 YQDEPV-LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL--DYSKrgllaLRQQVATVfqdPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVL-----------LDNLTVREhlmlfasikapwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFM 3959
Cdd:PRK13638 88 QQIFytdidsdiafsLRNLGVPE---------------AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3960 GMSKTVVLDEPSSGVDPCSRRSLWDILLK-YREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3829-4020 |
1.38e-22 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 99.10 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3829 LTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGVCPQQDVLLDNLTVREH--LML 3906
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNvgLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3907 FASIKapwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDIL 3986
Cdd:cd03298 96 SPGLK----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 116292744 3987 LKYREGR--TIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03298 172 LDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3815-4020 |
1.46e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.47 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFP--PTSGT-ITINGKNLQT------DLSKVREEL 3885
Cdd:PRK09984 10 LAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQRegrlarDIRKSRANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3886 GVCPQQDVLLDNLTVREHLMLFASIKAPWWTT------KELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFM 3959
Cdd:PRK09984 89 GYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3960 GMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3819-4020 |
2.93e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTD---LSKVREELGVCPQQ-DVL 3894
Cdd:PRK13639 11 YPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIVFQNpDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMlFA--SIKAPwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSI-GIAFMGmSKTVVLDEPS 3971
Cdd:PRK13639 91 LFAPTVEEDVA-FGplNLGLS---KEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIaGILAMK-PEIIVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 116292744 3972 SGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4696-4920 |
3.33e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.48 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSyrsvFGGkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGKAGILI 4775
Cdd:PRK09700 10 GIGKS----FGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYcpQQDALDELLTGWEHLqYYCRLR-----GIPK---QYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALV 4847
Cdd:PRK09700 85 IY--QELSVIDELTVLENL-YIGRHLtkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4848 GKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKN 4920
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3793-4002 |
3.41e-22 |
|
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: 104.36 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3793 GLSQQNGPGEMEGGNPGVALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGK 3872
Cdd:TIGR02868 318 AEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3873 NLQT-DLSKVREELGVCPQQDVLLDNlTVREHLMLfasiKAPWWTTKELQqqvnKTLDEVELTQH-QHKPAGV------- 3943
Cdd:TIGR02868 398 PVSSlDQDEVRRRVSVCAQDAHLFDT-TVRENLRL----ARPDATDEELW----AALERVGLADWlRALPDGLdtvlgeg 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3944 ---LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHL 4002
Cdd:TIGR02868 469 garLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3815-4032 |
6.42e-22 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 98.18 E-value: 6.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHkVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGVCPQQDVL 3894
Cdd:cd03296 8 VSKRFGDF-VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFASIK--APWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSS 3972
Cdd:cd03296 86 FRHMTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3973 GVDPCSRRSL--WDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:cd03296 166 ALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4691-4907 |
1.42e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.77 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSVfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGK 4770
Cdd:COG1135 1 MIELENLSKTFPTK-GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV-----DGVDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGIL-----IGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALA 4845
Cdd:COG1135 75 RELRaarrkIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4846 LVGKPDILLLDEPSSGMDPcskrylwQTiTQEV----RD-----GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG1135 155 LANNPKVLLCDEATSALDP-------ET-TRSIldllKDinrelGLTIVLITHEMDVVRRICDRVAVLENG 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3811-4033 |
2.03e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.69 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3811 ALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtdlskvreelgVCPq 3890
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--------------VSA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 qdvLLD-------NLTVREHLMLFASIkapwwttkeL---QQQVNKTLDEV----ELTQHQHKPAGVLSGGMKRKLSIGI 3956
Cdd:COG1134 92 ---LLElgagfhpELTGRENIYLNGRL---------LglsRKEIDEKFDEIvefaELGDFIDQPVKTYSSGMRARLAFAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3957 AFMGMSKTVVLDEPSSGVDP-----CSRRslwdiLLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLK 4030
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAafqkkCLAR-----IRELREsGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
...
gi 116292744 4031 ETY 4033
Cdd:COG1134 235 AAY 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3825-4019 |
2.59e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.60 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQ-QDVLL-------D 3896
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTfQHVRLfremtviE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 NLTVREHLMLFASIKAPWWTT-------KELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDE 3969
Cdd:PRK11300 100 NLLVAQHQQLKTGLFSGLLKTpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3970 PSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4694-4909 |
2.75e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.25 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSyrsvFGGkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLAS---AGK 4770
Cdd:COG1129 7 MRGISKS----FGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL---DGEPVRFRSprdAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGILIGYcpQQDALDELLTGWEHL---QYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALV 4847
Cdd:COG1129 79 AGIAIIH--QELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4848 GKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSF 4909
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4707-4918 |
3.95e-21 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 96.56 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGIL------IGYCPQ 4780
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-----DGQDIAAMSRKELRelrrkkISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4781 QDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSS 4860
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4861 GMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3819-4019 |
4.17e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.73 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSK-VREELGVCPQQ-DVLLD 3896
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGLVFQDpDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 NLTVREHLMlFASIKAPwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSI-GIAFMgMSKTVVLDEPSSGVD 3975
Cdd:PRK13647 94 SSTVWDDVA-FGPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIaGVLAM-DPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116292744 3976 PCSRRSLWDILLK-YREGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK13647 171 PRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
3838-4029 |
6.31e-21 |
|
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: 97.88 E-value: 6.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3838 ITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-----DLSKVREELGVCPQQDVLLDNLTVREHL---MLFAs 3909
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiFLPPEKRRIGYVFQEARLFPHLSVRGNLrygMKRA- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3910 ikapwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKY 3989
Cdd:TIGR02142 104 ------RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 116292744 3990 RE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:TIGR02142 178 HAefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3819-4026 |
6.79e-21 |
|
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: 94.48 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDH-KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQDVLLD 3896
Cdd:cd03244 12 YRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 NlTVREHLMLFASikapwWTTKELQQqvnkTLDEVELTQH-QHKPAG----------VLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:cd03244 92 G-TIRSNLDPFGE-----YSDEELWQ----ALERVGLKEFvESLPGGldtvveeggeNLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDeAEMLSDHVAVLQQGRLRCYAPP 4026
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4696-4918 |
7.57e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVFggkttAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGILI 4775
Cdd:PRK11607 24 NLTKSFDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-----DGVDLSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLL 4855
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4856 DEPSSGMDpcskRYLWQTITQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK11607 174 DEPMGALD----KKLRDRMQLEVVDilervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3820-4020 |
9.87e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 92.76 E-value: 9.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3820 EDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDVLLDNlT 3899
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3900 VREHLMLfasikapwwttkelqqqvnktldeveltqhqhkpagVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSR 3979
Cdd:cd03247 91 LRNNLGR------------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 116292744 3980 RSLWDILLKYREGRTIIFTTHHLDEAEMLsDHVAVLQQGRL 4020
Cdd:cd03247 135 RQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4707-4930 |
1.19e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 97.11 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSttfkilNGETP-----PSSGytviRTPQGDMVDLASAGKAGILIG-YCPQ 4780
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**------RGALPahv*gPDAG----RRPWRF*TWCANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4781 QDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSS 4860
Cdd:NF000106 94 R*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4861 GMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNRFGdGYTVKV 4930
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQI 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3822-4021 |
2.09e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 93.37 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtdlskvreelgVCPqqdvLLD----- 3896
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------------VSS----LLGlgggf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 --NLTVREHLMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGV 3974
Cdd:cd03220 96 npELTGRENIYLNGRLLG--LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3975 DPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:cd03220 174 DAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4696-4909 |
2.45e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 92.32 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAgkagilI 4775
Cdd:cd03226 4 NISFSY----KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS------I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQ--------QDALDELLTGwehlqyycrLRGIPKQyiPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALV 4847
Cdd:cd03226 74 GYVMQdvdyqlftDSVREELLLG---------LKELDAG--NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4848 GKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSF 4909
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4691-4864 |
2.55e-20 |
|
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: 93.12 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVI--------RTPQgdm 4762
Cdd:COG0410 3 MLEVENLHAGY-----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSG-SIRfdgeditgLPPH--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4763 vDLASAGkagilIGYCPQQDALDELLTGWEHLQ---YYCRLRGIPKQYIPEVAA---DLVRRLHleshvdKPVATYSGGT 4836
Cdd:COG0410 74 -RIARLG-----IGYVPEGRRIFPSLTVEENLLlgaYARRDRAEVRADLERVYElfpRLKERRR------QRAGTLSGGE 141
|
170 180
....*....|....*....|....*...
gi 116292744 4837 RRKLSTALALVGKPDILLLDEPSSGMDP 4864
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3803-4038 |
2.82e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.05 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3803 MEGGNPGVALISVTKEYE-DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSK 3880
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3881 VREELGVCPQQ------------DVL--LDNLTVrehlmlfasikapwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSG 3946
Cdd:PRK13648 81 LRKHIGIVFQNpdnqfvgsivkyDVAfgLENHAV---------------PYDEMHRRVSEALKQVDMLERADYEPNALSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3947 GMKRKLSI-GIAFMGMSkTVVLDEPSSGVDPCSRRSLWDILLKYREGR--TIIFTTHHLDEAeMLSDHVAVLQQGRLRCY 4023
Cdd:PRK13648 146 GQKQRVAIaGVLALNPS-VIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKE 223
|
250
....*....|....*
gi 116292744 4024 APPADLKETyGQGLT 4038
Cdd:PRK13648 224 GTPTEIFDH-AEELT 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3819-4020 |
2.82e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISML--MGLFPP---TSGTITINGKNL---QTDLSKVREELGVCPQ 3890
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIyspRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDvlldN---LTVREHLMLFASIKApwwtTKE---LQQQVNKTL------DEVEltQHQHKPAGVLSGGMKRKLSIGIAF 3958
Cdd:PRK14239 94 QP----NpfpMSIYENVVYGLRLKG----IKDkqvLDEAVEKSLkgasiwDEVK--DRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3959 MGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
3840-4019 |
3.65e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.58 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3840 ALLGTNGAGKTTIISMLMGLFPP---TSGTITINGKNLqtDLSKVREELGVCPQQDVLLDNLTVREHLMLFASIKAP-WW 3915
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPrRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3916 TTKELQQQVNKTLDEVELTQHQHKPAGV------LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKY 3989
Cdd:TIGR00955 133 TKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
170 180 190
....*....|....*....|....*....|..
gi 116292744 3990 REGRTIIFTTHHLDEAEM--LSDHVAVLQQGR 4019
Cdd:TIGR00955 213 AQKGKTIICTIHQPSSELfeLFDKIILMAEGR 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3822-4021 |
3.66e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSkvreELGVCPQQDVLLDNLTVR 3901
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA----DRGVVFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3902 EHLML---FASIKApwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCS 3978
Cdd:COG4525 95 DNVAFglrLRGVPK-----AERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116292744 3979 RRSLWDILLKY--REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:COG4525 170 REQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMSPGPGR 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3825-4018 |
3.77e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.93 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELG--VCPQQDVLLDNLTVRE 3902
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGigIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3903 HLML-------FASIKAPWWttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVD 3975
Cdd:PRK09700 100 NLYIgrhltkkVCGVNIIDW--REMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 116292744 3976 PCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:PRK09700 178 NKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3824-4058 |
3.83e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3824 VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL----QTDLSKVR-EELGVCPQQDVLLDNL 3898
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREVRrKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3899 TVREHL---MLFASIKApwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVD 3975
Cdd:PRK10070 122 TVLDNTafgMELAGINA-----EERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3976 PCSRRSLWDILLKY--REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETYGQGLTLTLSKQPSILETQEP 4053
Cdd:PRK10070 197 PLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSA 276
|
....*
gi 116292744 4054 KDVAR 4058
Cdd:PRK10070 277 KDIAR 281
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3825-4020 |
4.32e-20 |
|
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: 90.95 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVC-----PQQDVLLDNLT 3899
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3900 VREHLMLfasikapwwttkelqqqvnktldeveltqhqhkpAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSR 3979
Cdd:cd03215 95 VAENIAL----------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 116292744 3980 RSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:cd03215 141 AEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3823-4029 |
5.19e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.31 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3823 KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKV-REELGVCPQQDVLLDNLTVR 3901
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3902 EhlmLFASIKAPWWTT-----KELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDP 3976
Cdd:PRK10575 104 E---LVAIGRYPWHGAlgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3977 CSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK10575 181 AHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4707-4953 |
5.67e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGIL------IGYCPQ 4780
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-----DGVDIAKISDAELRevrrkkIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4781 QDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSS 4860
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4861 GMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNRFGDGYTVKVWLHKEGSQP 4939
Cdd:PRK10070 194 ALDPLIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQV 273
|
250
....*....|....
gi 116292744 4940 SAVSDCLKLHFPGI 4953
Cdd:PRK10070 274 FSAKDIARRTPNGL 287
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3815-4020 |
6.51e-20 |
|
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: 92.29 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPqQDV 3893
Cdd:cd03253 6 VTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrEVTLDSLRRAIGVVP-QDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 LLDNLTVReHLMLFASIKApwwtTKELQQQVNKT--LDEVELTQHQHKPAGV------LSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:cd03253 85 VLFNDTIG-YNIRYGRPDA----TDEEVIEAAKAaqIHDKIMRFPDGYDTIVgerglkLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAeMLSDHVAVLQQGRL 4020
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3822-4034 |
8.64e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQ----TDLSKVReelGVCPQQDVLLDN 3897
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspAELARRR---AVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3898 LTVREHLMLFAsikAPWWTT-KELQQQVNKTLDEVELTQHQHKPAGVLSGGMK------RKLSIGIAFMGMSKTVVLDEP 3970
Cdd:PRK13548 91 FTVEEVVAMGR---APHGLSrAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3971 SSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPAD------LKETYG 4034
Cdd:PRK13548 168 TSALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEvltpetLRRVYG 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3840-4026 |
8.99e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.97 E-value: 8.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3840 ALLGTNGAGKTTIISMLMGLFPPTSGTITINGK--NLQT---DLSKVREELGVCPQ--QDVLLDNlTVREHLMLfaSIKA 3912
Cdd:PRK13641 37 ALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhiTPETgnkNLKKLRKKVSLVFQfpEAQLFEN-TVLKDVEF--GPKN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3913 PWWTTKELQQQVNKTLDEVEL-TQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKY-R 3990
Cdd:PRK13641 114 FGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqK 193
|
170 180 190
....*....|....*....|....*....|....*.
gi 116292744 3991 EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPP 4026
Cdd:PRK13641 194 AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
4715-4935 |
9.94e-20 |
|
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: 94.41 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGIL------IGYCPQQDALDELL 4788
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL-----NGRTLFDSRKGIFLppekrrIGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4789 TGWEHLQY-YCRLRGIPKQYIPEvaaDLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSK 4867
Cdd:TIGR02142 91 SVRGNLRYgMKRARPSERRISFE---RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4868 R----YLwQTITQEVRDGCaaVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNRfgdgyTVKVWLHKE 4935
Cdd:TIGR02142 168 YeilpYL-ERLHAEFGIPI--LYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS-----PDLPWLARE 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4696-4890 |
1.25e-19 |
|
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: 89.92 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRS-VFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNG--ETPPSSGYTVIRTPQGDMVDLASagkag 4772
Cdd:cd03213 8 NLTVTVKSsPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRK----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4773 iLIGYCPQQDALDELLTGWEHLQYYCRLRGIpkqyipevaadlvrrlhleshvdkpvatySGGTRRKLSTALALVGKPDI 4852
Cdd:cd03213 83 -IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSL 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 116292744 4853 LLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHS 4890
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQ 170
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3812-4020 |
1.47e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.71 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3812 LISVTKEYEDHK---VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL----QTDLSKVREE 3884
Cdd:PRK11153 4 LKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3885 LGVCPQQDVLLDNLTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHK-PAGvLSGGMKRKlsIGIAFMGMSK 3963
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVAL--PLELAGTPKAEIKARVTELLELVGLSDKADRyPAQ-LSGGQKQR--VAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3964 TVVL--DEPSSGVDPCSRRSLWDiLLK--YRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11153 159 PKVLlcDEATSALDPATTRSILE-LLKdiNRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3815-4027 |
1.59e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.00 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYED-HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQQD 3892
Cdd:PRK13635 11 ISFRYPDaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLsEETVWDVRRQVGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3893 vllDN----LTVREHLMlFA--SIKAPwwtTKELQQQVNKTLDEVELTQH-QHKPAGvLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:PRK13635 91 ---DNqfvgATVQDDVA-FGleNIGVP---REEMVERVDQALRQVGMEDFlNREPHR-LSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGRLRCYAPPA 4027
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3824-4034 |
1.75e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.12 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3824 VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTIT-----INGKNLQTdlskvREELGVCPQQDVLLDNL 3898
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT-----RRRVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3899 TVREHLMLFA---SIKApwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVD 3975
Cdd:NF033858 355 TVRQNLELHArlfHLPA-----AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3976 PCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEmLSDHVAVLQQGRLRCYAPPADLKETYG 4034
Cdd:NF033858 430 PVARDMFWRLLieLSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4691-4907 |
2.09e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.33 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRsVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGK 4770
Cdd:PRK11153 1 MIELKNISKVFP-QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV-----DGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGIL-----IGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALA 4845
Cdd:PRK11153 75 KELRkarrqIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4846 LVGKPDILLLDEPSSGMDPcskrylwQTiTQEVRD---------GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK11153 155 LASNPKVLLCDEATSALDP-------AT-TRSILEllkdinrelGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3837-4008 |
2.48e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3837 QITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNlqTDLSKVREE---LGvcpQQDVLLDNLTVREHLMLFASIKAp 3913
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD--IDDPDVAEAchyLG---HRNAMKPALTVAENLEFWAAFLG- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3914 wwtTKELqqQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSigIAFMGMSKTVV--LDEPSSGVDPCSRRSLWDILLKYRE 3991
Cdd:PRK13539 103 ---GEEL--DIAAALEAVGLAPLAHLPFGYLSAGQKRRVA--LARLLVSNRPIwiLDEPTAALDAAAVALFAELIRAHLA 175
|
170 180
....*....|....*....|.
gi 116292744 3992 -GRTIIFTTHH---LDEAEML 4008
Cdd:PRK13539 176 qGGIVIAATHIplgLPGAREL 196
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3807-4020 |
3.01e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.21 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3807 NPGVALISVTKEY-EDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTD-LSKVREE 3884
Cdd:PRK13632 5 SVMIKVENVSFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3885 LGVCPQQDvllDN----LTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMG 3960
Cdd:PRK13632 85 IGIIFQNP---DNqfigATVEDDIAF--GLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3961 MSKTVVLDEPSSGVDPCSRRSLWDILLKYREGR--TIIFTTHHLDEAeMLSDHVAVLQQGRL 4020
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKL 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3815-4029 |
3.17e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.40 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKV-AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTS---GTITINGKNLQTD-LSKVREELGVCP 3889
Cdd:PRK13640 11 VSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKtVWDIREKVGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDvllDN----LTVREHLMLFASIKAPwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSI-GIAFMGmSKT 3964
Cdd:PRK13640 91 QNP---DNqfvgATVGDDVAFGLENRAV--PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIaGILAVE-PKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3965 VVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEI 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3810-4076 |
3.75e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNlQTDLSK---VREELG 3886
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKlqgIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3887 VCPQQ-DVLLDNLTVREHLMLFA-SIKAPwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKT 3964
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPeNLCLP---PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3965 VVLDEPSSGVDPCSRRSLWDILLK-YREGRTIIFTTHHLDEAEMlSDHVAVLQQGRLRCYAPPAD-LKETYGQGLTLTLs 4042
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENvLSDVSLQTLGLTP- 235
|
250 260 270
....*....|....*....|....*....|....*
gi 116292744 4043 kqPSILETQEP-KDVARVTSLIQIYIPQAFLKDSC 4076
Cdd:PRK13644 236 --PSLIELAENlKMHGVVIPWENTSSPSSFAEEIC 268
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3825-4020 |
3.76e-19 |
|
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: 95.96 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQDVLLDNlTVREH 3903
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3904 LMLFASIKAPwwttkelQQQVNKTLDEVELTQHQHK-----------PAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSS 3972
Cdd:TIGR01193 568 LLLGAKENVS-------QDEIWAACEIAEIKDDIENmplgyqtelseEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3973 GVDPCSRRSLWDILLKYREgRTIIFTTHHLDEAEMlSDHVAVLQQGRL 4020
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQ-SDKIIVLDHGKI 686
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
4722-4908 |
4.02e-19 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 89.28 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4722 GECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGIL------IGYCPQQDALDELLTGWEHLQ 4795
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-----NGTVLFDSRKKINLppqqrkIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4796 Y-YCRLRGIPKQYIPEvaaDLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDpcskRYLWQTI 4874
Cdd:cd03297 98 FgLKRKRNREDRISVD---ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD----RALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 116292744 4875 TQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGS 4908
Cdd:cd03297 171 LPELKQikknlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3831-4018 |
7.06e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.96 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3831 LTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNlQTDLSKVR-EELGV--CPQQDVLLDNLTVREHLmLF 3907
Cdd:PRK15439 32 FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP-CARLTPAKaHQLGIylVPQEPLLFPNLSVKENI-LF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3908 ASIKAPWWTTK--ELQQQVNKTLDeveltqhQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDI 3985
Cdd:PRK15439 110 GLPKRQASMQKmkQLLAALGCQLD-------LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSR 182
|
170 180 190
....*....|....*....|....*....|....
gi 116292744 3986 LLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:PRK15439 183 IRELLaQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3815-4057 |
9.42e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQQ-D 3892
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQNpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3893 VLLDNLTVrEHLMLFASIKAPwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSI-GIAFMgMSKTVVLDEPS 3971
Cdd:PRK13652 89 DQIFSPTV-EQDIAFGPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIaGVIAM-EPQVLVLDEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3972 SGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPAD--LKETYGQGLTLTLSKQPSI 4047
Cdd:PRK13652 166 AGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEifLQPDLLARVHLDLPSLPKL 245
|
250
....*....|
gi 116292744 4048 LETQEPKDVA 4057
Cdd:PRK13652 246 IRSLQAQGIA 255
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
3825-4029 |
1.02e-18 |
|
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: 88.58 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPP----TSGTITINGKNLQTdlSKVREELGVCPQQD---VLLDN 3897
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLP--LSIRGRHIATIMQNprtAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3898 LTVREHLMlfASIKAPWWTTKELQQQVNKTLDEVELTQHQ---HKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGV 3974
Cdd:TIGR02770 79 FTMGNHAI--ETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3975 DPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3810-4029 |
1.35e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.87 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL--------------Q 3875
Cdd:PRK10619 6 LNVIDLHKRYGEHEV-LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3876 TDLSKVREELGVCPQQDVLLDNLTVREHLMLfASIKAPWWTTKELQQQVNKTLDEVELTQH-QHKPAGVLSGGMKRKLSI 3954
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVME-APIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3955 GIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3821-4020 |
1.46e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 87.91 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQQDVLLDNlT 3899
Cdd:cd03248 26 DTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3900 VREHLMlFASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAG----VLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVD 3975
Cdd:cd03248 104 LQDNIA-YGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116292744 3976 PCSRRSLWDILLKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGRL 4020
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3823-4029 |
1.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.45 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3823 KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITING-----KNLQTDLSKVREELGVC---PQQDVL 3894
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithKTKDKYIRPVRKRIGMVfqfPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLtvrEHLMLFA--SIKAPWWTTKE----LQQQVNKTLDEVELTQHQhkpagvLSGGMKRKLSIgIAFMGMSKTV-VL 3967
Cdd:PRK13646 100 EDTV---EREIIFGpkNFKMNLDEVKNyahrLLMDLGFSRDVMSQSPFQ------MSGGQMRKIAI-VSILAMNPDIiVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3968 DEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3810-4019 |
1.51e-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: 88.06 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGV 3887
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3888 CpQQDVLLDNLTVREHLMLFASikapwwttkelqqqvNKTLDEVEL---TQHQH-----KPAGV----------LSGGMK 3949
Cdd:cd03251 81 V-SQDVFLFNDTVAENIAYGRP---------------GATREEVEEaarAANAHefimeLPEGYdtvigergvkLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3950 RKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGR 4019
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4691-4922 |
1.94e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.38 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrSVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGK 4770
Cdd:COG4525 3 MLTVRHVSVRY-PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL---DGVPVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGILigycpQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:COG4525 79 GVVF-----QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4851 DILLLDEPSSGMDPCSKRY-------LWQtitqevRDGCAAVLTSHSMEECEALCTRLAIMVdgsfrclGPPQHIKNRF 4922
Cdd:COG4525 154 RFLLMDEPFGALDALTREQmqellldVWQ------RTGKGVFLITHSVEEALFLATRLVVMS-------PGPGRIVERL 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3829-4029 |
2.31e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.05 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3829 LTLTFHRDQITALLGTNGAGKTTIISM---LMGLFPP--TSGTITINGKNL-QTDLSKVREELGVCPQQDVLLDNLTVRE 3902
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3903 HLMLFASIKAPWWTTKELQQQVNKTLDEVEL----TQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCS 3978
Cdd:PRK14247 102 NVALGLKLNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3979 RRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK14247 182 TAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4696-4922 |
2.49e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.21 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNG-ETPpSSGYTVIrtpqgDMVDLA---SAGKA 4771
Cdd:COG1118 7 NISKRF-----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETP-DSGRIVL-----NGRDLFtnlPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GIliGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPD 4851
Cdd:COG1118 76 RV--GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLWqtitQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI----KNRF 4922
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELR----RWLRRlhdelGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVydrpATPF 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3823-4032 |
2.56e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.95 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3823 KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTD----LSKVREELGVCPQ-------- 3890
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDkkvkLSDIRKKVGLVFQypeyqlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 ----QDVLL--DNLTVREhlmlfasikapwwttKELQQQVNKTLDEVELTQHQHKPAGV--LSGGMKRKLSI-GIAFMgM 3961
Cdd:PRK13637 99 etieKDIAFgpINLGLSE---------------EEIENRVKRAMNIVGLDYEDYKDKSPfeLSGGQKRRVAIaGVVAM-E 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3962 SKTVVLDEPSSGVDPCSRRslwDILLKYRE-----GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL-KET 4032
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRD---EILNKIKElhkeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfKEV 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3825-4029 |
2.64e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVRE------ELGVC---PQQDVLL 3895
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlrkEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3896 DNLtvrEHLMLFASIKAPwWTTKELQQQVNKTLDEVELTQHQHKPAGV-LSGGMKRKLSI-GIAFMGmSKTVVLDEPSSG 3973
Cdd:PRK13645 106 ETI---EKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDYVKRSPFeLSGGQKRRVALaGIIAMD-GNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3974 VDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3797-4032 |
2.91e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.39 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3797 QNGPGEMEGGNPGVALISVTKEYeDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqT 3876
Cdd:PRK09452 2 KKLNKQPSSLSPLVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3877 DLSKVREELGVCPQQDVLLDNLTVREHL-----MLfasiKAPwwtTKELQQQVNKTLDEVELTQH-QHKPAGvLSGGMKR 3950
Cdd:PRK09452 80 HVPAENRHVNTVFQSYALFPHMTVFENVafglrMQ----KTP---AAEITPRVMEALRMVQLEEFaQRKPHQ-LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3951 KLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPAD 4028
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELkaLQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
....
gi 116292744 4029 LKET 4032
Cdd:PRK09452 232 IYEE 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3808-4016 |
3.39e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3808 PGVALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKvrEELGV 3887
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3888 CPQQD-------VLLDNLTVREHLMLFASIKAPwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMG 3960
Cdd:PRK15056 83 VPQSEevdwsfpVLVEDVVMMGRYGHMGWLRRA---KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3961 MSKTVVLDEPSSGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQ 4016
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4696-4907 |
4.00e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASA--GKAGI 4773
Cdd:PRK11124 7 GINCFY-----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI---AGNHFDFSKTpsDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 L----IGYCPQQDALdelltgWEHL-------QYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLST 4842
Cdd:PRK11124 79 ElrrnVGMVFQQYNL------WPHLtvqqnliEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4843 ALALVGKPDILLLDEPSSGMDPcskrylwqTITQEVRD--------GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDP--------EITAQIVSiirelaetGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3821-4009 |
6.00e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.49 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDVLLDNLTV 3900
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 REHLMLFASIKAPwwttkeLQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRR 3980
Cdd:TIGR01189 91 LENLHFWAAIHGG------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180 190
....*....|....*....|....*....|...
gi 116292744 3981 SLWDILLKYRE-GRTIIFTTHH---LDEAEMLS 4009
Cdd:TIGR01189 165 LLAGLLRAHLArGGIVLLTTHQdlgLVEARELR 197
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3815-4020 |
6.56e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.45 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYED-----HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITING--KNLQTDLSKVREELGV 3887
Cdd:PRK13633 10 VSYKYESneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3888 CPQQDvllDN---LTVREHLMLFA----SIKApwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSI-GIAFM 3959
Cdd:PRK13633 90 VFQNP---DNqivATIVEEDVAFGpenlGIPP-----EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIaGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3960 gMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAeMLSDHVAVLQQGRL 4020
Cdd:PRK13633 162 -RPECIIFDEPTAMLDPSGRREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4692-4907 |
9.10e-18 |
|
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: 83.97 E-value: 9.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4692 MVLCNLSKSYRsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKA 4771
Cdd:cd03228 1 IEFKNVSFSYP---GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-----DGVDLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GI--LIGYCPQQDAL------DELLtgwehlqyycrlrgipkqyipevaadlvrrlhleshvdkpvatySGGTRRKLSTA 4843
Cdd:cd03228 73 SLrkNIAYVPQDPFLfsgtirENIL--------------------------------------------SGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4844 LALVGKPDILLLDEPSSGMDPCSKRYLWQTItQEVRDGCAAVLTSHSMEECEaLCTRLAIMVDG 4907
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEAL-RALAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3825-4020 |
9.41e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQtdLSKVREELG----VCPQQDVLLDNLTV 3900
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAALAagvaIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 REHLML--FASiKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDpcS 3978
Cdd:PRK11288 97 AENLYLgqLPH-KGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS--A 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116292744 3979 RRS--LWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11288 174 REIeqLFRVIRELRaEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4689-4918 |
9.46e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 9.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4689 GDMMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASA 4768
Cdd:PRK09536 1 MPMIDVSDLSVEF-----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV---AGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4769 GKAGILIGYCPQQDALDELLTGWE--------HLQYYCRLRGIPKQYIPEVAAdlvrRLHLESHVDKPVATYSGGTRRKL 4840
Cdd:PRK09536 73 RAASRRVASVPQDTSLSFEFDVRQvvemgrtpHRSRFDTWTETDRAAVERAME----RTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4841 STALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4694-4907 |
1.02e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqGDMVDLAS---AGK 4770
Cdd:COG3845 8 LRGITKRF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID---GKPVRIRSprdAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGI--------LIgycPQQDALDELLTGWEHLqyycRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLST 4842
Cdd:COG3845 80 LGIgmvhqhfmLV---PNLTVAENIVLGLEPT----KGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4843 ALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
4340-4616 |
1.14e-17 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 88.22 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4340 GGWSFGGQIPNDAEdvKTNTSKPRTLAKVWYNQKGFHSLPSYLNHLNNLILWHHLPANAVdwrQYGITLYSHPYGGALLN 4419
Cdd:pfam12698 77 GKIDGLLVIPKGFS--KDLLKGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVL---LLEALSTSAPIPVESTP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4420 EDRILESIRQCGVALCIVLGFSILSASIGSSVVRDRVTGAKRLQHISGLGHRTYWLINFLYDMLFYLVSVCLCVAVIGAF 4499
Cdd:pfam12698 152 LFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4500 QLTAFtfreNLAATALLLALFGYAMIPWMYLMSRIFSSSDVAFISYISLNFIFGLCTMLMTTMPrllaiiskaqnlqKIY 4579
Cdd:pfam12698 232 GIPFG----NLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLE-------------DPP 294
|
250 260 270
....*....|....*....|....*....|....*..
gi 116292744 4580 NVLKWAFTIFPQFCLGQGLIELCYNQIKYDLTHNFGI 4616
Cdd:pfam12698 295 SFLQWIFSIIPFFSPIDGLLRLIYGDSLWEIAPSLII 331
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4694-4907 |
1.24e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.83 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGKAGI 4773
Cdd:COG4161 5 LKNINCFY-----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 L---IGYCPQQDALdelltgWEHLQYY-------CRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTA 4843
Cdd:COG4161 80 LrqkVGMVFQQYNL------WPHLTVMenlieapCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4844 LALVGKPDILLLDEPSSGMDPcskrylwqTITQEVRD--------GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDP--------EITAQVVEiirelsqtGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3821-4001 |
1.31e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 84.47 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDVLLDNLTV 3900
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 REHLMLFASIKApwwttkelQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRR 3980
Cdd:cd03231 91 LENLRFWHADHS--------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|..
gi 116292744 3981 SLWDILLKYRE-GRTIIFTTHH 4001
Cdd:cd03231 163 RFAEAMAGHCArGGMVVLTTHQ 184
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3810-4029 |
1.41e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.85 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGVCP 3889
Cdd:PRK11432 7 VVLKNITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDVLLDNLTVREHL-----MLFASikapwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKT 3964
Cdd:PRK11432 85 QSYALFPHMSLGENVgyglkMLGVP-------KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3965 VVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4696-4917 |
1.89e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.36 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGKA---- 4771
Cdd:PRK11701 11 GLTKLY-----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 ------GILigycpQQDALDEL---------------LTGWEHlqyYCRLRGIPKQYIPEVAADLVRrlhleshVDKPVA 4830
Cdd:PRK11701 86 llrtewGFV-----HQHPRDGLrmqvsaggnigerlmAVGARH---YGDIRATAGDWLERVEIDAAR-------IDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4831 TYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSF 4909
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|....*
gi 116292744 4910 -------RCLGPPQH 4917
Cdd:PRK11701 231 vesgltdQVLDDPQH 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4696-4918 |
2.09e-17 |
|
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: 85.08 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGilI 4775
Cdd:cd03296 7 NVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF---GGEDATDVPVQERN--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYYCRLRGI----PKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPD 4851
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLwQTITQEVRD--GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:cd03296 157 VLLLDEPFGALDAKVRKEL-RRWLRRLHDelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3823-4018 |
2.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.84 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3823 KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITI------NGKNlQTDLSKVREELGVCPQ------ 3890
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKK-NKKLKPLRKKVGIVFQfpehql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 --QDVLLD------NLTVREhlmlfasikapwwttKELQQQVNKTLDEVELTQH--QHKPAGvLSGGMKRKLSI-GIafM 3959
Cdd:PRK13634 99 feETVEKDicfgpmNFGVSE---------------EDAKQKAREMIELVGLPEEllARSPFE-LSGGQMRRVAIaGV--L 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3960 GMSKTV-VLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:PRK13634 161 AMEPEVlVLDEPTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3803-4020 |
2.83e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3803 MEGGNPGVALISVTKEYE--DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL------ 3874
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3875 -QTDLSKVREELGVCPQQDvlldnlTVREHLMLFASIKAPWWT-----TKELQQQVNKTLDEVELTQHQH----KPAGVL 3944
Cdd:PRK14246 81 fQIDAIKLRKEVGMVFQQP------NPFPHLSIYDNIAYPLKShgikeKREIKKIVEECLRKVGLWKEVYdrlnSPASQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3945 SGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3802-4029 |
2.87e-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: 89.09 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3802 EMEGGNPGVALISVTKEY--EDHKV--AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTD 3877
Cdd:TIGR03269 272 EVEVGEPIIKVRNVSKRYisVDRGVvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3878 LSKVR---------------EELGVCPQQDVlLDNLTVREHLML---FASIKAPW------WTTKELQQQVNKTLDEvel 3933
Cdd:TIGR03269 352 MTKPGpdgrgrakryigilhQEYDLYPHRTV-LDNLTEAIGLELpdeLARMKAVItlkmvgFDEEKAEEILDKYPDE--- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3934 tqhqhkpagvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDH 4011
Cdd:TIGR03269 428 ----------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDR 497
|
250
....*....|....*...
gi 116292744 4012 VAVLQQGRLRCYAPPADL 4029
Cdd:TIGR03269 498 AALMRDGKIVKIGDPEEI 515
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4704-4864 |
3.97e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 83.61 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4704 VFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPQGDMVDLasAGKAGIL----IGYCP 4779
Cdd:cd03292 9 TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSG--TIRVNGQDVSDL--RGRAIPYlrrkIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4780 QQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPS 4859
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
....*
gi 116292744 4860 SGMDP 4864
Cdd:cd03292 165 GNLDP 169
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4663-4923 |
4.93e-17 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 89.12 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4663 LQDIVkpAKDIDVETEQMRVLEGRTGGDMmVLCNLSKSYRsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKIL 4742
Cdd:COG2274 448 LDDIL--DLPPEREEGRSKLSLPRLKGDI-ELENVSFRYP---GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4743 NGETPPSSGYTVIrtpqgDMVDLASAGKAGI--LIGYCPQQDAL-----DELLTGW------EHLQYYCRLRGIpkqyip 4809
Cdd:COG2274 522 LGLYEPTSGRILI-----DGIDLRQIDPASLrrQIGVVLQDVFLfsgtiRENITLGdpdatdEEIIEAARLAGL------ 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4810 evaADLVRRLH--LESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRdGCAAVLT 4887
Cdd:COG2274 591 ---HDFIEALPmgYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIII 666
|
250 260 270
....*....|....*....|....*....|....*.
gi 116292744 4888 SHSMeECEALCTRLAIMVDGSFRCLGPPQHIKNRFG 4923
Cdd:COG2274 667 AHRL-STIRLADRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4709-4918 |
5.31e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.90 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4709 TTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRtpQGDMVDLASAG------KAGILIgycpqQD 4782
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG-RILF--DGKPIDYSRKGlmklreSVGMVF-----QD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4783 ALDELLTG--WEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSS 4860
Cdd:PRK13636 91 PDNQLFSAsvYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4861 GMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3825-4029 |
6.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.79 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGT-----ITINGKNLQTDLSKVREELGVCPQ--QDVLLDN 3897
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3898 LTVREhlmlFASIKAPWWTTKELQQQV-NKTLDEVELTQH-QHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVD 3975
Cdd:PRK13643 101 TVLKD----VAFGPQNFGIPKEKAEKIaAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3976 PCSRRSLWDILLK-YREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13643 177 PKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3821-4019 |
6.17e-17 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 83.36 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQDVLLDNlT 3899
Cdd:cd03249 15 DVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3900 VREHLmLFASIKApwwtTKELQQQVNK--TLDE--VELTQHQHKPAG----VLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:cd03249 93 IAENI-RYGKPDA----TDEEVEEAAKkaNIHDfiMSLPDGYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3972 SGVDPCSRRSLWDILLKYREGRTIIFTTHHLdEAEMLSDHVAVLQQGR 4019
Cdd:cd03249 168 SALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQ 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3814-4031 |
6.28e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.43 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYeDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtDLSKV---REELGVCPQ 3890
Cdd:PRK11607 24 NLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV----DLSHVppyQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREHLMLfaSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEP 3970
Cdd:PRK11607 99 SYALFPHMTVEQNIAF--GLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3971 SSGVDPCSRRSLW----DILlkYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:PRK11607 177 MGALDKKLRDRMQlevvDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4709-4929 |
6.61e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.36 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4709 TTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqGDMVD------LASAGKAGILIgycpqQD 4782
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK---GEPIKydkkslLEVRKTVGIVF-----QN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4783 ALDELL--TGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSS 4860
Cdd:PRK13639 87 PDDQLFapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4861 GMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIknrFGDGYTVK 4929
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV---FSDIETIR 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3825-4029 |
6.86e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQdVLLDNLTVREH 3903
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISVVSQR-VHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3904 LmLFASIKApwwTTKELQQqvnkTLDEVELTQHQHKPAGV----------LSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:PRK11160 434 L-LLAAPNA---SDEALIE----VLQQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3974 VDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLsDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK11160 506 LDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4691-4864 |
7.35e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.79 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfGGKTTAVHGISLGIPRGE-CFgLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAG 4769
Cdd:COG2884 1 MIRFENVSKRY----PGGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLV-----NGQDLSRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGIL-----IGYCPqQDA--LDElLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLST 4842
Cdd:COG2884 71 RREIPylrrrIGVVF-QDFrlLPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180
....*....|....*....|..
gi 116292744 4843 ALALVGKPDILLLDEPSSGMDP 4864
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDP 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4693-4907 |
7.47e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.49 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4693 VLCNLSKSYRsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKA- 4771
Cdd:cd03246 2 EVENVSFRYP---GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-----DGADISQWDPNe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 -GILIGYCPQQdalDELLTGwehlqyycrlrgipkqyipEVAADLVrrlhleshvdkpvatySGGTRRKLSTALALVGKP 4850
Cdd:cd03246 74 lGDHVGYLPQD---DELFSG-------------------SIAENIL----------------SGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEAlCTRLAIMVDG 4907
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4696-4907 |
7.58e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.58 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGILI 4775
Cdd:cd03262 5 NLHKSF-----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-----DGLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 ----GYCPQQDALDELLTGWEHLQYYCR-LRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:cd03262 75 rqkvGMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4691-4916 |
9.31e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTV-----IRTPQGDMVDL 4765
Cdd:PRK09493 1 MIEFKNVSKHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4766 ASagKAGILIgycpQQDALDELLTGWEHLQY-YCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTAL 4844
Cdd:PRK09493 76 RQ--EAGMVF----QQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4845 ALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQ 4916
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQ 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3825-4020 |
1.04e-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: 84.72 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPP---TSGTITINGKNLQT----DLSKVR-EELGVCPqQDVL-- 3894
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELRKIRgREIQMIF-QDPMts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LD-NLTVREHLMLFASIKAPwWTTKELQQQVNKTLDEVELTQ---------HQhkpagvLSGGMKRKlsIGIAfMGMS-- 3962
Cdd:COG0444 99 LNpVMTVGDQIAEPLRIHGG-LSKAEARERAIELLERVGLPDperrldrypHE------LSGGMRQR--VMIA-RALAle 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3963 -KTVVLDEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:COG0444 169 pKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4711-4907 |
1.24e-16 |
|
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: 80.94 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRtpQGDMVDLASAGKA---GIliGYCPQqDALDEL 4787
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASG-EITL--DGKPVTRRSPRDAiraGI--AYVPE-DRKREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4788 LtgwehlqyycrlrgIPKQYIPEVAAdLVRRLhleshvdkpvatySGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSK 4867
Cdd:cd03215 89 L--------------VLDLSVAENIA-LSSLL-------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 116292744 4868 RYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4711-4907 |
1.29e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.61 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTV--------IRTPqgdmvdlASAGKAGIliGYCP--- 4779
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSG-EIrldgkpvrIRSP-------RDAIRAGI--AYVPedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4780 QQDALDELLTGWE-----HLQYYCRLRGIPKQYIPEVAADLVRRLHLE-SHVDKPVATYSGGTRRKLSTALALVGKPDIL 4853
Cdd:COG1129 337 KGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4854 LLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3825-4029 |
1.31e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.64 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-----DLSKVREELGVCPQ--------Q 3891
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQfpesqlfeE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLD------NLTVREhlmlfasikapwwttKELQQQVNKTLDEVELTQHQ-HKPAGVLSGGMKRKLSI-GIAFMgMSK 3963
Cdd:PRK13649 102 TVLKDvafgpqNFGVSQ---------------EEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIaGILAM-EPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3964 TVVLDEPSSGVDPCSRRSLWDILLK-YREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4707-4923 |
1.31e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILngetppsSGYTVIRTPQ-----GDMVDLASAGKAGILIGYCPQQ 4781
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGARKIQQGRvevlgGDMADARHRRAVCPRIAYMPQG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4782 daldeL-------LTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILL 4854
Cdd:NF033858 85 -----LgknlyptLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4855 LDEPSSGMDPCSKRYLWQTItQEVRDGCAA--VLTSHS-MEECEAlCTRLAIMVDGsfRCL--GPPQHIKNRFG 4923
Cdd:NF033858 160 LDEPTTGVDPLSRRQFWELI-DRIRAERPGmsVLVATAyMEEAER-FDWLVAMDAG--RVLatGTPAELLARTG 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4709-4915 |
1.42e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.56 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4709 TTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAG--------KAGILIGYcPQ 4780
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII-----DGVDITDKKvklsdirkKVGLVFQY-PE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4781 QDALDEllTGWEHLQYYCRLRGIPKQYIPE---VAADLVRrLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDE 4857
Cdd:PRK13637 94 YQLFEE--TIEKDIAFGPINLGLSEEEIENrvkRAMNIVG-LDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4858 PSSGMDPCSKrylwQTITQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPP 4915
Cdd:PRK13637 171 PTAGLDPKGR----DEILNKIKElhkeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3826-4029 |
1.42e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3826 VQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQ-TDLSKVREELGVCPQQDVLLDNLTVRE-- 3902
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDTSLSFEFDVRQvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3903 ------HLMLFasikAPWWTTKElqQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDP 3976
Cdd:PRK09536 99 emgrtpHRSRF----DTWTETDR--AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3977 CSR-RSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK09536 173 NHQvRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4690-4916 |
2.63e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4690 DMMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAG 4769
Cdd:PRK11432 5 NFVVLKNITKRF-----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI---DGEDVTHRSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGILIGYcpQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGK 4849
Cdd:PRK11432 77 QRDICMVF--QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4850 PDILLLDEPSSGMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQ 4916
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRElQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4714-4889 |
2.71e-16 |
|
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: 81.16 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4714 GISLGIPRGECFGLLGVNGAGKSTTFKILNG---ETPPSSGYTVIRTPQgdmvdlASAGKAGILIGYCPQQDALDELLTG 4790
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQP------RKPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4791 WEHLQYY--CRLRGIPKQYIP--EVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCS 4866
Cdd:cd03234 99 RETLTYTaiLRLPRKSSDAIRkkRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180
....*....|....*....|...
gi 116292744 4867 KRYLWQTITQEVRDGCAAVLTSH 4889
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3826-4020 |
3.16e-16 |
|
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: 79.57 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3826 VQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQQDVLLDNlTVREHl 3904
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGYLPQDDELFSG-SIAEN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3905 mlfasikapwwttkelqqqvnktldeveltqhqhkpagVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWD 3984
Cdd:cd03246 96 --------------------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 116292744 3985 IL--LKYReGRTIIFTTHHLDEAEMLsDHVAVLQQGRL 4020
Cdd:cd03246 138 AIaaLKAA-GATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3827-4021 |
3.45e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 86.31 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3827 QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQQDVLLdNLTVREHLm 3905
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvQYDHHYLHRQVALVGQEPVLF-SGSVRENI- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3906 LFASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAG----VLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRS 3981
Cdd:TIGR00958 576 AYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 116292744 3982 LWDilLKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGRLR 4021
Cdd:TIGR00958 656 LQE--SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4694-4922 |
5.00e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGI 4773
Cdd:PRK09452 17 LRGISKSF-----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML---DGQDITHVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 LIGYcpQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDIL 4853
Cdd:PRK09452 89 NTVF--QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4854 LLDEPSSGMDpcskrY-LWQTITQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI----KNRF 4922
Cdd:PRK09452 167 LLDESLSALD-----YkLRKQMQNELKAlqrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3809-4020 |
7.48e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.44 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3809 GVALISVTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGK--NLQTDLS-----KV 3881
Cdd:COG4161 2 SIQLKNINCFYGSHQ-ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSekairLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3882 REELGVCPQQDVLLDNLTVREHLmlfasIKAPWW----TTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIA 3957
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENL-----IEAPCKvlglSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3958 FMgMSKTVVL-DEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:COG4161 156 LM-MEPQVLLfDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3821-4020 |
7.94e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 80.22 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQDVLLdNLT 3899
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3900 VREHLML------------FASIKAPWWTTKELQQQVNKTLDEveltqhqhKPAGvLSGGMKRKLSIGIAFMGMSKTVVL 3967
Cdd:cd03252 92 IRDNIALadpgmsmervieAAKLAGAHDFISELPEGYDTIVGE--------QGAG-LSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3968 DEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLdEAEMLSDHVAVLQQGRL 4020
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRI 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4714-4889 |
1.33e-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: 78.69 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4714 GISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLASAGKAGILIGYcpqQDALDELLTGWEH 4793
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG-RVLLNGGPLDFQRDSIARGLLYLGH---APGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4794 LQYYCRLRGipkqyiPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQT 4873
Cdd:cd03231 94 LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*.
gi 116292744 4874 ITQEVRDGCAAVLTSH 4889
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3814-4020 |
1.34e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITIngKNLQTDLSK---------VREE 3884
Cdd:PRK11124 7 GINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI--AGNHFDFSKtpsdkaireLRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3885 LGVCPQQDVLLDNLTVREHLmlfasIKAPW----WTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMg 3960
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNL-----IEAPCrvlgLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3961 MSKTVVL-DEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11124 158 MEPQVLLfDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3824-4031 |
1.54e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.41 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3824 VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITIngknLQTDLSKVREELGVCPQ-----QDV---LL 3895
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV----LGGDMADARHRRAVCPRiaympQGLgknLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3896 DNLTVREHLMLFASI----KApwwttkELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:NF033858 91 PTLSVFENLDFFGRLfgqdAA------ERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3972 SGVDPCSRRSLWDILLKYREGR---TIIFTTHHLDEAEMLsDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:NF033858 165 TGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3837-4000 |
1.65e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 84.78 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3837 QITALLGTNGAGKTTIISML-----MGLFppTSGTITINGKNLQTDLSKVreeLGVCPQQDVLLDNLTVREHLMLFASIK 3911
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRS---IGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3912 APWWTTK-ELQQQVNKTLDEVELTQHQHKPAGVLSGGM----KRKLSIGIAFMGMSKTVV-LDEPSSGVDPcsrRSLWDI 3985
Cdd:TIGR00956 865 QPKSVSKsEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDS---QTAWSI 941
|
170
....*....|....*....
gi 116292744 3986 LLKYRE----GRTIIFTTH 4000
Cdd:TIGR00956 942 CKLMRKladhGQAILCTIH 960
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
3495-3740 |
2.27e-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: 81.28 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3495 LQDMIERAIIVVQTGQESLEPTTQAQAAPYPCHTSDLF---LNNVGFFFPLIMMLTWMVAVASMVRKLVYEREIQIEEYM 3571
Cdd:pfam12698 116 ILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFnpqSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3572 RMMGLHPTIHFLSWFLENMATLALSSAALAVILKMSGIFMHSDAFIIFLYLLdFGVSAVMMSYFLSVFFNQAnTAALCTS 3651
Cdd:pfam12698 196 LVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGNLGLLLLLFLL-YGLAYIALGYLLGSLFKNS-EDAQSII 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3652 LGYMISFLPYVVLLVLHNQLSFAIQTLLCLLSTTAFGQGVFFITFLEgqeegiqwgnmyrapepGGMTFGWVCWMILFDA 3731
Cdd:pfam12698 274 GIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIYGD-----------------SLWEIAPSLIILLLFA 336
|
....*....
gi 116292744 3732 ILYFLGGWY 3740
Cdd:pfam12698 337 VVLLLLALL 345
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3837-4000 |
2.72e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 77.28 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3837 QITALLGTNGAGKTTIISML-----MGLfppTSGTITINGKNLQTDLSKvreELGVCPQQDVLLDNLTVREHLMLFASIK 3911
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDKNFQR---STGYVEQQDVHSPNLTVREALRFSALLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3912 ApwwttkelqqqvnktldeveltqhqhkpagvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPcsrRSLWDI--LLK- 3988
Cdd:cd03232 108 G-------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS---QAAYNIvrFLKk 153
|
170
....*....|...
gi 116292744 3989 -YREGRTIIFTTH 4000
Cdd:cd03232 154 lADSGQAILCTIH 166
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3831-4029 |
2.81e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.78 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3831 LTFH--RDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTD-LSKVREELGVCPQQDvllDN----LTVREH 3903
Cdd:PRK13650 26 VSFHvkQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIGMVFQNP---DNqfvgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3904 LMLFASIKApwWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLW 3983
Cdd:PRK13650 103 VAFGLENKG--IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3984 DILLKYRE--GRTIIFTTHHLDEAEmLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13650 181 KTIKGIRDdyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4705-4921 |
2.90e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.57 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4705 FGGkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMV--DLASAGKAGILIGYcpQQD 4782
Cdd:TIGR02633 11 FGG-VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKasNIRDTERAGIVIIH--QEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4783 ALDELLTGWEH--LQYYCRLRGIPKQYIPEV--AADLVRRLHLE-SHVDKPVATYSGGTRRKLSTALALVGKPDILLLDE 4857
Cdd:TIGR02633 88 TLVPELSVAENifLGNEITLPGGRMAYNAMYlrAKNLLRELQLDaDNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4858 PSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGsfrclgppQHIKNR 4921
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--------QHVATK 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3814-4029 |
3.87e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.21 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITING---KNLQTDLSKVREELGVCPQ 3890
Cdd:PRK09493 6 NVSKHFGPTQV-LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREHLMlFASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEP 3970
Cdd:PRK09493 85 QFYLFPHLTALENVM-FGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3971 SSGVDPCSR-------RSLWDillkyrEGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK09493 164 TSALDPELRhevlkvmQDLAE------EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4690-4891 |
4.44e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4690 DMMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQgdmvdlasag 4769
Cdd:PRK09544 3 SLVSLENVSVSF-----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGK---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 kagILIGYCPQQDALDELLTgwEHLQYYCRLR-GIPKQYI-PevAADLVRRLHLeshVDKPVATYSGGTRRKLSTALALV 4847
Cdd:PRK09544 67 ---LRIGYVPQKLYLDTTLP--LTVNRFLRLRpGTKKEDIlP--ALKRVQAGHL---IDAPMQKLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116292744 4848 GKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSM 4891
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4688-4923 |
6.36e-15 |
|
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: 81.74 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4688 GGDMMVLCNLSKSYRsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSG-YTV----IRTPQGDm 4762
Cdd:COG4987 330 GGPSLELEDVSFRYP---GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGsITLggvdLRDLDED- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4763 vDLASagkagiLIGYCPQQ-----------------DALDELLtgWEHLQyycrlrgipkqyipEVA-ADLVRRLH--LE 4822
Cdd:COG4987 406 -DLRR------RIAVVPQRphlfdttlrenlrlarpDATDEEL--WAALE--------------RVGlGDWLAALPdgLD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4823 SHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGcAAVLTSHSMEECEAlCTRLA 4902
Cdd:COG4987 463 TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRLAGLER-MDRIL 540
|
250 260
....*....|....*....|.
gi 116292744 4903 IMVDGSFRCLGPPQHIKNRFG 4923
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNG 561
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3916-4041 |
7.48e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 79.78 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3916 TTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWD-ILLKYREGRT 3994
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDeVRSMVRDGAT 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 116292744 3995 IIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETYGqGLTLTL 4041
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQI 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3825-4020 |
7.52e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqtDLSKVRE--ELGV--CP---QQDVLLDN 3897
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV--RIRSPRDaiRAGIayVPedrKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3898 LTVREHLMLfASI----KAPWWTTKELQQQVNKTLDEVEL-TQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSS 3972
Cdd:COG1129 345 LSIRENITL-ASLdrlsRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 116292744 3973 GVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:COG1129 424 GIDVGAKAEIYRLIRELaAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3814-4029 |
7.63e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKVAvQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSK-VREELGVCPQQD 3892
Cdd:PRK10253 12 QLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3893 VLLDNLTVREHLMLFASIKAPWWT--TKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEP 3970
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQPLFTrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3971 SSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK10253 171 TTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3822-4020 |
1.10e-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: 77.54 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSK---VREEL---------GVC 3888
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyQLDRKQrraFRRDVqlvfqdspsAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PQQDVlldNLTVREHLMLFASIKApwwttKELQQQVNKTLDEVEL-TQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVL 3967
Cdd:TIGR02769 103 PRMTV---RQIIGEPLRHLTSLDE-----SEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3968 DEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3822-4018 |
1.50e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREE----------LGVCPQQ 3891
Cdd:PRK15112 25 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQrirmifqdpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DV--LLDnLTVREHLMLfasikapwwTTKELQQQVNKTLDEVEL-TQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:PRK15112 105 RIsqILD-FPLRLNTDL---------EPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3969 EPSSGVDPCSRRSLWDILLKYREGRTI--IFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3837-4031 |
1.53e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.05 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3837 QITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREE--LGVCPQQDVLLDNLTVREHLMLFASIKAPW 3914
Cdd:PRK10762 31 RVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEagIGIIHQELNLIPQLTIAENIFLGREFVNRF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3915 ----WttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYR 3990
Cdd:PRK10762 111 gridW--KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 116292744 3991 -EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:PRK10762 189 sQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTE 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4694-4909 |
1.58e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYRSVfggktTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGKAGI 4773
Cdd:PRK11288 7 FDGIGKTFPGV-----KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 LIGYcpQQDALDELLTGWEHL---QYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:PRK11288 82 AIIY--QELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSF 4909
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4708-4907 |
1.67e-14 |
|
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: 76.09 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4708 KTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGY-----TVIRtpQGDMVDLASAgkagilIGYCPQQD 4782
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgTDIR--QLDPADLRRN------IGYVPQDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4783 ALdelltgwehlqYYCRLR-----GIP---KQYIPEVA-----ADLVRRlH---LESHVDKPVATYSGGTRRKLSTALAL 4846
Cdd:cd03245 88 TL-----------FYGTLRdnitlGAPladDERILRAAelagvTDFVNK-HpngLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4847 VGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGcAAVLTSH--SMEEceaLCTRLAIMVDG 4907
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHrpSLLD---LVDRIIVMDSG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3819-4020 |
1.68e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.00 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISML--MG-LFPP--TSGTITINGKNL---QTDLSKVREELGVCPQ 3890
Cdd:COG1117 21 YGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNdLIPGarVEGEILLDGEDIydpDVDVVELRRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLL-----DNLT--VREHLMLfasikapwwTTKELQQQVNKTL------DEVE--LtqhqHKPAGVLSGGMKRKLSI- 3954
Cdd:COG1117 100 KPNPFpksiyDNVAygLRLHGIK---------SKSELDEIVEESLrkaalwDEVKdrL----KKSALGLSGGQQQRLCIa 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3955 -GIAfmgMSKTVVL-DEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:COG1117 167 rALA---VEPEVLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3815-4059 |
1.83e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.87 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFP--PTSGTITINGKNLQTDLSKVREELGVC--PQ 3890
Cdd:TIGR02633 7 IVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIViiHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREHLMLFASIKAPWWTTK--ELQQQVNKTLDEVELT-QHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVL 3967
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPGGRMAynAMYLRAKNLLRELQLDaDNVTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3968 DEPSSGVDPCSRRSLWDIL--LKyREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETygQGLTLTLSKQP 4045
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSED--DIITMMVGREI 242
|
250
....*....|....
gi 116292744 4046 SILETQEPKDVARV 4059
Cdd:TIGR02633 243 TSLYPHEPHEIGDV 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4691-4907 |
1.90e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpQGDMVDLASAGK 4770
Cdd:PRK11614 5 MLSFDKVSAHY-----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFD--GKDITDWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGILIGYCPQQDALDELLTGWEHL----------QYYCRLRGIpkqyipevaADLVRRLHLESHvdKPVATYSGGTRRKL 4840
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLamggffaerdQFQERIKWV---------YELFPRLHERRI--QRAGTMSGGEQQML 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4841 STALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4711-4913 |
2.13e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 76.78 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTvirTPQGDMVDLA-SAGkagiligycpqqdaLDELLT 4789
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAiSAG--------------LSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4790 GWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDpcskry 4869
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD------ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4870 lwQTITQEVRD--------GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLG 4913
Cdd:PRK13546 176 --QTFAQKCLDkiyefkeqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4691-4918 |
2.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSvfggKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIR-TPQGDMVDLASAG 4769
Cdd:PRK13644 1 MIRLENVSYSYPD----GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgIDTGDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 K-AGIL--------IGYCPQQDaldeLLTGWEHLqyyCrlrgIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKL 4840
Cdd:PRK13644 77 KlVGIVfqnpetqfVGRTVEED----LAFGPENL---C----LPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4841 STALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEAlCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4711-4918 |
2.28e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTpqGDMVdLASAG------KAGIL--------IG 4776
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG--TITV--GGMV-LSEETvwdvrrQVGMVfqnpdnqfVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4777 YCPQqdalDELLTGWEHlqyycrlRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLD 4856
Cdd:PRK13635 97 ATVQ----DDVAFGLEN-------IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4857 EPSSGMDPCSKRYLWQTITQEVRDGCAAVLT-SHSMEECeALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3826-4020 |
2.45e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3826 VQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTdlskvreelgVCPQQ-------------- 3891
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT----------RSPQDglangivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 -DVLLDNLTVREHLMLFA----SIKAPWWTTKELQQQVNktlDEVEL----TQHQHKPAGVLSGGMKRKLSIGIAFMGMS 3962
Cdd:PRK10762 338 rDGLVLGMSVKENMSLTAlryfSRAGGSLKHADEQQAVS---DFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3963 KTVVLDEPSSGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
4715-4918 |
3.30e-14 |
|
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: 77.83 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqGDMVDLASAgkAGI-------LIGYCPQQDALDEL 4787
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL----GGEVLQDSA--RGIflpphrrRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4788 LTGWEHLQYYCRLRGIPKQYIPevAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSK 4867
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4868 R----YLwQTITQEVRdgCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:COG4148 170 AeilpYL-ERLRDELD--IPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4691-4927 |
3.41e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.89 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfGGKTtAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTvirTPQGDMVDLASAGK 4770
Cdd:PRK11248 1 MLQISHLYADY----GGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI---TLDGKPVEGPGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 aGILI---GYCPQQDALDELLTGWEhlqyycrLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALV 4847
Cdd:PRK11248 73 -GVVFqneGLLPWRNVQDNVAFGLQ-------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4848 GKPDILLLDEPSSGMDPCSKRYLwQTITQEV--RDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLgppQHIKNRFGDG 4925
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQM-QTLLLKLwqETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARR 220
|
..
gi 116292744 4926 YT 4927
Cdd:PRK11248 221 FV 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3817-4020 |
3.73e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3817 KEYEDHKV---AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVR-----EELGVC 3888
Cdd:PRK11629 13 KRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PQQDVLLDNLTVREHLM--LFASIKAPwwttKELQQQVNKTLDEVELTQH-QHKPAGvLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:PRK11629 93 YQFHHLLPDFTALENVAmpLLIGKKKP----AEINSRALEMLAAVGLEHRaNHRPSE-LSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAvLQQGRL 4020
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4691-4907 |
4.07e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.89 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqG-DMVDLASAG 4769
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID---GkDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGI--------LIGYCPQqdaldelLTGWEHLQY-YCR-----LR-GIPKQYIpEVAADLVRRLH--LESHVDKPVATY 4832
Cdd:COG1101 78 RAKYigrvfqdpMMGTAPS-------MTIEENLALaYRRgkrrgLRrGLTKKRR-ELFRELLATLGlgLENRLDTKVGLL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4833 SGGTRRKLSTALALVGKPDILLLDEPSSGMDP-CSKRYLwqTITQEV--RDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPkTAALVL--ELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4696-4907 |
4.21e-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: 76.00 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRS--VFG--GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTpqgdmVDLASAGKA 4771
Cdd:TIGR02769 7 DVTHTYRTggLFGakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRG-----QDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 G---------ILIGYCPQ----QDALDELLTgwEHLQYYCRLRGIPKQyipEVAADLVRRLHLES-HVDKPVATYSGGTR 4837
Cdd:TIGR02769 82 QrrafrrdvqLVFQDSPSavnpRMTVRQIIG--EPLRHLTSLDESEQK---ARIAELLDMVGLRSeDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4838 RKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4705-4920 |
4.43e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.41 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4705 FGGkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqgdmvDLASAGKAGILIG-------- 4776
Cdd:PRK11300 15 FGG-LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR-------GQHIEGLPGHQIArmgvvrtf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4777 ----YCPQQDALDELLTGwEHLQYYCR-LRGIPKqyIP----------EVAADLVRRLHLESHVDKPVATYSGGTRRKLS 4841
Cdd:PRK11300 87 qhvrLFREMTVIENLLVA-QHQQLKTGlFSGLLK--TPafrraesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4842 TALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKN 4920
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4705-4921 |
4.52e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4705 FGGkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPpsSGytvirTPQGDMV----DLASAG-----KAGILI 4775
Cdd:PRK13549 15 FGG-VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--HG-----TYEGEIIfegeELQASNirdteRAGIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYcpQQDALDELLTGWEHLQYYCRLR--GI---PKQYIPevAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:PRK13549 87 IH--QELALVKELSVLENIFLGNEITpgGImdyDAMYLR--AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGsfrclgppQHIKNR 4921
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG--------RHIGTR 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3823-4018 |
4.73e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3823 KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSkvreELGVCPQQDVLLDNLTVRE 3902
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3903 H----LMLFASIKApwwttkELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCS 3978
Cdd:PRK11248 90 NvafgLQLAGVEKM------QRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 116292744 3979 RRSLWDILLK--YREGRTIIFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:PRK11248 164 REQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4710-4914 |
5.24e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4710 TAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGetppssgytVIRTPQGDMVDLASAGKAGI---LIGYCPQQDALD- 4785
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMG---------FVRLASGKISILGQPTRQALqknLVAYVPQSEEVDw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4786 ---------ELLTGWEHLQYycrLRgIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLD 4856
Cdd:PRK15056 92 sfpvlvedvVMMGRYGHMGW---LR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4857 EPSSGMDPCSKRYLWqTITQEVRD-GCAAVLTSHSMEECEALCTrLAIMVDGSFRCLGP 4914
Cdd:PRK15056 168 EPFTGVDVKTEARII-SLLRELRDeGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGP 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3815-4019 |
5.34e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFP--PTSGTITINGKNLQTDLSKVREELGVC--PQ 3890
Cdd:PRK13549 11 ITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAGIAiiHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREHLMLFASikapwWTTK------ELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKT 3964
Cdd:PRK13549 90 ELALVKELSVLENIFLGNE-----ITPGgimdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3965 VVLDEPSSGVDPCSRRSLWDIL--LKyREGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3827-4019 |
7.16e-14 |
|
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: 73.66 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3827 QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtdlskvreeLGVCPQQDVLLdNLTVREHLML 3906
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWIQ-NGTIRENILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3907 FASIKAPWWttKE------LQQQVnKTLDEVELTQHQHKpaGV-LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSR 3979
Cdd:cd03250 89 GKPFDEERY--EKvikacaLEPDL-EILPDGDLTEIGEK--GInLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 116292744 3980 RSLWD--ILLKYREGRTIIFTTHHLdeaEMLS--DHVAVLQQGR 4019
Cdd:cd03250 164 RHIFEncILGLLLNNKTRILVTHQL---QLLPhaDQIVVLDNGR 204
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
4711-4924 |
1.03e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.62 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqgdmvdlASAGKAGILIGycpqqdaLDELLTG 4790
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK---------GSAALIAISSG-------LNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4791 WEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDpcskryl 4870
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD------- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4871 wQTITQEVRD--------GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIKNRFGD 4924
Cdd:PRK13545 176 -QTFTKKCLDkmnefkeqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4691-4939 |
1.21e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.38 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSksYRsvFGGKTTaVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIR---TPQGDMVDLAS 4767
Cdd:COG4559 1 MLEAENLS--VR--LGGRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSG--EVRlngRPLAAWSPWEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4768 AGKAGILigycPQQDALDELLTGWE--------HLQYYCRLRGIPKQyipevAADLVRRLHLEshvDKPVATYSGGTRRK 4839
Cdd:COG4559 74 ARRRAVL----PQHSSLAFPFTVEEvvalgrapHGSSAAQDRQIVRE-----ALALVGLAHLA---GRSYQTLSGGEQQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4840 --LSTALALV-----GKPDILLLDEPSSGMDPcskrYLWQTITQEVRD----GCAAV-------LTSHsmeeceaLCTRL 4901
Cdd:COG4559 142 vqLARVLAQLwepvdGGPRWLFLDEPTSALDL----AHQHAVLRLARQlarrGGGVVavlhdlnLAAQ-------YADRI 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 116292744 4902 AIMVDGSFRCLGPPQ------HIKNRFgdGYTVKVWLHKEGSQP 4939
Cdd:COG4559 211 LLLHQGRLVAQGTPEevltdeLLERVY--GADLRVLAHPEGGCP 252
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-82 |
1.24e-13 |
|
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: 78.52 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 1 MGHAgRQFQALLWKNWICRLRHPVLSLAEFFWPCILFMILTVLRFQEPPRHRENCYLQARDLPSRGVLPFVQGLLCNTGS 80
Cdd:TIGR01257 1 MGFL-RQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNN 79
|
..
gi 116292744 81 SC 82
Cdd:TIGR01257 80 PC 81
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4703-4907 |
1.40e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4703 SVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILN--GETPPSSGYT--------VIRTPQGDMVDLASAgkag 4772
Cdd:PRK14239 12 SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITgsivynghNIYSPRTDTVDLRKE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4773 ilIGYCPQQDALDELlTGWEHLQYYCRLRGIP-KQYIPEVAA---------DLVR-RLHleshvDKPVAtYSGGTRRKLS 4841
Cdd:PRK14239 88 --IGMVFQQPNPFPM-SIYENVVYGLRLKGIKdKQVLDEAVEkslkgasiwDEVKdRLH-----DSALG-LSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4842 TALALVGKPDILLLDEPSSGMDPCSKRYLWQTITqEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLL-GLKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4715-4962 |
1.61e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.48 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIR----TPQGDMVDLASAGKAGILIGYCPQQDALDEllTG 4790
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhiTPETGNKNLKKLRKKVSLVFQFPEAQLFEN--TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4791 WEHLQYYCRLRGIPKQYIPEVAADLVRRLHL-ESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRY 4869
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4870 LWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHIknrFGDgytvKVWLHKEG-SQPSAVSDCLKL 4948
Cdd:PRK13641 184 MMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI---FSD----KEWLKKHYlDEPATSRFASKL 256
|
250
....*....|....
gi 116292744 4949 HFPGIQFKGQRLNL 4962
Cdd:PRK13641 257 EKGGFKFSEMPLTI 270
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4706-4922 |
1.64e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 77.10 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4706 GGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTpqgDMVDLASAGKA--GILIGYCPQQDa 4783
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAG--SVRL---DGADLSQWDREelGRHIGYLPQDV- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4784 ldELLTGW--EHLqyyCRLRGIPKQYIpeVAA-------DLVRRLHL--ESHVDKPVATYSGGTRRKLSTALALVGKPDI 4852
Cdd:COG4618 416 --ELFDGTiaENI---ARFGDADPEKV--VAAaklagvhEMILRLPDgyDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4853 LLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMeecEAL--CTRLAIMVDGSFRCLGPPQHIKNRF 4922
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFGPRDEVLARL 557
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4696-4918 |
1.68e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.51 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYtvIRTPQGDMVDLASAGKAgilI 4775
Cdd:PRK10851 7 NIKKSF-----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH--IRFHGTDVSRLHARDRK---V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQDALDELLTGWEHLQYycRLRGIPKQYIPEVAA---------DLVRRLHLeshVDKPVATYSGGTRRKLSTALAL 4846
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAF--GLTVLPRRERPNAAAikakvtqllEMVQLAHL---ADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4847 VGKPDILLLDEPSSGMDPCS----KRYLWQtITQEVRdgCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVrkelRRWLRQ-LHEELK--FTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3815-4023 |
1.72e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGknlqtdlskvREELGVCPQQDVL 3894
Cdd:COG0488 4 LSKSFGGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLM-----------------------------------LFASIKApWwttkELQQQVNKTLDEVELTQHQH- 3938
Cdd:COG0488 73 DDDLTVLDTVLdgdaelraleaeleeleaklaepdedlerlaelqeEFEALGG-W----EAEARAEEILSGLGFPEEDLd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3939 KPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYReGrTIIFTTH--H-LDEaemLSDHVAVL 4015
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP-G-TVLVVSHdrYfLDR---VATRILEL 222
|
....*...
gi 116292744 4016 QQGRLRCY 4023
Cdd:COG0488 223 DRGKLTLY 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3815-4020 |
2.02e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.92 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCpQQDV 3893
Cdd:PRK13657 340 VSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVV-FQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 LLDNLTVREHLmlfaSIKAPWWTTKELQQ--QVNKTLDEVEltqhqHKPAGV----------LSGGMKRKLSIGIAFMGM 3961
Cdd:PRK13657 419 GLFNRSIEDNI----RVGRPDATDEEMRAaaERAQAHDFIE-----RKPDGYdtvvgergrqLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3962 SKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLD---EAemlsDHVAVLQQGRL 4020
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNGRV 547
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3828-4031 |
2.50e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.65 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3828 ELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL----QTDLSKVREELGVCPQQDVLLDNLTV--- 3900
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVfdn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 -----REHLMLFASIkapwwttkeLQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVD 3975
Cdd:PRK11831 105 vayplREHTQLPAPL---------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3976 PCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:PRK11831 176 PITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4696-4918 |
2.78e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.68 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGK-AGIL 4774
Cdd:PRK13652 8 DLCYSYS----GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 IgycpqQDALDELL--TGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDI 4852
Cdd:PRK13652 84 F-----QNPDDQIFspTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4853 LLLDEPSSGMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3812-4019 |
2.80e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.92 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3812 LISVTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKN---------LQTDLSKVR 3882
Cdd:PRK10982 1 MSNISKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksskeaLENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3883 EELGVCPQQDVlLDNLTVREHLMlfasiKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMS 3962
Cdd:PRK10982 80 QELNLVLQRSV-MDNMWLGRYPT-----KGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3963 KTVVLDEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4713-4889 |
3.22e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4713 HGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGY-----TVIRTpQGDmvDLASAgkagiLIgYCPQQDALDEL 4787
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEvlwqgEPIRR-QRD--EYHQD-----LL-YLGHQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4788 LTGWEHLQYYCRLRGipkQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKlsTALA--LVGKPDILLLDEPSSGMDPC 4865
Cdd:PRK13538 89 LTALENLRFYQRLHG---PGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPFTAIDKQ 163
|
170 180
....*....|....*....|....
gi 116292744 4866 SKRYLWQTITQEVRDGCAAVLTSH 4889
Cdd:PRK13538 164 GVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4697-4926 |
3.76e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4697 LSKSYRsvfggKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNG-----ETPPSSGYTVIRTPQGDMVDLASAGKA 4771
Cdd:PRK09984 10 LAKTFN-----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdKSAGSHIELLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GILIGYCPQQDALDELLTGWEH---------------LQYYCRLRgipKQYipevAADLVRRLHLESHVDKPVATYSGGT 4836
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENvligalgstpfwrtcFSWFTREQ---KQR----ALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4837 RRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQT---ITQEvrDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLG 4913
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTlrdINQN--DGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
250
....*....|....
gi 116292744 4914 PPQHIKN-RFGDGY 4926
Cdd:PRK09984 236 SSQQFDNeRFDHLY 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3829-4036 |
4.01e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 71.40 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3829 LTLTFHRDQITALLGTNGAGKTTIISMLMGlFP---PTSGTITINGKNLqTDLS---KVREELGVCPQQDVLLDNLTVRE 3902
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPpeeRARLGIFLAFQYPPEIPGVKNAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3903 HLmlfasikapwwttkelqQQVNKTldeveltqhqhkpagvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSL 3982
Cdd:cd03217 97 FL-----------------RYVNEG----------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3983 WDILLKYR-EGRTIIFTTHHLDEAEML-SDHVAVLQQGRLRCYAPPADLKETYGQG 4036
Cdd:cd03217 144 AEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKG 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
4714-4907 |
4.18e-13 |
|
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: 72.11 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4714 GISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGILIGYcpqqdALDELLTGWEH 4793
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL---EGKQITEPGPDRMVVFQNY-----SLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4794 --LQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLW 4871
Cdd:TIGR01184 75 iaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 116292744 4872 QTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:TIGR01184 155 EELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3819-4020 |
4.31e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.57 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHKVaVQELTLTFHRDQITALLGTNGAGKTTII---SMLMGLFPPT--SGTITINGKNL---QTDLSKVREELGVCPQ 3890
Cdd:PRK14267 14 YGSNHV-IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArvEGEVRLFGRNIyspDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREHLMLFASIKAPWWTTKELQQQVNKTLDEV----ELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVV 3966
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3967 LDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3807-4037 |
4.97e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.54 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3807 NPGVALISVTKEYEDHK-------------------VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTI 3867
Cdd:PRK13546 2 NVSVNIKNVTKEYRIYRtnkermkdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3868 TINGknlqtDLSKVREELGVCPQQdVLLDNLTVREHLMLFasikapwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGG 3947
Cdd:PRK13546 82 DRNG-----EVSVIAISAGLSGQL-TGIENIEFKMLCMGF--------KRKEIKAMTPKIIEFSELGEFIYQPVKKYSSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3948 MKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPP 4026
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
250
....*....|.
gi 116292744 4027 ADLKETYGQGL 4037
Cdd:PRK13546 228 DDVLPKYEAFL 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3815-4020 |
5.08e-13 |
|
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: 75.52 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKV-AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCpQQD 3892
Cdd:TIGR02203 336 VTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALV-SQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3893 VLLDNLTVREHLMLFASIKAPWWTTKELQQQVNKT--LDEVELTQHQhkPAGV----LSGGMKRKLSIGIAFMGMSKTVV 3966
Cdd:TIGR02203 415 VVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQdfVDKLPLGLDT--PIGEngvlLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3967 LDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGRL 4020
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3829-4032 |
5.65e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.82 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3829 LTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTD-LSKVREELGVCPQQ-DVLLDNLTVREHLML 3906
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNpDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3907 faSIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDIL 3986
Cdd:PRK13642 106 --GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3987 --LKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:PRK13642 184 heIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3813-4018 |
6.16e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.96 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3813 ISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtDLSKV--RE-ELGVCP 3889
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLhaRDrKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQDVLLDNLTVREHLMLFASI----KAPwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVlprrERP--NAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDIL------LKYregrTIIFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4704-4889 |
6.31e-13 |
|
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: 70.74 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4704 VFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGetppssgytviRTPQGDMV-DLASAGKAG-----ILIGY 4777
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-----------RKTAGVITgEILINGRPLdknfqRSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4778 CPQQDALDELLTGWEHLQYYCRLRGIpkqyipevaadlvrrlhleshvdkpvatySGGTRRKLSTALALVGKPDILLLDE 4857
Cdd:cd03232 84 VEQQDVHSPNLTVREALRFSALLRGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190
....*....|....*....|....*....|..
gi 116292744 4858 PSSGMDPCSKRYLWQTITQEVRDGCAAVLTSH 4889
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4685-4928 |
7.34e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4685 GRTGGDMMvlcNLSKSYrsVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQ---GD 4761
Cdd:PRK14246 4 GKSAEDVF---NISRLY--LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4762 MVDLASAGKAGILIGYCPQQDALDELLTGWEHLQYYCRLRGIP-KQYIPEVAADLVRRLHLESHV----DKPVATYSGGT 4836
Cdd:PRK14246 79 DIFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVydrlNSPASQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4837 RRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITqEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQ 4916
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT-ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237
|
250
....*....|....*.
gi 116292744 4917 HI----KNRFGDGYTV 4928
Cdd:PRK14246 238 EIftspKNELTEKYVI 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3808-4021 |
7.53e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3808 PGVALISVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTS-----GTITINGKNL---QTDLS 3879
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3880 KVREELG-VCPQQDVLldNLTVREHLMLfaSIKAPWWTTK-ELQQQVNKTLDEVEL---TQHQ-HKPAGVLSGGMKRKLS 3953
Cdd:PRK14258 85 RLRRQVSmVHPKPNLF--PMSVYDNVAY--GVKIVGWRPKlEIDDIVESALKDADLwdeIKHKiHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3954 IGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3812-4001 |
7.77e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3812 LISVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQ 3891
Cdd:PRK13540 4 VIELDFDYHDQPL-LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLDNLTVREHLMLFASikapwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:PRK13540 83 SGINPYLTLRENCLYDIH-------FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....
gi 116292744 3972 SGVDpcsRRSLWDILLKYREGR----TIIFTTHH 4001
Cdd:PRK13540 156 VALD---ELSLLTIITKIQEHRakggAVLLTSHQ 186
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3809-4020 |
7.80e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3809 GVALISVTKEYEDHKVAvQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQtDLSKVREELGVC 3888
Cdd:PRK11000 3 SVTLRNVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PQQDVLLDNLTVREHlMLF----ASIKAPwwttkELQQQVNKTLDEVELTqH--QHKPAGvLSGGMKRKLSIGIAFMGMS 3962
Cdd:PRK11000 81 FQSYALYPHLSVAEN-MSFglklAGAKKE-----EINQRVNQVAEVLQLA-HllDRKPKA-LSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3963 KTVVLDEPSSGVDPCSR---RSLWDILLKyREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRvqmRIEISRLHK-RLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4694-4889 |
9.04e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.63 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfGGKTTaVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPqgdmvdlasagkaGI 4773
Cdd:cd03221 3 LENLSKTY----GGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGS-------------TV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 LIGYCPQqdaldelltgwehlqyycrlrgipkqyipevaadlvrrlhleshvdkpvatYSGGTRRKLSTALALVGKPDIL 4853
Cdd:cd03221 64 KIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....*.
gi 116292744 4854 LLDEPSSGMDPCSKRYLWQTITQEvrdGCAAVLTSH 4889
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEY---PGTVILVSH 125
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3824-4026 |
9.39e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.96 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3824 VAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITI----NGKNLQT-------------DLSKVREELG 3886
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNhelitnpyskkikNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3887 VC---PQQDVLLDnlTVREHLMlFASIkAPWWTTKELQQQVNKTLDEVELTQH--QHKPAGvLSGGMKRKLSIGIAFMGM 3961
Cdd:PRK13631 120 MVfqfPEYQLFKD--TIEKDIM-FGPV-ALGVKKSEAKKLAKFYLNKMGLDDSylERSPFG-LSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3962 SKTVVLDEPSSGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPP 4026
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4689-4918 |
9.40e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.04 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4689 GDMMVLC-NLSKSYRSVFGGK-TTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIR----TPQGDM 4762
Cdd:PRK13633 1 MNEMIKCkNVSYKYESNEESTeKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4763 VDLASagKAGILIgycpqQDALDELLT---------GWEHLqyycrlrGIPKQYIPEVAADLVRRLHLESHVDKPVATYS 4833
Cdd:PRK13633 81 WDIRN--KAGMVF-----QNPDNQIVAtiveedvafGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4834 GGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECeALCTRLAIMVDGSFRCL 4912
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVME 225
|
....*.
gi 116292744 4913 GPPQHI 4918
Cdd:PRK13633 226 GTPKEI 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4696-4892 |
9.58e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.08 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSvfggKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASA----GKA 4771
Cdd:PRK13647 9 DLHFRYKD----GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV---MGREVNAENEkwvrSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GILIgycpqQDALDELL--TGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGK 4849
Cdd:PRK13647 82 GLVF-----QDPDDQVFssTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 116292744 4850 PDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSME 4892
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVD 199
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4691-4920 |
1.01e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.95 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYRSvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASA-- 4768
Cdd:PRK13632 7 MIKVENVSFSYPN---SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-----DGITISKEnl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4769 ----GKAGIL--------IGycpqQDALDELLTGWEHlqyycrlRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGT 4836
Cdd:PRK13632 79 keirKKIGIIfqnpdnqfIG----ATVEDDIAFGLEN-------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4837 RRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTIT--QEVRDGCAAVLTsHSMEECeALCTRLAIMVDGSFRCLGP 4914
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISIT-HDMDEA-ILADKVIVFSEGKLIAQGK 225
|
....*.
gi 116292744 4915 PQHIKN 4920
Cdd:PRK13632 226 PKEILN 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4696-4904 |
1.12e-12 |
|
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: 72.39 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRsVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPsSGYTvirtpQGDMV----DLASAGKA 4771
Cdd:COG0444 6 NLKVYFP-TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPP-PGIT-----SGEILfdgeDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GIL------IGYCPQ--QDALDELLT-GW---EHLQYYcrlRGIPKQYIPEVAADLVRRLHL---ESHVDKpvatY---- 4832
Cdd:COG0444 79 ELRkirgreIQMIFQdpMTSLNPVMTvGDqiaEPLRIH---GGLSKAEARERAIELLERVGLpdpERRLDR----Yphel 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4833 SGGTRRKLSTALALVGKPDILLLDEPSSGMDPcskrylwqTITQEV---------RDGCAAVLTSHSMEECEALCTRLAI 4903
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDV--------TIQAQIlnllkdlqrELGLAILFITHDLGVVAEIADRVAV 223
|
.
gi 116292744 4904 M 4904
Cdd:COG0444 224 M 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4691-4918 |
1.23e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLC-NLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVirTPQGDMVDLASAG 4769
Cdd:PRK11231 1 MTLRTeNLTVGY-----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSG-TV--FLGDKPISMLSSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 KAGILIGYCPQQDALDELLTGWE--------HLQYYCRLRGIPKQYIpEVAadlVRRLHLESHVDKPVATYSGGTRRKLS 4841
Cdd:PRK11231 73 QLARRLALLPQHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARV-NQA---MEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4842 TALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4711-4891 |
1.41e-12 |
|
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: 70.59 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGI--LIGYCPQQDAL---- 4784
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-----DGHDLALADPAWLrrQVGVVLQENVLfnrs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4785 --DELLTGWEhlqyycrlrGIPKQYIPEVAA-----DLVRRLHL--ESHVDKPVATYSGGTRRKLSTALALVGKPDILLL 4855
Cdd:cd03252 92 irDNIALADP---------GMSMERVIEAAKlagahDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 116292744 4856 DEPSSGMDPCSKRylwqTITQEVRDGCA---AVLTSHSM 4891
Cdd:cd03252 163 DEATSALDYESEH----AIMRNMHDICAgrtVIIIAHRL 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4687-4892 |
1.48e-12 |
|
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: 74.02 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4687 TGGDMMVLCNLSKSYrsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLA 4766
Cdd:COG4988 332 AGPPSIELEDVSFSY----PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI-----NGVDLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4767 SAGKAGI--LIGYCPQQDAL------DELLTG-----WEHLQYYCRLRGipkqyipevAADLVRRLH--LESHVDKPVAT 4831
Cdd:COG4988 403 DLDPASWrrQIAWVPQNPYLfagtirENLRLGrpdasDEELEAALEAAG---------LDEFVAALPdgLDTPLGEGGRG 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4832 YSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTItQEVRDGCAAVLTSHSME 4892
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL-RRLAKGRTVILITHRLA 533
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4703-4916 |
2.25e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4703 SVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPQGDMVDLASAGKAGILiGYCPQQD 4782
Cdd:PRK13548 9 SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG--EVRLNGRPLADWSPAELARRR-AVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4783 ALD---------EL-LTGWehlqyycRLRGIPKQYIPEVAADLVRRLHLEshvDKPVATYSGGTRRKLSTALALV----- 4847
Cdd:PRK13548 86 SLSfpftveevvAMgRAPH-------GLSRAEDDALVAAALAQVDLAHLA---GRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4848 -GKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAV--------LTSHsmeeceaLCTRLAIMVDGSFRCLGPPQ 4916
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVivvlhdlnLAAR-------YADRIVLLHQGRLVADGTPA 226
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4722-4901 |
2.62e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4722 GECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQgdmvdlASAGKAGILIGYCPQQDALDELLTGWEHLQYYCRLR 4801
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT------ATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4802 GIPKQYIPEVAADLVrrlHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDG 4881
Cdd:PRK13543 111 GRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
170 180
....*....|....*....|
gi 116292744 4882 CAAVLTSHSMEECEALCTRL 4901
Cdd:PRK13543 188 GAALVTTHGAYAAPPVRTRM 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3815-4000 |
2.64e-12 |
|
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: 67.47 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNlqtdlskvreELGVCPQqdvl 3894
Cdd:cd03221 6 LSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------KIGYFEQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 ldnltvrehlmlfasikapwwttkelqqqvnktldeveltqhqhkpagvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGV 3974
Cdd:cd03221 71 -------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180
....*....|....*....|....*.
gi 116292744 3975 DPCSRRSLWDILLKYRegRTIIFTTH 4000
Cdd:cd03221 102 DLESIEALEEALKEYP--GTVILVSH 125
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3825-4020 |
2.69e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTD--------------LSK---------- 3880
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklvIQKtrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3881 -VREELGVCPQ-QDVLLDNLTVREHLMlFASIKapWWTTK-ELQQQVNKTLDEVELTQH--QHKPAGvLSGGMKRKLSI- 3954
Cdd:PRK13651 102 eIRRRVGVVFQfAEYQLFEQTIEKDII-FGPVS--MGVSKeEAKKRAAKYIELVGLDESylQRSPFE-LSGGQKRRVALa 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3955 GIAFMGmSKTVVLDEPSSGVDPCSRRSLWDILLK-YREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK13651 178 GILAME-PDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4709-4918 |
2.98e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4709 TTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqGDMVDLASAG---------KAGILIGYcP 4779
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV----GDIVVSSTSKqkeikpvrkKVGVVFQF-P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4780 QQDALDEllTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHV-DKPVATYSGGTRRKLSTALALVGKPDILLLDEP 4858
Cdd:PRK13643 94 ESQLFEE--TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4859 SSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4696-4863 |
3.00e-12 |
|
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: 73.05 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGetppssgytvirtpqgdmVDLASAGKA---- 4771
Cdd:TIGR03719 9 RVSKVV----PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG------------------VDKDFNGEArpqp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GILIGYCPQQDALDELLTGWEHLQYYCR-LRGIPKQYiPEVAA-----------------------------DLVRRLHL 4821
Cdd:TIGR03719 67 GIKVGYLPQEPQLDPTKTVRENVEEGVAeIKDALDRF-NEISAkyaepdadfdklaaeqaelqeiidaadawDLDSQLEI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 4822 ESHV------DKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:TIGR03719 146 AMDAlrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4712-4907 |
3.02e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGY-------TVIRTPQgdmvDLASAGKA---------GILI 4775
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYvtldgheVVTRSPQ----DGLANGIVyisedrkrdGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQD----ALDELLTGWEHLQYYcrlrgipkqyiPEVAA--DLVRRLHLES-HVDKPVATYSGGTRRKLSTALALVG 4848
Cdd:PRK10762 344 GMSVKENmsltALRYFSRAGGSLKHA-----------DEQQAvsDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 4849 KPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4692-4907 |
3.47e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.46 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4692 MVLC-NLSKSYRSvfgGK--TTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQgdMVDLASA 4768
Cdd:PRK11629 5 LLQCdNLCKRYQE---GSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP--MSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4769 GKAGIL---IGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALA 4845
Cdd:PRK11629 80 AKAELRnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4846 LVGKPDILLLDEPSSGMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAiMVDG 4907
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDG 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4676-4889 |
3.50e-12 |
|
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: 72.66 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4676 ETEQMRVLEG-RTGGDMMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTV 4754
Cdd:TIGR03719 306 ETAEIYIPPGpRLGDKVIEAENLTKAF-----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4755 IrtpqGDMVDLAsagkagiligYCPQQ-DALDELLTGWE-------HLQyycrlrgIPKQYIPEVAadLVRRLHLE-SHV 4825
Cdd:TIGR03719 381 I----GETVKLA----------YVDQSrDALDPNKTVWEeisggldIIK-------LGKREIPSRA--YVGRFNFKgSDQ 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4826 DKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTItqEVRDGCAAVLtSH 4889
Cdd:TIGR03719 438 QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL--LNFAGCAVVI-SH 498
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3822-4020 |
3.68e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.10 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGknlqTDLSKVREELGVCPQQDVLL---DNL 3898
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG----EPLAKLNRAQRKAFRRDIQMvfqDSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3899 -------TVRE-------HLMlfaSIKApwwttKELQQQVNKTLDEVELT-QHQHKPAGVLSGGMKRKLSIGIAFMGMSK 3963
Cdd:PRK10419 100 savnprkTVREiireplrHLL---SLDK-----AERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3964 TVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4694-4907 |
3.90e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYRSVfggktTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGI 4773
Cdd:PRK15439 14 ARSISKQYSGV-----EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI---GGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 L-IGYCPQQDALDELLTGWEHLqyycrLRGIPK-QYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPD 4851
Cdd:PRK15439 86 LgIYLVPQEPLLFPNLSVKENI-----LFGLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3819-4013 |
4.02e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.81 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3819 YEDHkVAVQELTLTFHRDQITALLGTNGAGKTTII---SMLMGLFPP--TSGTITINGKNL---QTDLSKVREELGVCPQ 3890
Cdd:PRK14243 20 YGSF-LAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLyapDVDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 Q-----DVLLDNLTVREHLMLFASikapwwttkELQQQVNKTL------DEVeltQHQHKPAGV-LSGGMKRKLSIGIAF 3958
Cdd:PRK14243 99 KpnpfpKSIYDNIAYGARINGYKG---------DMDELVERSLrqaalwDEV---KDKLKQSGLsLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3959 MGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVA 4013
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3820-4031 |
4.59e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3820 EDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSkVRE--ELGVC-----PQQD 3892
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLS-PRErrRLGVAyipedRLGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3893 VLLDNLTVREHLMLFASIKAPWWT-----TKELQQQVNKTLDE--VeLTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:COG3845 346 GLVPDMSVAENLILGRYRRPPFSRggfldRKAIRAFAEELIEEfdV-RTPGPDTPARSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKE 4031
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATR 491
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3794-4029 |
6.12e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3794 LSQQNGPGEMEGGNPGVALISVTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSG-----TIT 3868
Cdd:PRK14271 6 LGGQSGAADVDAAAPAMAAVNLTLGFAG-KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3869 INGKNL--QTDLSKVREELGVCPQQD-----VLLDNLT--VREHLML----FASIKAPWWTTKELQQQVNKTLDEVELTq 3935
Cdd:PRK14271 85 LGGRSIfnYRDVLEFRRRVGMLFQRPnpfpmSIMDNVLagVRAHKLVprkeFRGVAQARLTEVGLWDAVKDRLSDSPFR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3936 hqhkpagvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMLSDHVAVL 4015
Cdd:PRK14271 164 --------LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALF 235
|
250
....*....|....
gi 116292744 4016 QQGRLRCYAPPADL 4029
Cdd:PRK14271 236 FDGRLVEEGPTEQL 249
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3821-4020 |
6.61e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGlFPPTSGTITINGKNL-QTDLSKVREEL---GvcpqQDVLLD 3896
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELrELDPESWRKHLswvG----QNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 NLTVREHLMLfASIKApwwTTKELQQ-----QVNKTLDEVEL---TQHQHKPAGvLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:PRK11174 436 HGTLRDNVLL-GNPDA---SDEQLQQalenaWVSEFLPLLPQgldTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3969 EPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDE-AEMlsDHVAVLQQGRL 4020
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDlAQW--DQIWVMQDGQI 561
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
4719-4863 |
7.70e-12 |
|
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: 68.59 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4719 IPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytvirtpqgdmvdlaSAGKAGILIGYCPQQDALDELLTGWEHLQYYC 4798
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG---------------DIEIELDTVSYKPQYIKADYEGTVRDLLSSIT 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4799 RLRGIPKQYIPEVAadlvRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:cd03237 87 KDFYTHPYFKTEIA----KPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3808-4020 |
8.26e-12 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 68.70 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3808 PGVALISVTKEYEDHKvAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTD----LSK--- 3880
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGK-GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqLSEaer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3881 ---VREELGVCPQQDvlLDNL--------TVREHLML-----FASIKApwwTTKELQQQVnktldEVELTQHQHKPAgVL 3944
Cdd:TIGR02323 81 rrlMRTEWGFVHQNP--RDGLrmrvsagaNIGERLMAigarhYGNIRA---TAQDWLEEV-----EIDPTRIDDLPR-AF 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3945 SGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3830-4029 |
9.71e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3830 TLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNlQTDLSKVREELGVCPQQDVLLDNLTVREH--LMLF 3907
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNigLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3908 ASIKapwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILL 3987
Cdd:PRK10771 98 PGLK----LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 116292744 3988 KYREGR--TIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK10771 174 QVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3812-4000 |
9.87e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.68 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3812 LISVTKEYE--DHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT----DLSKVREE 3884
Cdd:PRK10535 7 LKDIRRSYPsgEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3885 -LGVCPQQDVLLDNLTVREHL---MLFASIKapwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMG 3960
Cdd:PRK10535 87 hFGFIFQRYHLLSHLTAAQNVevpAVYAGLE-----RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 116292744 3961 MSKTVVLDEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTH 4000
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTH 202
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
3829-4034 |
1.06e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3829 LTLTFHRDQITALLGTNGAGKTTIISMLMGLFpPTSGTITINGKNLQT----DLSKVREELGvcpQQDVLLDNLTVREHL 3904
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYLS---QQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3905 MLFASIKAPwwtTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGM-------SKTVVLDEPSSGVDpC 3977
Cdd:PRK03695 91 TLHQPDKTR---TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVwpdinpaGQLLLLDEPMNSLD-V 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3978 SRRSLWDILLKY--REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPAD------LKETYG 4034
Cdd:PRK03695 167 AQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvltpenLAQVFG 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4655-4890 |
1.55e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 70.47 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4655 RWPRDHSVLQDIVK------PAKDIDVETEQMRVLEGRTggdmMVLCNLSKSYrsvfGGKTTAVHGISLGIPRGECFGLL 4728
Cdd:TIGR02868 296 QLTRVRAAAERIVEvldaagPVAEGSAPAAGAVGLGKPT----LELRDLSAGY----PGAPPVLDGVSLDLPPGERVAIL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4729 GVNGAGKSTTFKILNGETPPSSG-YTVirtpqgDMVDLASAGKAGI--LIGYCPQQ------DALDELLTGwehlqyycr 4799
Cdd:TIGR02868 368 GPSGSGKSTLLATLAGLLDPLQGeVTL------DGVPVSSLDQDEVrrRVSVCAQDahlfdtTVRENLRLA--------- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4800 lRGipkQYIPEVAADLVRRLHLESHV-------DKPV----ATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKR 4868
Cdd:TIGR02868 433 -RP---DATDEELWAALERVGLADWLralpdglDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
250 260
....*....|....*....|..
gi 116292744 4869 YLWQTITQeVRDGCAAVLTSHS 4890
Cdd:TIGR02868 509 ELLEDLLA-ALSGRTVVLITHH 529
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3821-4016 |
1.68e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtDLSKVREELgvcpQQDVLL----- 3895
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE----PIRRQRDEY----HQDLLYlghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3896 ---DNLTVREHLMLFASIKAPwwTTKELQQQVnktLDEVELTQHQHKPAGVLSGGMKRKlsIGIAFMGMSKTV--VLDEP 3970
Cdd:PRK13538 84 gikTELTALENLRFYQRLHGP--GDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRR--VALARLWLTRAPlwILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 116292744 3971 SSGVDPCSRRSLWDILLKY-REGRTIIFTTHHldEAEMLSDHVAVLQ 4016
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHaEQGGMVILTTHQ--DLPVASDKVRKLR 201
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4691-4864 |
1.97e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.33 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqGDMVDLASAGK 4770
Cdd:COG1126 1 MIEIENLHKSF-----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD---GEDLTDSKKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGIL--IGYCPQQDALdelltgWEHL---------QyyCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRK 4839
Cdd:COG1126 73 NKLRrkVGMVFQQFNL------FPHLtvlenvtlaP--IKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQR 144
|
170 180
....*....|....*....|....*
gi 116292744 4840 LSTALALVGKPDILLLDEPSSGMDP 4864
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDP 169
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4712-4915 |
2.08e-11 |
|
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: 66.40 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGECFGLLGVNGAGKSTTFKILNGEtppsSGYTVIRtpqGDMV----DLASA-----GKAGILIGYcpqqd 4782
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----PKYEVTE---GEILfkgeDITDLppeerARLGIFLAF----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4783 aldelltgwehlqyycrlrgipkQYIPEVA----ADLVRRLHleshvdkpvATYSGGTRRKLSTALALVGKPDILLLDEP 4858
Cdd:cd03217 84 -----------------------QYPPEIPgvknADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4859 SSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEAL-CTRLAIMVDGSFRCLGPP 4915
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3800-4020 |
2.60e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3800 PGEMEGGNPgVALISVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTItINGknlQTDLS 3879
Cdd:PRK11247 4 TARLNQGTP-LLLNAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3880 KVREELGVCPQQDVLLDNLTVREHLMLfaSIKAPWwttkelQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFM 3959
Cdd:PRK11247 78 EAREDTRLMFQDARLLPWKKVIDNVGL--GLKGQW------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 3960 GMSKTVVLDEPSSGVDPCSR-------RSLWDillkyREGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRiemqdliESLWQ-----QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4704-4892 |
3.20e-11 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 69.62 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4704 VFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGIL--IGYCPQQ 4781
Cdd:TIGR02857 330 AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV-----NGVPLADADADSWRdqIAWVPQH 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4782 DALDElLTGWEHLQYYCR-------LRGIPKQYIPEVAADLVRRLHLEshVDKPVATYSGGTRRKLSTALALVGKPDILL 4854
Cdd:TIGR02857 405 PFLFA-GTIAENIRLARPdasdaeiREALERAGLDEFVAALPQGLDTP--IGEGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 116292744 4855 LDEPSSGMDPCSKrylwQTITQEVRD---GCAAVLTSHSME 4892
Cdd:TIGR02857 482 LDEPTAHLDAETE----AEVLEALRAlaqGRTVLLVTHRLA 518
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4712-4907 |
3.41e-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: 69.47 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPS-SGYTVIRTPQGDMVDLASAGKAGILI--------GYCPQQd 4782
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMvpedrkrhGIVPIL- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4783 ALDELLTgWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLE-SHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSG 4861
Cdd:TIGR02633 355 GVGKNIT-LSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116292744 4862 MDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4694-4918 |
3.48e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.46 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYRS--VFGGKttAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIR----TPQGDMVDLAS 4767
Cdd:PRK13649 5 LQNVSYTYQAgtPFEGR--ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtliTSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4768 AGKAGILIGYCPQQDALDEllTGWEHLQYYCRLRGIPKqyipEVAADLVR-RLHL----ESHVDKPVATYSGGTRRKLST 4842
Cdd:PRK13649 83 IRKKVGLVFQFPESQLFEE--TVLKDVAFGPQNFGVSQ----EEAEALAReKLALvgisESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4843 ALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4704-4918 |
4.03e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4704 VFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILN-----GETPPSSGYTV-----IRTPQGDMVDLASagKAGI 4773
Cdd:PRK14267 12 VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRlfgrnIYSPDVDPIEVRR--EVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 LIGY---CPQqdaldelLTGWEHLQYYCRLRGI--PKQYIPEVAADLVRRLHLESHV-----DKPvATYSGGTRRKLSTA 4843
Cdd:PRK14267 90 VFQYpnpFPH-------LTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVkdrlnDYP-SNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4844 LALVGKPDILLLDEPSSGMDPCSKRYLwQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKI-EELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4691-4890 |
4.25e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLC-NLSkSYRsvfGGKTtAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAg 4769
Cdd:PRK13539 1 MMLEGeDLA-CVR---GGRV-LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4770 kagilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAAD--LVRRLHLeshvdkPVATYSGGTRRKLSTA-LAL 4846
Cdd:PRK13539 75 -----CHYLGHRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAvgLAPLAHL------PFGYLSAGQKRRVALArLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 116292744 4847 VGKPdILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHS 4890
Cdd:PRK13539 144 SNRP-IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3810-4017 |
4.48e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3810 VALISVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtdlskvrEELGVCP 3889
Cdd:PRK09544 5 VSLENVSVSFGQRRV-LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------LRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3890 QQdVLLDN---LTVREHLMLFASIKapwwttkelQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVV 3966
Cdd:PRK09544 74 QK-LYLDTtlpLTVNRFLRLRPGTK---------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3967 LDEPSSGVDPCSRRSLWDILLKYRE--GRTIIFTTHHLDEAEMLSDHVAVLQQ 4017
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3823-4019 |
5.11e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.65 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3823 KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtDLSKVREE--------------LGVC 3888
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK----DVTKLPEYkrakyigrvfqdpmMGTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PqqdvlldNLTVREHLMLFASIKAP----WWTTKELQQQVNKTLDEVE--LTQHQHKPAGVLSGGMKRKLSIGIAFMGMS 3962
Cdd:COG1101 95 P-------SMTIEENLALAYRRGKRrglrRGLTKKRRELFRELLATLGlgLENRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3963 KTVVLDEPSSGVDPcsRRSlwDILLKY------REGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:COG1101 168 KLLLLDEHTAALDP--KTA--ALVLELtekiveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4708-4918 |
5.25e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.75 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4708 KTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNG----ETPPSSGYTV--IRTPQGDMVDLASagKAGILIGYCPQQ 4781
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVdgITLTAKTVWDIRE--KVGIVFQNPDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4782 ----DALDELLTGWEHlqyycrlRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDE 4857
Cdd:PRK13640 97 fvgaTVGDDVAFGLEN-------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4858 PSSGMDPCSKRYLWQTITQEVRDGCAAVLT-SHSMEECEaLCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3828-4020 |
5.53e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3828 ELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVcpqqdVLLDNLTVREHLMLF 3907
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL-----VYLPEDRQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3908 ASI----------KAPWW--TTKElqqqvNKTLDE------VELTqHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDE 3969
Cdd:PRK15439 356 APLawnvcalthnRRGFWikPARE-----NAVLERyrralnIKFN-HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3970 PSSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3837-4019 |
7.37e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.75 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3837 QITALLGTNGAGKTTIISMLMGLFPPTS--GTITINGKNLQTDLSKvreELGVCPQQDVLLDNLTVREHLMLFASIKAPW 3914
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK---RTGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3915 WTTKELQQQVNKT-LDEVELTQHQHKPAGV-----LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLK 3988
Cdd:PLN03211 172 SLTKQEKILVAESvISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190
....*....|....*....|....*....|...
gi 116292744 3989 Y-REGRTIIFTTHH-LDEAEMLSDHVAVLQQGR 4019
Cdd:PLN03211 252 LaQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4714-4910 |
7.68e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4714 GISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSG-YTVIRTPQGDMVDLASAGKAGILIGYCPQQDALDELLTGWE 4792
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGeVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4793 HLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQ 4872
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 116292744 4873 TITQEVRD-GCAAVLTSHSmEECEALCTRLAIMVDGSFR 4910
Cdd:PRK10584 188 LLFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4711-4931 |
8.22e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.34 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYT-----VIRTPQGDMVDLASAGKAGILIGYCPQQ---D 4782
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvddiTITHKTKDKYIRPVRKRIGMVFQFPESQlfeD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4783 ALD-ELLTGWEHLqyycrlrGIPKQYIPEVAADLVRRLHLESHV-DKPVATYSGGTRRKLSTALALVGKPDILLLDEPSS 4860
Cdd:PRK13646 102 TVErEIIFGPKNF-------KMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4861 GMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPqhiKNRFGDGYTVKVW 4931
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP---KELFKDKKKLADW 243
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4714-4918 |
9.64e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.80 E-value: 9.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4714 GISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGkagiLIGYCPQ-----QDALDELL 4788
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLW---QGKPLDYSKRG----LLALRQQvatvfQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4789 -TGWEH-LQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCS 4866
Cdd:PRK13638 92 yTDIDSdIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4867 KRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3821-4019 |
9.75e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTdLS--KVREELGVCPQQDVLLDNl 3898
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST-LKpeIYRQQVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3899 TVREHLMLfasikaPWWTTKEL--QQQVNKTLDEVELTQHQ-HKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVD 3975
Cdd:PRK10247 96 TVYDNLIF------PWQIRNQQpdPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3976 PCSRRSLWDILLKYREGRTI--IFTTH------HLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIavLWVTHdkdeinHADKVITLQPHAGEMQEAR 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4715-4907 |
1.13e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDLASAGKAGILigYCP---QQDAL--DELLT 4789
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLV--YLPedrQSSGLylDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4790 gWEHLQYYCRLRGIPKQyiPEVAADLVRRLHLE-----SHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDP 4864
Cdd:PRK15439 360 -WNVCALTHNRRGFWIK--PARENAVLERYRRAlnikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 116292744 4865 CSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4707-4893 |
1.18e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGEcFGLL-GVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGILIGYCPQQDAL- 4784
Cdd:PRK10247 18 GDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLF---EGEDISTLKPEIYRQQVSYCAQTPTLf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4785 -----DELLTGWEhlqyycrLRGI---PKQYipevAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLD 4856
Cdd:PRK10247 94 gdtvyDNLIFPWQ-------IRNQqpdPAIF----LDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 116292744 4857 EPSSGMDPCSKRYLWQTITQEVRDGCAAVL-TSHSMEE 4893
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLwVTHDKDE 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3815-4020 |
1.31e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL----QTDLSKVREELGVCPQ 3890
Cdd:PRK10908 7 VSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 QDVLLDNLTVREHLMLFASIKAPwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEP 3970
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGA--SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3971 SSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4696-4863 |
1.59e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfGGKTTAVHGislG-IPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYtvirtpqgdmVDLAsagkagIL 4774
Cdd:PRK13409 345 DLTKKL----GDFSLEVEG---GeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE----------VDPE------LK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 IGYCPQ-----QDALDELLtgwehlqyycrLRGIPKQ-----YIPEvaadLVRRLHLESHVDKPVATYSGGTRRKLSTAL 4844
Cdd:PRK13409 402 ISYKPQyikpdYDGTVEDL-----------LRSITDDlgssyYKSE----IIKPLQLERLLDKNVKDLSGGELQRVAIAA 466
|
170
....*....|....*....
gi 116292744 4845 ALVGKPDILLLDEPSSGMD 4863
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLD 485
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4722-4889 |
1.60e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4722 GECFGLLGVNGAGKSTTFKILNGETppSSGYTV--IRTPQGDMVDLASAGKagilIGYCPQQDALDELLTGWEHLQYYCR 4799
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERV--TTGVITggDRLVNGRPLDSSFQRS----IGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4800 LR---GIPK----QYIPEVaadlVRRLHLESHVDKPVATYSGG----TRRKLSTALALVGKPDILL-LDEPSSGMDPCSK 4867
Cdd:TIGR00956 863 LRqpkSVSKsekmEYVEEV----IKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170 180
....*....|....*....|..
gi 116292744 4868 RYLWQTITQEVRDGCAAVLTSH 4889
Cdd:TIGR00956 939 WSICKLMRKLADHGQAILCTIH 960
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
3838-4025 |
1.65e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3838 ITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqtdlskVREELGVC--PQ--------QDV-LLDNLTVREHL-- 3904
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL------FDAEKGIClpPEkrrigyvfQDArLFPHYKVRGNLry 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3905 -MlfasikapwwtTKELQQQVNKTldeVELTQHQH----KPAGvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSR 3979
Cdd:PRK11144 100 gM-----------AKSMVAQFDKI---VALLGIEPlldrYPGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 3980 RSLWDILLKY-REGRT-IIFTTHHLDEAEMLSDHVAVLQQGRLRCYAP 4025
Cdd:PRK11144 165 RELLPYLERLaREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4707-4918 |
1.70e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.99 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGILIGYCPQQDALDE 4786
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVV---NGQTINLVRDKDGQLKVADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4787 LLTG-------WEHL-------QYYCRLRGIPKQYIPEVAADLVRRLHL-ESHVDKPVATYSGGTRRKLSTALALVGKPD 4851
Cdd:PRK10619 93 RLTMvfqhfnlWSHMtvlenvmEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4852 ILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4694-4863 |
1.85e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.44 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYRSvfGGKTTAV-HGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPQGDMVDLASAGKAG 4772
Cdd:PRK10535 7 LKDIRRSYPS--GEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG--TYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4773 IL---IGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGK 4849
Cdd:PRK10535 83 LRrehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170
....*....|....
gi 116292744 4850 PDILLLDEPSSGMD 4863
Cdd:PRK10535 163 GQVILADEPTGALD 176
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4716-4907 |
1.91e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 63.67 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4716 SLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAGILIGYCPQQDALDELLTGWEH-- 4793
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI-----NGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4794 --LQYYCRLRGIPKQYIPEVAAdlvrRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCskryLW 4871
Cdd:cd03298 93 lgLSPGLKLTAEDRQAIEVALA----RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA----LR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 116292744 4872 QTITQEVRDGCA-----AVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:cd03298 165 AEMLDLVLDLHAetkmtVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4717-4863 |
2.09e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4717 LGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVI--------------RTPQGDMVDLASAG---KAGILIGYCP 4779
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqqdppRNVEGTVYDFVAEGieeQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4780 -----QQDALDELLTGWEHLQYYCRLRGIPK--QYIPEVAAdlvrRLHLEShvDKPVATYSGGTRRKLSTALALVGKPDI 4852
Cdd:PRK11147 104 ishlvETDPSEKNLNELAKLQEQLDHHNLWQleNRINEVLA----QLGLDP--DAALSSLSGGWLRKAALGRALVSNPDV 177
|
170
....*....|.
gi 116292744 4853 LLLDEPSSGMD 4863
Cdd:PRK11147 178 LLLDEPTNHLD 188
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4691-4921 |
2.23e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSyrsvFGGKTTaVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTpqGD-MVDLA-SA 4768
Cdd:PRK11264 3 AIEVKNLVKK----FHGQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAG--TIRV--GDiTIDTArSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4769 GKAGILI-------GYC-------PQQDALDELLTGwehlqyYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSG 4834
Cdd:PRK11264 74 SQQKGLIrqlrqhvGFVfqnfnlfPHRTVLENIIEG------PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4835 GTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGP 4914
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
250
....*....|....
gi 116292744 4915 -------PQHIKNR 4921
Cdd:PRK11264 228 akalfadPQQPRTR 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4719-4863 |
2.32e-10 |
|
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: 67.12 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4719 IPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTvirtpqgdmvdlasagKAGILIGYCPQ-----QDALDELLtgweh 4793
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------------DEDLKISYKPQyispdYDGTVEEF----- 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4794 lqyycrLRGIPKQYIPE--VAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:COG1245 422 ------LRSANTDDFGSsyYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3800-4000 |
2.60e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.56 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3800 PGEMEggNPGVAlisvtkeyEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGlfPPTSGtiTINGKNLQTDLS 3879
Cdd:PLN03140 880 PAEMK--EQGVT--------EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDIRISGFP 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3880 KVREEL----GVCPQQDVLLDNLTVREHLMLFASIKAPWWTTKELQQQ-VNKTLDEVELTQHQHKPAGV-----LSGGMK 3949
Cdd:PLN03140 946 KKQETFarisGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMfVDEVMELVELDNLKDAIVGLpgvtgLSTEQR 1025
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3950 RKLSIGIAFMGMSKTVVLDEPSSGVDPcsrRSLWDILLKYRE----GRTIIFTTH 4000
Cdd:PLN03140 1026 KRLTIAVELVANPSIIFMDEPTSGLDA---RAAAIVMRTVRNtvdtGRTVVCTIH 1077
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4715-4907 |
2.94e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqGDMVDLASAG---KAGILIgyCPQ---QDALDELL 4788
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD---GKPIDIRSPRdaiRAGIML--CPEdrkAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4789 TGWEHLQYYCRLRGIPKQYI------PEVAADLVRRLHLES-HVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSG 4861
Cdd:PRK11288 347 SVADNINISARRHHLRAGCLinnrweAENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116292744 4862 MDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3796-4019 |
3.05e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3796 QQNGPGEMEGGNPGVALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQ 3875
Cdd:PRK10790 327 QQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3876 TdLSKVREELGVC-PQQD--VLLDnlTVREHLMLFASIKapwwttkelQQQVNKTLDEVELTQHQHK-PAGV-------- 3943
Cdd:PRK10790 407 S-LSHSVLRQGVAmVQQDpvVLAD--TFLANVTLGRDIS---------EEQVWQALETVQLAELARSlPDGLytplgeqg 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3944 --LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLD---EAemlsDHVAVLQQG 4018
Cdd:PRK10790 475 nnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEA----DTILVLHRG 550
|
.
gi 116292744 4019 R 4019
Cdd:PRK10790 551 Q 551
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4696-4889 |
3.32e-10 |
|
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: 62.33 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKA-GIL 4774
Cdd:cd03247 5 NVSFSYP---EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-----DGVPVSDLEKAlSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 IGYCPQQdaldelltgwehlqyycrlrgiPKQYIPEVAADLVRRLhleshvdkpvatySGGTRRKLSTALALVGKPDILL 4854
Cdd:cd03247 77 ISVLNQR----------------------PYLFDTTLRNNLGRRF-------------SGGERQRLALARILLQDAPIVL 121
|
170 180 190
....*....|....*....|....*....|....*
gi 116292744 4855 LDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSH 4889
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHH 156
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3821-4000 |
3.97e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.26 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREEL-----GVCPQQDVL 3894
Cdd:PRK10584 20 EHELSIlTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvGFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFASIKAPwwTTKELQQQVNKTLDEVELTQH-QHKPAGvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:PRK10584 100 IPTLNALENVELPALLRGE--SSRQSRNGAKALLEQLGLGKRlDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180
....*....|....*....|....*....
gi 116292744 3974 VDPCSRRSLWDIL--LKYREGRTIIFTTH 4000
Cdd:PRK10584 177 LDRQTGDKIADLLfsLNREHGTTLILVTH 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4696-4922 |
3.97e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSyrsvFGGKTtAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNG--ETPPSSG---YTVIRTPQGDMVDLASagK 4770
Cdd:TIGR03269 5 NLTKK----FDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiYHVALCEKCGYVERPS--K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AGILIGYC-------------------------------------PQQDALDELLTGWEHLQYycrlrgiPKQYIPEVAA 4813
Cdd:TIGR03269 78 VGEPCPVCggtlepeevdfwnlsdklrrrirkriaimlqrtfalyGDDTVLDNVLEALEEIGY-------EGKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4814 DLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSME 4892
Cdd:TIGR03269 151 DLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPE 230
|
250 260 270
....*....|....*....|....*....|
gi 116292744 4893 ECEALCTRLAIMVDGSFRCLGPPQHIKNRF 4922
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4712-4924 |
4.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGILIGYCPQQ--------DA 4783
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---DGDLLTEENVWDIRHKIGMVFQNpdnqfvgaTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4784 LDELLTGWEHlqyycrlRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK13650 100 EDDVAFGLEN-------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116292744 4864 PCSKRYLWQTItQEVRD--GCAAVLTSHSMEECeALCTRLAIMVDGSFRCLGPPQHIKNRFGD 4924
Cdd:PRK13650 173 PEGRLELIKTI-KGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
4705-4926 |
5.51e-10 |
|
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: 63.54 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4705 FGGKTTAVHGisLGIPR-GECFGLLGVNGAGKSTTFKILNGETPPSSGytvirtpqgdmvdlasagkagiliGYCPQQDa 4783
Cdd:cd03236 10 YGPNSFKLHR--LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLG------------------------KFDDPPD- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4784 LDELLT---GWEHLQYYCRLRG--------------IPKQYIPEVAA------------DLVRRLHLESHVDKPVATYSG 4834
Cdd:cd03236 63 WDEILDefrGSELQNYFTKLLEgdvkvivkpqyvdlIPKAVKGKVGEllkkkdergkldELVDQLELRHVLDRNIDQLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4835 GTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIM--VDGSFRCL 4912
Cdd:cd03236 143 GELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLygEPGAYGVV 222
|
250
....*....|....*..
gi 116292744 4913 GPPQHIK---NRFGDGY 4926
Cdd:cd03236 223 TLPKSVRegiNEFLDGY 239
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4696-4858 |
5.65e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYrsvfGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKIL-------NGETPPSSGYTVirtpqgdmvdlasa 4768
Cdd:PRK11819 11 RVSKVV----PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkefEGEARPAPGIKV-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4769 gkagiliGYCPQQDALDELLTGWEHLQYYC--------RLRGI------PKQYIPEVAA---------------DLVRRL 4819
Cdd:PRK11819 73 -------GYLPQEPQLDPEKTVRENVEEGVaevkaaldRFNEIyaayaePDADFDALAAeqgelqeiidaadawDLDSQL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 116292744 4820 HLESHV------DKPVATYSGGTRRKLstALA--LVGKPDILLLDEP 4858
Cdd:PRK11819 146 EIAMDAlrcppwDAKVTKLSGGERRRV--ALCrlLLEKPDMLLLDEP 190
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3841-4026 |
5.67e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 62.43 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3841 LLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQDVLLDNlTVREHLMLFasikapwwttke 3919
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQDPTLFSG-TIRSNLDPF------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3920 lqqqvNKTLDEVELTQHQHKPAGV-LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFT 3998
Cdd:cd03369 106 -----DEYSDEEIYGALRVSEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTI 180
|
170 180
....*....|....*....|....*...
gi 116292744 3999 THHLdEAEMLSDHVAVLQQGRLRCYAPP 4026
Cdd:cd03369 181 AHRL-RTIIDYDKILVMDAGEVKEYDHP 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3821-4019 |
6.36e-10 |
|
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: 65.48 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFpPTSGTITINGKNLQT----DLSKVREELgvcpqQDVLLD 3896
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGlsrrALRPLRRRM-----QVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3897 -------NLTVREHL---MLfasIKAPWWTTKELQQQVNKTLDEVELT-QHQHKPAGVLSGGMKRKLSIGIAfMGMS-KT 3964
Cdd:COG4172 371 pfgslspRMTVGQIIaegLR---VHGPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARA-LILEpKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3965 VVLDEPSSGVDpcsrRS----LWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:COG4172 447 LVLDEPTSALD----VSvqaqILDLLrdLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
4713-4917 |
7.03e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4713 HGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVDlasAGKAGILIGYCPQQDALDELLTGWE 4792
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPID---AKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4793 HLQYYCRLR---GIPKQYIPEVAADLVRRLHLESHVD------KPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:TIGR00955 119 HLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4864 PCSKRYLWQTITQEVRDGCAAVLTSH--SMEECEaLCTRLAIMVDGSFRCLGPPQH 4917
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQ 253
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3820-4041 |
7.25e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3820 EDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPP----TSGTITINGKNLQtdLSKVREELGVcpqqdVLL 3895
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA--PCALRGRKIA-----TIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3896 DN--------LTVREHlmlfasikapwwtTKELQQQVNKTLDEVELTQHQH-----KPAGVL-------SGGMKRKLSIG 3955
Cdd:PRK10418 86 QNprsafnplHTMHTH-------------ARETCLALGKPADDATLTAALEavgleNAARVLklypfemSGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3956 IAFMGMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETY 4033
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
....*...
gi 116292744 4034 GQGLTLTL 4041
Cdd:PRK10418 233 KHAVTRSL 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3822-4021 |
8.46e-10 |
|
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: 64.85 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPT-SGTITINGK--NLQTDLSKVREELGVCPQ---QDVLL 3895
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3896 DNLTVREHLMLfASIKApwWTTKEL------QQQVNKTLDEVEL-TQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:TIGR02633 352 PILGVGKNITL-SVLKS--FCFKMRidaaaeLQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3969 EPSSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4705-4918 |
1.29e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4705 FGGKTTaVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVirtpQGDMV-----------DLASAGKAGI 4773
Cdd:PRK14271 31 FAGKTV-LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRY----SGDVLlggrsifnyrdVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 LIGYcPQ---QDALDELLTGWEHLQYYCR--LRGIPKQYIPEVAA-DLVR-RLHleshvDKPVaTYSGGTRRKLSTALAL 4846
Cdd:PRK14271 106 LFQR-PNpfpMSIMDNVLAGVRAHKLVPRkeFRGVAQARLTEVGLwDAVKdRLS-----DSPF-RLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4847 VGKPDILLLDEPSSGMDPCSKRYLWQTItQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFI-RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4707-4918 |
1.70e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPQgdMVDLAS---AGKAGILI--GYCPQQ 4781
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH--IQHYASkevARRIGLLAqnATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4782 DALDELLT--GWEHLQYYCRLRgipkQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPS 4859
Cdd:PRK10253 96 ITVQELVArgRYPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 4860 SGMDPCSKRYLWQTITQEVRD---GCAAVLtsHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREkgyTLAAVL--HDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3814-4020 |
1.85e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.69 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTI-----TING----KNLQTDLSKVREE 3884
Cdd:PRK11264 8 NLVKKFHGQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarslSQQKGLIRQLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3885 LGVCPQQDVLLDNLTVREHLmlfasIKAPWWTTKELQQQV----NKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAfMG 3960
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENI-----IEGPVIVKGEPKEEAtaraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARA-LA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3961 MSKTVVL-DEPSSGVDPcsrRSLWDILLKYR----EGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11264 161 MRPEVILfDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4710-4918 |
1.91e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4710 TAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVI-RTPQGDMVDLASAGKagilIGYCPQQDALDELL 4788
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdAQPLESWSSKAFARK----VAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4789 TGWEHL---QY-----YCRLRGIPKQYIPEvAADLVrrlHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSS 4860
Cdd:PRK10575 101 TVRELVaigRYpwhgaLGRFGAADREKVEE-AISLV---GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 4861 GMDPCSK---RYLWQTITQEVRDGCAAVLtsHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK10575 177 ALDIAHQvdvLALVHRLSQERGLTVIAVL--HDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3831-3976 |
2.80e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.63 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3831 LTFHRDQITALL--GTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQqdvLLDNLTVREHLMLF 3907
Cdd:PRK13543 30 LDFHVDAGEALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLPG---LKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3908 ASIKApwwttKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDP 3976
Cdd:PRK13543 107 CGLHG-----RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4696-4907 |
3.10e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYR--SVFG--GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytVIRTPQGDMVDLASAGKA 4771
Cdd:PRK10419 8 GLSHHYAhgGLSGkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG--NVSWRGEPLAKLNRAQRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 GI-----LIGycpqQDALDEL----LTGW---EHLQYYCRLRGIPKQyipEVAADLVRRLHL-ESHVDKPVATYSGGTRR 4838
Cdd:PRK10419 86 AFrrdiqMVF----QDSISAVnprkTVREiirEPLRHLLSLDKAERL---ARASEMLRAVDLdDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4839 KLSTALALVGKPDILLLDEPSSGMDpcskRYLWQTITQEVRD-----GCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLD----LVLQAGVIRLLKKlqqqfGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3821-4018 |
3.17e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFpPTSGTITINGKNLQT----DLSKVREELGVCPQ--QDVL 3894
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNlnrrQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVREHLMLFASIKAPWWTTKELQQQVNKTLDEVEL---TQHQHkPAGvLSGGMKRKLSIGIAFMGMSKTVVLDEPS 3971
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLdpeTRHRY-PAE-FSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 116292744 3972 SGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQG 4018
Cdd:PRK15134 454 SSLDKTVQAQILALLksLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3830-4020 |
5.04e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3830 TLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSK--VREELGVCPQ---QDVLL------DNL 3898
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaIRAGIMLCPEdrkAEGIIpvhsvaDNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3899 TV--REHLMLFASIKAPWWTTKELQQQVNKtldeveL---TQHQHKPAGVLSGGMKRK------LSIGIafmgmsKTVVL 3967
Cdd:PRK11288 353 NIsaRRHHLRAGCLINNRWEAENADRFIRS------LnikTPSREQLIMNLSGGNQQKailgrwLSEDM------KVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3968 DEPSSGVDPCSRRSLWDILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3822-4020 |
6.31e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQQDVLLDNlTV 3900
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKLQLDSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 REHLMLfasiKAPWWTTKELQQQV---NKTLDEVELTQHQHKPAG----VLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:PRK10789 406 ANNIAL----GRPDATQQEIEHVArlaSVHDDILRLPQGYDTEVGergvMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 116292744 3974 VDPCSRRSLWDILLKYREGRTIIFTTHHLdEAEMLSDHVAVLQQGRL 4020
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHI 527
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3814-4000 |
6.48e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKVaVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTItingknlqtdlsKVRE--ELGVCPQ- 3890
Cdd:PRK15064 324 NLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSEnaNIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 -QDVLLDNLTVREHLmlfasikAPWWTTKELQQQVNKTLDEVELTQHQ-HKPAGVLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:PRK15064 391 hAYDFENDLTLFDWM-------SQWRQEGDDEQAVRGTLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190
....*....|....*....|....*....|..
gi 116292744 3969 EPSSGVDPCSRRSLWDILLKYrEGrTIIFTTH 4000
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKY-EG-TLIFVSH 493
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3815-4023 |
6.58e-09 |
|
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: 60.64 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQE-LTLTFHRDQITALLGTNGAGKTTIISMLMGLFPpTSGTITINGKNLQT-DLSKVREELGVCPQQd 3892
Cdd:cd03289 8 LTAKYTEGGNAVLEnISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGVIPQK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3893 VLLDNLTVREHLMLFASikapwWTTKELQqqvnKTLDEVELTQHQHKPAG-----------VLSGGMKRKLSIGIAFMGM 3961
Cdd:cd03289 86 VFIFSGTFRKNLDPYGK-----WSDEEIW----KVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3962 SKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLdEAEMLSDHVAVLQQGRLRCY 4023
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQY 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4716-4916 |
6.87e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.60 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4716 SLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVI------RTPqgdmvdlASAGKAGILIgycpQQDALDELLT 4789
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLngqdhtTTP-------PSRRPVSMLF----QENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4790 GWEH----LQYYCRLRGIPKQYIPEVAadlvRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPC 4865
Cdd:PRK10771 88 VAQNiglgLNPGLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4866 skryLWQTITQEVRDGCAA-----VLTSHSMEECEALCTRLAIMVDGSFRCLGPPQ 4916
Cdd:PRK10771 164 ----LRQEMLTLVSQVCQErqltlLMVSHSLEDAARIAPRSLVVADGRIAWDGPTD 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4707-4863 |
7.25e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytvirtpqgdMVDLASagkaGILIGYCPQQDaLDE 4786
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG----------EIGLAK----GIKLGYFAQHQ-LEF 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 4787 LLTGWEHLQYYCRLrgIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK10636 388 LRADESPLQHLARL--APQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4696-4863 |
7.63e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSyrsvFGGKTTaVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqGDMVDLAsagkagili 4775
Cdd:PRK11819 329 NLSKS----FGDRLL-IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI----GETVKLA--------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 gYCPQQ-DALDELLTGWE-------HLQY---------YC---RLRGIPKQyipevaadlvrrlhleshvdKPVATYSGG 4835
Cdd:PRK11819 391 -YVDQSrDALDPNKTVWEeisggldIIKVgnreipsraYVgrfNFKGGDQQ--------------------KKVGVLSGG 449
|
170 180
....*....|....*....|....*...
gi 116292744 4836 TRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4691-4896 |
9.72e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 58.65 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSksyrsVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPP---SSGYTVIRtpQGDMVDLAS 4767
Cdd:COG4136 1 MLSLENLT-----ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLN--GRRLTALPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4768 AGKAgilIGYCPQQDALDELLTGWEHLQYYCRlRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALV 4847
Cdd:COG4136 74 EQRR---IGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4848 GKPDILLLDEPSSGMDPcskrylwqTITQEVRD---------GCAAVLTSHSMEECEA 4896
Cdd:COG4136 150 AEPRALLLDEPFSKLDA--------ALRAQFREfvfeqirqrGIPALLVTHDEEDAPA 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4707-4907 |
1.55e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqGDMVDLASAG---KAGIliGYCP---Q 4780
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD---GEDITGLSPRerrRLGV--AYIPedrL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4781 QDAL-------DELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLE-SHVDKPVATYSGGTRRKLSTALALVGKPDI 4852
Cdd:COG3845 344 GRGLvpdmsvaENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRtPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4853 LLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4715-4907 |
1.56e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.61 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQG-DMVDLASAGKagiligycP-----QQDALDELL 4788
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW---NGqDLTALPPAER--------PvsmlfQENNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4789 TGWEH----LQYYCRLRGIPKQYIPEVAAdlvrRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDP 4864
Cdd:COG3840 87 TVAQNiglgLRPGLKLTAEQRAQVEQALE----RVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 116292744 4865 CskryLWQTITQEVRDGCAA-----VLTSHSMEECEALCTRLAIMVDG 4907
Cdd:COG3840 163 A----LRQEMLDLVDELCRErgltvLMVTHDPEDAARIADRVLLVADG 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4716-4863 |
1.64e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.95 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4716 SLGIPR-GECFGLLGVNGAGKSTTFKILNGE---------TPPS--------SG-----Y---------TVIRTPQgdMV 4763
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILSGElkpnlgdydEEPSwdevlkrfRGtelqdYfkklangeiKVAHKPQ--YV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4764 DLASA---GKAGILIgycpqqDALDElltgwehlqyycrlRGipkqyipeVAADLVRRLHLESHVDKPVATYSGGTRRKL 4840
Cdd:COG1245 170 DLIPKvfkGTVRELL------EKVDE--------------RG--------KLDELAEKLGLENILDRDISELSGGELQRV 221
|
170 180
....*....|....*....|...
gi 116292744 4841 STALALVGKPDILLLDEPSSGMD 4863
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4715-4889 |
1.73e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLASAGKAGILIGYcpqQDALDELLTGWEHL 4794
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG-EILFERQSIKKDLCTYQKQLCFVGH---RSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4795 QYYCRLRGIPKQyipevAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTI 4874
Cdd:PRK13540 96 LYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170
....*....|....*
gi 116292744 4875 TQEVRDGCAAVLTSH 4889
Cdd:PRK13540 171 QEHRAKGGAVLLTSH 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4712-4917 |
1.74e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSsgytvIRTPQG----DMVDLASAGKAGILIGYCPQ--QDALD 4785
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAG-----VRQTAGrvllDGKPVAPCALRGRKIATIMQnpRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4786 ELLTGWEHLQYYCRLRGIPK------QYIPEVAADLVRRLhLESHvdkPVATySGGTRRKLSTALALVGKPDILLLDEPS 4859
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPAddatltAALEAVGLENAARV-LKLY---PFEM-SGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4860 SGMDPCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGP-------PQH 4917
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDvetlfnaPKH 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3817-4003 |
2.08e-08 |
|
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: 61.08 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3817 KEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFpPTSGTITINGKNLQT-DLSKVREELGVCPQQdVLL 3895
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGVIPQK-VFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3896 DNLTVREHLMLFASikapwWTTKELQqqvnKTLDEVELTQHQHKPAG-----------VLSGGMKRKLSIGIAFMGMSKT 3964
Cdd:TIGR01271 1304 FSGTFRKNLDPYEQ-----WSDEEIW----KVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190
....*....|....*....|....*....|....*....
gi 116292744 3965 VVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLD 4003
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4711-4918 |
2.41e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.88 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGY-----TVIrTPQGDMVDLAS-AGKAGILIGYcPQQDAL 4784
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTvtigeRVI-TAGKKNKKLKPlRKKVGIVFQF-PEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4785 DEllTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHL-ESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK13634 100 EE--TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4864 PCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
4727-4914 |
2.69e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4727 LLGVNGAGKSTTFKILNGETPPSSGYTVI--RTpqgdMVDLASagkaGIL-------IGYCPQQDALdelltgWEH---- 4793
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLngRV----LFDAEK----GIClppekrrIGYVFQDARL------FPHykvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4794 --LQYYCrlrgipKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKR--- 4868
Cdd:PRK11144 95 gnLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRell 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 116292744 4869 -YLwQTITQEVRdgCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGP 4914
Cdd:PRK11144 169 pYL-ERLAREIN--IPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4716-4863 |
4.12e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4716 SLGIPR-GECFGLLGVNGAGKSTTFKILNGETPPSSG----------------------Y---------TVIRTPQgdMV 4763
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtelqnYfkklyngeiKVVHKPQ--YV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4764 DLASA---GKAGILIgycpqqDALDElltgwehlqyycrlRGipkqyipeVAADLVRRLHLESHVDKPVATYSGGTRRKL 4840
Cdd:PRK13409 170 DLIPKvfkGKVRELL------KKVDE--------------RG--------KLDEVVERLGLENILDRDISELSGGELQRV 221
|
170 180
....*....|....*....|...
gi 116292744 4841 STALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLD 244
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4691-4858 |
4.95e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.40 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4691 MMVLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSG------YTVIRTPQGDMvd 4764
Cdd:COG4604 1 MIEIKNVSKRY-----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGevlvdgLDVATTPSREL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4765 lasAGKAGILigycPQQDALDELLT-------G-WEHLQyyCRLRGIPKQYIPEVaadlVRRLHLESHVDKPVATYSGGT 4836
Cdd:COG4604 74 ---AKRLAIL----RQENHINSRLTvrelvafGrFPYSK--GRLTAEDREIIDEA----IAYLDLEDLADRYLDELSGGQ 140
|
170 180
....*....|....*....|..
gi 116292744 4837 RRKLSTALALVGKPDILLLDEP 4858
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEP 162
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4715-4863 |
5.13e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLAsagkagiligycpqQDALDELLTGWEHL 4794
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG-TVFRSAKVRMAVFS--------------QHHVDGLDLSSNPL 592
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4795 QYYCR-LRGIPKQYIpevaadlvrRLHLESH------VDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PLN03073 593 LYMMRcFPGVPEQKL---------RAHLGSFgvtgnlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3815-3989 |
5.69e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITInGKNLQtdLSKVREelgvcpQQDVL 3894
Cdd:TIGR03719 328 LTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK--LAYVDQ------SRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVrehlmlfasikapWwttkelqQQVNKTLDEVELTQH-----------------QHKPAGVLSGGMKRKLSIGIA 3957
Cdd:TIGR03719 398 DPNKTV-------------W-------EEISGGLDIIKLGKReipsrayvgrfnfkgsdQQKKVGQLSGGERNRVHLAKT 457
|
170 180 190
....*....|....*....|....*....|..
gi 116292744 3958 FMGMSKTVVLDEPSSGVDPCSRRSLWDILLKY 3989
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNF 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3822-4021 |
5.87e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFP-PTSGTITINGKNLQTD------------LSKVREELGVC 3888
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRnpqqaiaqgiamVPEDRKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PQQDVLlDNLT--VREHLMLFASIKAPwwttKElQQQVNKTLDEVEL-TQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTV 3965
Cdd:PRK13549 354 PVMGVG-KNITlaALDRFTGGSRIDDA----AE-LKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3966 VLDEPSSGVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRLR 4021
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4711-4909 |
7.65e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLA---SAGKAGILIGYcpQQDALDEL 4787
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY---LGKEVTFNgpkSSQEAGIGIIH--QELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4788 LTGWEHL----QYYCRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK10762 94 LTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 116292744 4864 PCSKRYLWQTItQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSF 4909
Cdd:PRK10762 174 DTETESLFRVI-RELKSqGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4706-4889 |
8.57e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 58.64 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4706 GGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTV------IRTpqgdmVDLASAGKAgilIGYCP 4779
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG-RIlidgvdIRD-----LTLESLRRQ---IGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4780 qQDALdeLLTG--WEHLQYycrlrGIPKQYIPEV--------AADLVRRLH--LESHVDKPVATYSGGTRRKLSTALALV 4847
Cdd:COG1132 421 -QDTF--LFSGtiRENIRY-----GRPDATDEEVeeaakaaqAHEFIEALPdgYDTVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 116292744 4848 GKPDILLLDEPSSGMDPCSKRYLWQTItQEVRDGCAAVLTSH 4889
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEAL-ERLMKGRTTIVIAH 533
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4703-4864 |
9.18e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.58 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4703 SVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNgetppssgytviRtpqgdMVDLASAGKA-G-ILIG---- 4776
Cdd:COG1117 18 NVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLN------------R-----MNDLIPGARVeGeILLDgedi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4777 YCPQQDaLDEL---------------LTGWEHLQYYCRLRGI-PKQYIPEVAADLVRRLHLESHV----DKPVATYSGGT 4836
Cdd:COG1117 81 YDPDVD-VVELrrrvgmvfqkpnpfpKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDEVkdrlKKSALGLSGGQ 159
|
170 180
....*....|....*....|....*...
gi 116292744 4837 RRKLSTALALVGKPDILLLDEPSSGMDP 4864
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3820-4034 |
9.63e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3820 EDHKVAVQELTLTFHRDQITALLGTNGAGKTtiiSMLMGLF---PPTSGTITINGKNL-QTDLSKVREELGVCPQQDVLL 3895
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKS---SLTLGLFrinESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3896 DNlTVREHLMLFA--SIKAPWWTTK--ELQQQVNKTLDEVEltqHQHKPAGV-LSGGMKRKLSIGIAFMGMSKTVVLDEP 3970
Cdd:TIGR00957 1373 SG-SLRMNLDPFSqySDEEVWWALElaHLKTFVSALPDKLD---HECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3971 SSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAeMLSDHVAVLQQGRLRCYAPPADLKETYG 4034
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI-MDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3814-4019 |
9.90e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYeDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKN-LQTDLSK---------VRE 3883
Cdd:PRK11701 11 GLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYAlseaerrrlLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3884 ELGVCPQ--QDVLLDNLT----VREHLMlfasiKAPWWTTKELQQQVNKTLDEVELTQHQ--HKPAgVLSGGMKRKLSIG 3955
Cdd:PRK11701 90 EWGFVHQhpRDGLRMQVSaggnIGERLM-----AVGARHYGDIRATAGDWLERVEIDAARidDLPT-TFSGGMQQRLQIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3956 IAFMGMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4712-4910 |
9.91e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTV--------IRTPQgdmvdlaSAGKAGILI-------- 4775
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIfidgkpvkIRNPQ-------QAIAQGIAMvpedrkrd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQQD--------ALDELlTGWEHLQYYCRLRGIPKQyipevaadlVRRLHLE-SHVDKPVATYSGGTRRKLSTALAL 4846
Cdd:PRK13549 351 GIVPVMGvgknitlaALDRF-TGGSRIDDAAELKTILES---------IQRLKVKtASPELAIARLSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4847 VGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFR 4910
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4696-4863 |
1.11e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSY--RSVFggkttavHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytvirtpqgdMVDLASAGKagi 4773
Cdd:PRK15064 324 NLTKGFdnGPLF-------KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSENAN--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4774 lIGYCPQQDA----LDELLTGWEHlQYycrlrGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGGTR-RKLSTALALvG 4848
Cdd:PRK15064 384 -IGYYAQDHAydfeNDLTLFDWMS-QW-----RQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKgRMLFGKLMM-Q 455
|
170
....*....|....*
gi 116292744 4849 KPDILLLDEPSSGMD 4863
Cdd:PRK15064 456 KPNVLVMDEPTNHMD 470
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3815-4021 |
1.29e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGVCPQQDV- 3893
Cdd:PRK10522 328 VTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFh 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3894 LLDNLTVREHLMLFASIKAPWWTTKELQQQVnkTLDEVELTQHQhkpagvLSGGMKRKLSIGIAFMGMSKTVVLDEPSSG 3973
Cdd:PRK10522 408 LFDQLLGPEGKPANPALVEKWLERLKMAHKL--ELEDGRISNLK------LSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 116292744 3974 VDPCSRRSLWDILLKY-RE-GRTIIFTTHHlDEAEMLSDHVAVLQQGRLR 4021
Cdd:PRK10522 480 QDPHFRREFYQVLLPLlQEmGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3823-4032 |
1.40e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3823 KVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITingknlqtdlskVREELGVCPQQDVLLdNLTVRE 3902
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------------AERSIAYVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3903 HLMLFASIKApwwttKELQQQVNKTLDEVELTQhqhKPAGV----------LSGGMKRKLSIGIAFMGMSKTVVLDEPSS 3972
Cdd:PTZ00243 740 NILFFDEEDA-----ARLADAVRVSQLEADLAQ---LGGGLeteigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3973 GVDP-CSRRSLWDILLKYREGRTIIFTTHHLDEAEmLSDHVAVLQQGRLRCYAPPADLKET 4032
Cdd:PTZ00243 812 ALDAhVGERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRT 871
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3825-4037 |
1.80e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.59 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGknlQTDLSKVREELGvcpQQDVLLDNLTVREHL 3904
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---SAALIAISSGLN---GQLTGIENIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3905 MLFasikapwwTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWD 3984
Cdd:PRK13545 113 MGL--------TKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3985 ILLKYRE-GRTIIFTTHHLDEAEMLSDHVAVLQQGRLRCYAPPADLKETYGQGL 4037
Cdd:PRK13545 185 KMNEFKEqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFL 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3815-4067 |
1.95e-07 |
|
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: 57.50 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGL--FPPTSGTITIN----GKNLQTDL-SKVREELGV 3887
Cdd:TIGR03269 6 LTKKFDG-KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcEKCGYVERpSKVGEPCPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3888 CPQQ------------DVLLDNLTVREHLML---FA----------SIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAG 3942
Cdd:TIGR03269 85 CGGTlepeevdfwnlsDKLRRRIRKRIAIMLqrtFAlygddtvldnVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3943 V---LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLK--YREGRTIIFTTHHLDEAEMLSDHVAVLQQ 4017
Cdd:TIGR03269 165 IardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 116292744 4018 GRLRCYAPPADLKETYGQGLTLTlsKQPSILETQEPkdVARVTSLIQIYI 4067
Cdd:TIGR03269 245 GEIKEEGTPDEVVAVFMEGVSEV--EKECEVEVGEP--IIKVRNVSKRYI 290
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3826-4020 |
2.26e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3826 VQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL--QTDLSKVREELGVCPQ---QDVLLDNLTV 3900
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 REHLMLFASIKAPWW-------TTKELQQQVNKTLDEVELTQHQ-HKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSS 3972
Cdd:PRK09700 359 AQNMAISRSLKDGGYkgamglfHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 116292744 3973 GVDPCSRRSLWDILLKY-REGRTIIFTTHHLDEAEMLSDHVAVLQQGRL 4020
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3825-4034 |
2.64e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQT-DLSKVREELGVCPQQdVLLDNLTV--- 3900
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQN-VHLFNDTIann 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 ----------RE---------HLMLFASikapwwttkELQQQVNKTLDEveltqhqhkpAGV-LSGGMKRKLSIGIAFMG 3960
Cdd:PRK11176 437 iayarteqysREqieeaarmaYAMDFIN---------KMDNGLDTVIGE----------NGVlLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3961 MSKTVVLDEPSSGVDPCSRRSLWDILLKYREGRTIIFTTHHLDEAEMlSDHVAVLQQGRLRCYAPPADLKETYG 4034
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
4727-4889 |
4.10e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4727 LLGVNGAGKSTTFKILNGETppSSGYTvirtpQGDmVDLASAGKA----GILIGYCPQQDALDELLTGWEHLQYYCRLRg 4802
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRK--TGGYI-----EGD-IRISGFPKKqetfARISGYCEQNDIHSPQVTVRESLIYSAFLR- 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4803 IPKQ--------YIPEVAaDLVRRLHL-ESHVDKP-VATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQ 4872
Cdd:PLN03140 982 LPKEvskeekmmFVDEVM-ELVELDNLkDAIVGLPgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1060
|
170
....*....|....*..
gi 116292744 4873 TITQEVRDGCAAVLTSH 4889
Cdd:PLN03140 1061 TVRNTVDTGRTVVCTIH 1077
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3821-4029 |
5.20e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPT--------SGTITINGKNL-QTDLSKVREELGVCPQQ 3891
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLaAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3892 DVLLDNLTVREHLML--FASIKAPWWTTKELQQQVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGM-------- 3961
Cdd:PRK13547 92 AQPAFAFSAREIVLLgrYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292744 3962 -SKTVVLDEPSSGVDPCSRRSLWDILLKY-REGRTIIFT-THHLDEAEMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PRK13547 172 pPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4694-4926 |
5.47e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.42 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4694 LCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqGD--MVDLASAGKA 4771
Cdd:PRK11000 6 LRNVTKAY-----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI----GEkrMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4772 gilIGYCPQQDALDELLTGWEHLQYYCRLRGIPKQYIP---EVAADLVRRLHLESHvdKPVAtYSGGTRRKLSTALALVG 4848
Cdd:PRK11000 77 ---VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINqrvNQVAEVLQLAHLLDR--KPKA-LSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4849 KPDILLLDEPSSGMDPCSKRYLWQTITQ-EVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI----KNRFG 4923
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRlHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFV 230
|
...
gi 116292744 4924 DGY 4926
Cdd:PRK11000 231 AGF 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4688-4918 |
6.63e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.86 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4688 GGDMMVLCNLSKSYRSVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRtpqgDMVDLAS 4767
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG----DIYIGDK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4768 AGKAGILIGYCPQQdaldelltgwehLQYYCRLR------------------------------GIPKQYIPEVAADLVR 4817
Cdd:PRK13631 94 KNNHELITNPYSKK------------IKNFKELRrrvsmvfqfpeyqlfkdtiekdimfgpvalGVKKSEAKKLAKFYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4818 RLHL-ESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEA 4896
Cdd:PRK13631 162 KMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLE 241
|
250 260
....*....|....*....|..
gi 116292744 4897 LCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK13631 242 VADEVIVMDKGKILKTGTPYEI 263
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4708-4863 |
7.52e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4708 KTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPS---------SGYTV---IRTPQGDMVdlasagkagili 4775
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvegdihyNGIPYkefAEKYPGEII------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 gYCPQQDALDELLTGWEHLQYYCRLRGipkqyipevaADLVRRLhleshvdkpvatySGGTRRKLSTALALVGKPDILLL 4855
Cdd:cd03233 87 -YVSEEDVHFPTLTVRETLDFALRCKG----------NEFVRGI-------------SGGERKRVSIAEALVSRASVLCW 142
|
....*...
gi 116292744 4856 DEPSSGMD 4863
Cdd:cd03233 143 DNSTRGLD 150
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4707-4918 |
1.02e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.38 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4707 GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNG-----ETPPSSGYTVIRTPQGDMVDLASAGKAGILIGYCPQQ 4781
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4782 DALdelLTGWEHLQYYCRLRGIPKQyipevAADLVRRL-----------HLESHVDKPVATYSGGTRRKLSTALALVGKP 4850
Cdd:PRK14247 94 IPN---LSIFENVALGLKLNRLVKS-----KKELQERVrwalekaqlwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4851 DILLLDEPSSGMDPCSKRYLwQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4705-4863 |
1.21e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.97 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4705 FGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpqgDMVDLASAGKAG------------ 4772
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-----DGTDIRTVTRASlrrniavvfqda 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4773 ----------ILIGycpQQDALD-ELLTGWEHLQyycrlrgipkqyipevAADLVRR--LHLESHVDKPVATYSGGTRRK 4839
Cdd:PRK13657 419 glfnrsiednIRVG---RPDATDeEMRAAAERAQ----------------AHDFIERkpDGYDTVVGERGRQLSGGERQR 479
|
170 180
....*....|....*....|....
gi 116292744 4840 LSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALD 503
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4712-4880 |
1.21e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.81 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGEcfGLL--GVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLasagkagiligycPQ-----QDAL 4784
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSG-RIARPAGARVLFL-------------PQrpylpLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4785 DELLTgwehlqYYCRLRGIPKQYIPEVA-----ADLVRRLHLESHVDKpvaTYSGGTRRKLSTALALVGKPDILLLDEPS 4859
Cdd:COG4178 443 REALL------YPATAEAFSDAELREALeavglGHLAERLDEEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180
....*....|....*....|.
gi 116292744 4860 SGMDPCSKRYLWQTITQEVRD 4880
Cdd:COG4178 514 SALDEENEAALYQLLREELPG 534
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4716-4918 |
1.41e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4716 SLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYtviRTPQGDMVDLASAGKAGILIGYCPQQDALDELLTGWEHLQ 4795
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---RQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4796 YYCR---LRGIPKqyiPEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQ 4872
Cdd:PRK10938 100 RTTAeiiQDEVKD---PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116292744 4873 TITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGPPQHI 4918
Cdd:PRK10938 177 LLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3797-4021 |
1.55e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3797 QNGPGEmeggnPGVALISVTKEY-----EDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITIng 3871
Cdd:PLN03232 604 QNPPLQ-----PGAPAISIKNGYfswdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3872 knlqtdlskVREELGVCPQQDVLLdNLTVREHLmLFASIKAP--WWTTKE---LQQQVNkTLDEVELTQHQHKpaGV-LS 3945
Cdd:PLN03232 677 ---------IRGSVAYVPQVSWIF-NATVRENI-LFGSDFESerYWRAIDvtaLQHDLD-LLPGRDLTEIGER--GVnIS 742
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3946 GGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILLKYR-EGRTIIFTTHHLDEAEMLsDHVAVLQQGRLR 4021
Cdd:PLN03232 743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3815-3989 |
1.94e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3815 VTKEYEDhKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITInGKNLQtdLSKVREelgvcpQQDVL 3894
Cdd:PRK11819 330 LSKSFGD-RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK--LAYVDQ------SRDAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNLTVrehlmlfasikapWwttkelqQQVNKTLDEVELTQH-----------------QHKPAGVLSGGMKRKLSigia 3957
Cdd:PRK11819 400 DPNKTV-------------W-------EEISGGLDIIKVGNReipsrayvgrfnfkggdQQKKVGVLSGGERNRLH---- 455
|
170 180 190
....*....|....*....|....*....|....*....
gi 116292744 3958 fmgMSKTV-------VLDEPSSGVDPCSRRSLWDILLKY 3989
Cdd:PRK11819 456 ---LAKTLkqggnvlLLDEPTNDLDVETLRALEEALLEF 491
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4696-4908 |
2.77e-06 |
|
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: 51.32 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSG-YTVIRTpqgdmvdlasagkagil 4774
Cdd:cd03250 5 DASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGsVSVPGS----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4775 IGYCPQQDAL------DELLTGWEHLQYycRLRgipkqyipEV--AADLVRRLHLESHVDKPV-----ATYSGGTRRKLS 4841
Cdd:cd03250 68 IAYVSQEPWIqngtirENILFGKPFDEE--RYE--------KVikACALEPDLEILPDGDLTEigekgINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4842 TALALVGKPDILLLDEPSSGMDPCSKRYLWQT-ITQEVRDGCAAVLTSHSMEECEAlCTRLAIMVDGS 4908
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4711-4921 |
2.79e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.71 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4711 AVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGIL---IGYCPQQD--ALD 4785
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF---NGQRIDTLSPGKLQALrrdIQFIFQDPyaSLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4786 ELLTGWEHLQYYCRLRGI-PKQYIPEVAADLVRRLHLE-SHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 4864 PCSKRYLWQTITQEVRD-GCAAVLTSHSMEECEALCTRLAIMVDGSFRCLGP-------PQHIKNR 4921
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPrravfenPQHPYTR 561
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4696-4893 |
3.72e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.96 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSvfggkTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVirtpQGDM-----------VD 4764
Cdd:PRK14258 12 NLSFYYDT-----QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRV----EGRVeffnqniyerrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4765 LASAGKAGILIGycPQQDALDelLTGWEHLQYYCRLRGI-PKQYIPEVAADLVRRLHL----ESHVDKPVATYSGGTRRK 4839
Cdd:PRK14258 83 LNRLRRQVSMVH--PKPNLFP--MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4840 LSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTI-TQEVRDGCAAVLTSHSMEE 4893
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqSLRLRSELTMVIVSHNLHQ 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
4710-4889 |
3.73e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4710 TAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPpSSGYTvirtpqGDMvdLASAGKAG--IL--IGYCPQQDALD 4785
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ-GNNFT------GTI--LANNRKPTkqILkrTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4786 ELLTGWEHLqYYCRLRGIP----KQYIPEVAADLVRRLHLESHVDKPVAT-----YSGGTRRKLSTALALVGKPDILLLD 4856
Cdd:PLN03211 153 PHLTVRETL-VFCSLLRLPksltKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|...
gi 116292744 4857 EPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSH 4889
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
3822-4008 |
4.34e-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: 50.05 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3822 HKVAVQELTLTFHRDQITALLGTNGAGKTTII-SMLMGLFpptsgtitinGKNLQTDLSKVreelgvcpqqdvlldnltv 3900
Cdd:cd03227 7 FPSYFVPNDVTFGEGSLTIITGPNGSGKSTILdAIGLALG----------GAQSATRRRSG------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 rehlmlfasikapwwttkeLQQQVNKTLDEVELTQHQHKpagvLSGGMKRKLSIGIAFMGMSK----TVVLDEPSSGVDP 3976
Cdd:cd03227 58 -------------------VKAGCIVAAVSAELIFTRLQ----LSGGEKELSALALILALASLkprpLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|...
gi 116292744 3977 CSRRSLWDILLKYR-EGRTIIFTTHHLDEAEML 4008
Cdd:cd03227 115 RDGQALAEAILEHLvKGAQVIVITHLPELAELA 147
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4696-4907 |
4.62e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVfggktTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKA---G 4772
Cdd:PRK10982 3 NISKSFPGV-----KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF---QGKEIDFKSSKEAlenG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4773 IL-----IGYCPQQDALDEL------LTGW--EHLQYYCRLRGIPKQyipevaadlvrrlhLESHVD--KPVATYSGGTR 4837
Cdd:PRK10982 75 ISmvhqeLNLVLQRSVMDNMwlgrypTKGMfvDQDKMYRDTKAIFDE--------------LDIDIDprAKVATLSVSQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4838 RKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK10982 141 QMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4703-4893 |
4.69e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.71 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4703 SVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTV----------IRTPQGDMVDLASAgkag 4772
Cdd:PRK14243 17 NVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVegkvtfhgknLYAPDVDPVEVRRR---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4773 ilIGYCPQQ-DALDELLtgWEHLQYYCRLRGIpKQYIPEVAADLVRRLHLESHV-DK---PVATYSGGTRRKLSTALALV 4847
Cdd:PRK14243 93 --IGMVFQKpNPFPKSI--YDNIAYGARINGY-KGDMDELVERSLRQAALWDEVkDKlkqSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116292744 4848 GKPDILLLDEPSSGMDPCSKRYLWQTItQEVRDGCAAVLTSHSMEE 4893
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELM-HELKEQYTIIIVTHNMQQ 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3825-4019 |
4.95e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3825 AVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL----QTDLSKVREELgvcpqQDVLLDNLTV 3900
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDI-----QMIFQDPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3901 REHLMLFASIKA-------PWWTTKELQQQVNKTLDEVEL-----TQHQHKpagvLSGGMKRKLSIGIAFMGMSKTVVLD 3968
Cdd:PRK15079 111 LNPRMTIGEIIAeplrtyhPKLSRQEVKDRVKAMMLKVGLlpnliNRYPHE----FSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 116292744 3969 EPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLqqLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4696-4864 |
6.03e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLASAGKAGILI 4775
Cdd:PRK13651 7 NIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG-TIEWIFKDEKNKKKTKEKEKVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 GYCPQ---------------------QDALDELL--TGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHL-ESHVDKPVAT 4831
Cdd:PRK13651 86 KLVIQktrfkkikkikeirrrvgvvfQFAEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFE 165
|
170 180 190
....*....|....*....|....*....|...
gi 116292744 4832 YSGGTRRKLSTALALVGKPDILLLDEPSSGMDP 4864
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
4714-4889 |
6.46e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.99 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4714 GISLGIPRGECFGLLGVNGAGKSTTFKILNGETpPSSGytVIRTPQGDMVDLaSAGKAGILIGYCPQQDALDELLTGWEH 4793
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQG--EILLNGRPLSDW-SAAELARHRAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4794 LQYYcRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGG--TRRKLSTALALVgKPDI------LLLDEPSSGMDPC 4865
Cdd:COG4138 90 LALH-QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGewQRVRLAAVLLQV-WPTInpegqlLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....
gi 116292744 4866 SKRYLWQTITQEVRDGCAAVLTSH 4889
Cdd:COG4138 168 QQAALDRLLRELCQQGITVVMSSH 191
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
4715-4889 |
8.19e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPpSSGYTVIrtpQGDMVDLASAGKAGILIGYCPQQDALDELLTGWEHL 4794
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQF---AGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4795 QYYcRLRGIPKQYIPEVAADLVRRLHLESHVDKPVATYSGG--TRRKLSTALALVgKPDI------LLLDEPSSGMDPCS 4866
Cdd:PRK03695 91 TLH-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQV-WPDInpagqlLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|...
gi 116292744 4867 KRYLWQTITQEVRDGCAAVLTSH 4889
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSH 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4687-4908 |
8.23e-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: 52.61 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4687 TGGDMMVLcNLSKSYRSvfGGKTTaVHGISLGIPRGECFGLLGVNGAGKSTTF----KILNGEtppssGYTVIRTPQGDM 4762
Cdd:TIGR01271 1214 SGGQMDVQ-GLTAKYTE--AGRAV-LQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTE-----GEIQIDGVSWNS 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4763 VDLASAGKAgilIGYCPQQDALdelLTGW--EHLQYYCRLRgipKQYIPEVAADLVRRLHLESHVDK-------PVATYS 4833
Cdd:TIGR01271 1285 VTLQTWRKA---FGVIPQKVFI---FSGTfrKNLDPYEQWS---DEEIWKVAEEVGLKSVIEQFPDKldfvlvdGGYVLS 1355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4834 GGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDgCAAVLTSHSME---ECEALctrlaIMVDGS 4908
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEHRVEallECQQF-----LVIEGS 1427
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3827-4002 |
1.67e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3827 QELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITIN-GKNLQ-TDLSKVREELGVCPQQDVLLDNLTVREHL 3904
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKdINLKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3905 MLFASIKAPWWTTKELQQQVN------------------------KTLDEVELTQHQHK--------------------- 3939
Cdd:PTZ00265 482 YSLYSLKDLEALSNYYNEDGNdsqenknkrnscrakcagdlndmsNTTDSNELIEMRKNyqtikdsevvdvskkvlihdf 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292744 3940 --------------PAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHL 4002
Cdd:PTZ00265 562 vsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4693-4907 |
1.82e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4693 VLCNLSKSYrsvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPpssgytvirtpQGDMVDLASAGK-- 4770
Cdd:PRK10938 262 VLNNGVVSY-----NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-----------QGYSNDLTLFGRrr 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 -AGIL-------IGYCPQQdaldelltgwEHLQYY--CRLR-----------GIpKQYIPE----VAADLVRRLHLESHV 4825
Cdd:PRK10938 326 gSGETiwdikkhIGYVSSS----------LHLDYRvsTSVRnvilsgffdsiGI-YQAVSDrqqkLAQQWLDILGIDKRT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4826 -DKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVL-TSHSMEECEALCT-RLA 4902
Cdd:PRK10938 395 aDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAEDAPACIThRLE 474
|
....*
gi 116292744 4903 IMVDG 4907
Cdd:PRK10938 475 FVPDG 479
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
3837-4015 |
2.56e-05 |
|
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: 49.29 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3837 QITALLGTNGAGKTTIISMLMGLFPPTSGTITIN-----------GKNLQTDLSKVREELGVCPQQDVLLDNLTvrehlm 3905
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwdeildefrGSELQNYFTKLLEGDVKVIVKPQYVDLIP------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3906 lfasiKAPWWTTKELQQQVNKT--LDEV----ELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSR 3979
Cdd:cd03236 101 -----KAVKGKVGELLKKKDERgkLDELvdqlELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 116292744 3980 -------RSLwdillkYREGRTIIFTTHHLDEAEMLSDHVAVL 4015
Cdd:cd03236 176 lnaarliREL------AEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4712-4923 |
3.51e-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: 50.71 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIRTPqgdmvdlasagkagilIGYCPQQdALDELLTGW 4791
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------------VAYVPQQ-AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4792 EHLQYYCRLRgiPKQYIPEV-AADLVRRLHL-----ESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPC 4865
Cdd:TIGR00957 717 ENILFGKALN--EKYYQQVLeACALLPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4866 SKRYLWQTIT--QEVRDGCAAVLTSHSMEECEALcTRLAIMVDGSFRCLGPPQHIKNRFG 4923
Cdd:TIGR00957 795 VGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4715-4890 |
3.74e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 47.15 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4715 ISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPQGDMVDLASAGkagiligYCPQQDALDELLTGWEHl 4794
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-RIGMPEGEDLLFLPQRP-------YLPLGTLREQLIYPWDD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4795 qyycrlrgipkqyipevaadlvrrlhleshvdkpvaTYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTI 4874
Cdd:cd03223 91 ------------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170
....*....|....*..
gi 116292744 4875 TQEvrdgCAAVLT-SHS 4890
Cdd:cd03223 135 KEL----GITVISvGHR 147
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4725-4910 |
6.72e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4725 FGLLGVNGAGKSTTFKILNGETPPSSGyTVIRTPqgdmvdlasagkaGILIGYCPQ-QDA------LDELLTG----WEH 4793
Cdd:PRK15064 30 YGLIGANGCGKSTFMKILGGDLEPSAG-NVSLDP-------------NERLGKLRQdQFAfeeftvLDTVIMGhtelWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4794 LQYYCRLrgipkqY-IPEVA-ADLVRRLHLESH-------------------VDKPVATYSG-------GTRRKLSTALA 4845
Cdd:PRK15064 96 KQERDRI------YaLPEMSeEDGMKVADLEVKfaemdgytaearagelllgVGIPEEQHYGlmsevapGWKLRVLLAQA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4846 LVGKPDILLLDEPSSGMDPCSKRYLWQTITQevRDgCAAVLTSHSMEECEALCTRLAIMVDGSFR 4910
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RN-STMIIISHDRHFLNSVCTHMADLDYGELR 231
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3828-4000 |
8.99e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3828 ELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITIngKNLQTD------LSKVREELGvcpqqdvLLDNLTVR 3901
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINniakpyCTYIGHNLG-------LKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3902 EHLMLFASIkapwWTTKELqqqVNKTLDEVELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRS 3981
Cdd:PRK13541 89 ENLKFWSEI----YNSAET---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|
gi 116292744 3982 LWD-ILLKYREGRTIIFTTH 4000
Cdd:PRK13541 162 LNNlIVMKANSGGIVLLSSH 181
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4709-4873 |
9.41e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4709 TTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGytvirtpqgdmvDLASAGKagilIGYCPQQDAL---- 4784
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG------------KIKHSGR----ISFSPQTSWImpgt 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4785 --DELLTGWEHLQYycRLRGIPKqyipevAADLVRRLHLESHVDKPV-----ATYSGGTRRKLSTALALVGKPDILLLDE 4857
Cdd:TIGR01271 503 ikDNIIFGLSYDEY--RYTSVIK------ACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDS 574
|
170
....*....|....*.
gi 116292744 4858 PSSGMDPCSKRYLWQT 4873
Cdd:TIGR01271 575 PFTHLDVVTEKEIFES 590
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4828-4907 |
1.01e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4828 PVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDG 4907
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3814-4014 |
1.13e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.63 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKVAVQELTLtfHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTItingkNLQTDLS-KvreelgvcPQ-- 3890
Cdd:COG1245 346 DLTKSYGGFSLEVEGGEI--REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLKISyK--------PQyi 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 -QDVlldNLTVREHLM--LFASIKAPWWTTkELQQ--QVNKTLDeveltqhqhKPAGVLSGGMKRKLSIGIAfmgMSKTV 3965
Cdd:COG1245 411 sPDY---DGTVEEFLRsaNTDDFGSSYYKT-EIIKplGLEKLLD---------KNVKDLSGGELQRVAIAAC---LSRDA 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116292744 3966 ---VLDEPSSGVDPCSRRSLWDILLKYREGR--TIIFTTHHLDEAEMLSDHVAV 4014
Cdd:COG1245 475 dlyLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3826-4019 |
1.15e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3826 VQELTLTFHRDQITALLGTNGAGKT-TIISMLMGL-FPP---TSGTITINGKNL----QTDLSKVR-EELGVCPQQD-VL 3894
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLlhasEQTLRGVRgNKIAMIFQEPmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3895 LDNL-TVREHLMLFASIKapwwttKELQQQVNKT-----LDEVELTQ---------HQhkpagvLSGGMKRKLSIGIAFM 3959
Cdd:PRK15134 105 LNPLhTLEKQLYEVLSLH------RGMRREAARGeilncLDRVGIRQaakrltdypHQ------LSGGERQRVMIAMALL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116292744 3960 GMSKTVVLDEPSSGVDPCSRRSLWDIL--LKYREGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
3538-3741 |
1.23e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 46.35 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3538 FFFP-LIMMLTWMVAVASMVRKLVYEREIQIEEYMRMMGLHPTIHFLSWFLenmATLALSSAALAVILKMSGIFMH---- 3612
Cdd:COG0842 4 FLVPgLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVL---AYLLRGLLQALLVLLVALLFFGvplr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3613 -SDAFIIFLYLLDFGVSAVMMSYFLSVFFNQANTAALCTSLGYMISFL------PYvvllvlhNQLSFAIQTLLCLLSTT 3685
Cdd:COG0842 81 gLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFlsgaffPI-------ESLPGWLQAIAYLNPLT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 116292744 3686 AFGQGVFFItFLEGQEEGIQWGNMYrapepggmtfgwvcWMILFDAILYFLGGWYF 3741
Cdd:COG0842 154 YFVEALRAL-FLGGAGLADVWPSLL--------------VLLAFAVVLLALALRLF 194
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4700-4863 |
1.49e-04 |
|
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: 48.20 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4700 SYRSVFGGKttAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLASAGKAGILIGYCP 4779
Cdd:TIGR01193 480 SYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL---NGFSLKDIDRHTLRQFINYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4780 QQ------DALDELLTG------WEHLQYYCRLRGIpKQYIPEVAADLVRRLHLEShvdkpvATYSGGTRRKLSTALALV 4847
Cdd:TIGR01193 555 QEpyifsgSILENLLLGakenvsQDEIWAACEIAEI-KDDIENMPLGYQTELSEEG------SSISGGQKQRIALARALL 627
|
170
....*....|....*.
gi 116292744 4848 GKPDILLLDEPSSGMD 4863
Cdd:TIGR01193 628 TDSKVLILDESTSNLD 643
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4810-4909 |
1.50e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4810 EVAADLVRRLHLESH-VDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTS 4888
Cdd:NF040905 382 KVAEEYRKKMNIKTPsVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVIS 461
|
90 100
....*....|....*....|.
gi 116292744 4889 HSMEECEALCTRLAIMVDGSF 4909
Cdd:NF040905 462 SELPELLGMCDRIYVMNEGRI 482
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3809-4019 |
1.76e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3809 GVALISVTKEYEDHKVAVQELTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLqTDLSKVREELGVC 3888
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3889 PQQDVLLDNLTVREHLMLFASI----KApwwttkELQQQVNKTLDEVELTQH-QHKPAGvLSGGMKRKLSIGIAFMGMSK 3963
Cdd:PRK11650 82 FQNYALYPHMSVRENMAYGLKIrgmpKA------EIEERVAEAARILELEPLlDRKPRE-LSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116292744 3964 TVVLDEPSSGVDPCSR-----------RSLwdillkyreGRTIIFTTHHLDEAEMLSDHVAVLQQGR 4019
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRvqmrleiqrlhRRL---------KTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4722-4863 |
2.14e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4722 GECFGLLGVNGAGKSTTFKILNGETPPSSG-YTVIRTPQGDMVDLASAGKAGILIGYCPQQD----ALD-ELLTGWEH-- 4793
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGsYTFPGNWQLAWVNQETPALPQPALEYVIDGDreyrQLEaQLHDANERnd 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4794 ----LQYYCRLRGIPKQYIPEVAADLVRRLHL-ESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMD 4863
Cdd:PRK10636 107 ghaiATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4692-4910 |
2.40e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.39 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4692 MVLCNLSKSYRSvfgGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTF----KILNGEtppssGYTVIRTPQGDMVDLAS 4767
Cdd:cd03289 3 MTVKDLTAKYTE---GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNTE-----GDIQIDGVSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4768 AGKAgilIGYCPQQDALdelLTG--WEHLQYYCRLRgipKQYIPEVAADLVRRLHLESHVDKP--VATYSG-----GTRR 4838
Cdd:cd03289 75 WRKA---FGVIPQKVFI---FSGtfRKNLDPYGKWS---DEEIWKVAEEVGLKSVIEQFPGQLdfVLVDGGcvlshGHKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4839 KLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDgCAAVLTSHSMeecEAL--CTRLAIMVDGSFR 4910
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD-CTVILSEHRI---EAMleCQRFLVIEENKVR 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4696-4858 |
2.66e-04 |
|
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: 47.37 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSYRSVfGGKTTAVHGISLGIPRGECFGLLGVNGAGKS-TTFKILnGETPPSSGYtvirtPQGDM----VDLASAGK 4770
Cdd:COG4172 11 DLSVAFGQG-GGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAAH-----PSGSIlfdgQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4771 AgiligycpqqdaldELltgwehlqyyCRLRG-------------------IPKQyIPEV---------AADLVRRLHLE 4822
Cdd:COG4172 84 R--------------EL----------RRIRGnriamifqepmtslnplhtIGKQ-IAEVlrlhrglsgAAARARALELL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116292744 4823 SHV-----DKPVATY----SGGTRRKLSTALALVGKPDILLLDEP 4858
Cdd:COG4172 139 ERVgipdpERRLDAYphqlSGGQRQRVMIAMALANEPDLLIADEP 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4702-4908 |
2.91e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4702 RSVFGGKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVIrtpQGDMVDLAS---AGKAGILI--- 4775
Cdd:PRK09700 269 RNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL---NGKDISPRSpldAVKKGMAYite 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4776 -----GYCP-----QQDALDELLTgwehLQYYCRLRGIPKQYIPEVAADLVRR-LHLESH-VDKPVATYSGGTRRKLSTA 4843
Cdd:PRK09700 346 srrdnGFFPnfsiaQNMAISRSLK----DGGYKGAMGLFHEVDEQRTAENQRElLALKCHsVNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 4844 LALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSMEECEALCTRLAIMVDGS 4908
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4830-4927 |
4.27e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4830 ATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRY---LWQTITQEVRdgCAAVLTSHSMEECEALCTRLAIMVD 4906
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQilaLLKSLQQKHQ--LAYLFISHDLHVVRALCHQVIVLRQ 501
|
90 100
....*....|....*....|.
gi 116292744 4907 GSFRCLGPPQHIKNRFGDGYT 4927
Cdd:PRK15134 502 GEVVEQGDCERVFAAPQQEYT 522
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3829-4029 |
4.33e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3829 LTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNL-QTDLSKVREELGVCPQQDVLLDNlTVREHLMLF 3907
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3908 ASIK-APWWTTKElQQQVNKTLDE--VELTQHQHKPAGVLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWD 3984
Cdd:PLN03232 1334 SEHNdADLWEALE-RAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQR 1412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116292744 3985 ILLKYREGRTIIFTTHHLDEAeMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PLN03232 1413 TIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
3784-4018 |
5.27e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 45.62 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3784 FFNEDFGN--KGLSQQNGPGEMEGGNPGVALisvtKEYEDHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLF 3860
Cdd:cd03291 12 FWDEGFGEllEKAKQENNDRKHSSDDNNLFF----SNLCLVGAPVlKNINLKIEKGEMLAITGSTGSGKTSLLMLILGEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3861 PPTSGTITINGKnlqtdlskvreeLGVCPQQDVLLDNlTVREHLMLFAS---------IKAPwwttkELQQQVNKtldev 3931
Cdd:cd03291 88 EPSEGKIKHSGR------------ISFSSQFSWIMPG-TIKENIIFGVSydeyryksvVKAC-----QLEEDITK----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3932 eLTQHQHKPAG----VLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWD-ILLKYREGRTIIFTTHHLDEAE 4006
Cdd:cd03291 145 -FPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLMANKTRILVTSKMEHLK 223
|
250
....*....|..
gi 116292744 4007 MlSDHVAVLQQG 4018
Cdd:cd03291 224 K-ADKILILHEG 234
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
4820-4892 |
5.32e-04 |
|
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: 45.46 E-value: 5.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292744 4820 HLESHVDKPVATY--SGGTRRKLSTALAL---VGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTSHSME 4892
Cdd:pfam13304 223 LLENGGGGELPAFelSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
3940-4000 |
5.32e-04 |
|
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: 45.46 E-value: 5.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116292744 3940 PAGVLSGGMKRKLSIGIAFMGMSK---TVVLDEPSSGVDPCSRRSLWDILLKYREGRT-IIFTTH 4000
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3814-3975 |
8.02e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3814 SVTKEYEDHKVAVQELTLtfHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGKnlqtdLS-KvreelgvcPQ-- 3890
Cdd:PRK13409 345 DLTKKLGDFSLEVEGGEI--YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----ISyK--------PQyi 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3891 ---QDVlldnlTVREHLMlfaSIKA----PWWTTkELQQ--QVNKTLDeveltqhqhKPAGVLSGGMKRKLSIGIAfmgM 3961
Cdd:PRK13409 410 kpdYDG-----TVEDLLR---SITDdlgsSYYKS-EIIKplQLERLLD---------KNVKDLSGGELQRVAIAAC---L 468
|
170
....*....|....*..
gi 116292744 3962 SKTV---VLDEPSSGVD 3975
Cdd:PRK13409 469 SRDAdlyLLDEPSAHLD 485
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3840-4002 |
9.45e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3840 ALLGTNGAGKTTIISMLMGLFPPTSGTITIngknlqtdlskVREELGVCPQQDVLLdNLTVREHLmLFASIKAPwwttke 3919
Cdd:PLN03130 647 AIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIF-NATVRDNI-LFGSPFDP------ 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3920 lqQQVNKTLDEVELtQH--QHKPAGVL----------SGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWDILL 3987
Cdd:PLN03130 708 --ERYERAIDVTAL-QHdlDLLPGGDLteigergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI 784
|
170
....*....|....*..
gi 116292744 3988 KyRE--GRTIIFTTHHL 4002
Cdd:PLN03130 785 K-DElrGKTRVLVTNQL 800
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3841-4029 |
1.51e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3841 LLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQ----TDLSKVreeLGVCPQQDVLLDNlTVREHLMLFASIK-APWW 3915
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfglMDLRKV---LGIIPQAPVLFSG-TVRFNLDPFNEHNdADLW 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3916 TTKE---LQQQVNKT---LDeVELTQhqhkpAGV-LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSrrslwDILLK 3988
Cdd:PLN03130 1346 ESLErahLKDVIRRNslgLD-AEVSE-----AGEnFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT-----DALIQ 1414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116292744 3989 --YRE---GRTIIFTTHHLDEAeMLSDHVAVLQQGRLRCYAPPADL 4029
Cdd:PLN03130 1415 ktIREefkSCTMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENL 1459
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4696-4907 |
1.65e-03 |
|
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: 44.68 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4696 NLSKSY---RSVFG---GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTfkilngetppssGYTVIR--TPQGDMV---- 4763
Cdd:COG4172 280 DLKVWFpikRGLFRrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL------------GLALLRliPSEGEIRfdgq 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4764 DLASAGKAGILigycP-----Q---QD---ALD------ELLTgwEHLQYYCrlRGIPKQYIPEVAADLVRRLHL-ESHV 4825
Cdd:COG4172 348 DLDGLSRRALR----PlrrrmQvvfQDpfgSLSprmtvgQIIA--EGLRVHG--PGLSAAERRARVAEALEEVGLdPAAR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4826 DKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDpcskrylwQTITQEV----RD-----GCAAVLTSHSMEECEA 4896
Cdd:COG4172 420 HRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD--------VSVQAQIldllRDlqrehGLAYLFISHDLAVVRA 491
|
250
....*....|.
gi 116292744 4897 LCTRLAIMVDG 4907
Cdd:COG4172 492 LAHRVMVMKDG 502
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3784-4023 |
2.00e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.90 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3784 FFNEDFGN--KGLSQQNGPGEMEGGNPGVALisvtKEYEDHKVAV-QELTLTFHRDQITALLGTNGAGKTTIISMLMGLF 3860
Cdd:TIGR01271 401 SWDEGIGElfEKIKQNNKARKQPNGDDGLFF----SNFSLYVTPVlKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGEL 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3861 PPTSGTITINGKnlqtdlskvreeLGVCPQQDVLLDNlTVREHLMLFASIKAPWWTTKELQQQVNKtlDEVELTQHQHKP 3940
Cdd:TIGR01271 477 EPSEGKIKHSGR------------ISFSPQTSWIMPG-TIKDNIIFGLSYDEYRYTSVIKACQLEE--DIALFPEKDKTV 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3941 AG----VLSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLWD-ILLKYREGRTIIFTT---HHLDEAemlsDHV 4012
Cdd:TIGR01271 542 LGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEsCLCKLMSNKTRILVTsklEHLKKA----DKI 617
|
250
....*....|.
gi 116292744 4013 AVLQQGrlRCY 4023
Cdd:TIGR01271 618 LLLHEG--VCY 626
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4696-4755 |
2.07e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116292744 4696 NLSKSYRSVFG----GKTTAVHGISLGIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGYTVI 4755
Cdd:PRK15112 9 NLSKTFRYRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI 72
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4779-4863 |
3.39e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4779 PQQDALDELLTGWEHLQYYCRLRGIPKQYIPEVAADLVRRLHLESHVD-KPVATYSGGTRRKLSTALALVGKPDILLLDE 4857
Cdd:PLN03073 291 ANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQvKATKTFSGGWRMRIALARALFIEPDLLLLDE 370
|
....*.
gi 116292744 4858 PSSGMD 4863
Cdd:PLN03073 371 PTNHLD 376
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3821-3975 |
4.69e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3821 DHKVAVQELTLTFHR-DQItALLGTNGAGKTTIISMLMGLFPPTSGTITINGKNLQTDLSKVREELGvcPQQDVlLDNLT 3899
Cdd:PRK11147 330 DGKQLVKDFSAQVQRgDKI-ALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELD--PEKTV-MDNLA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3900 ----------VREHLM------LFASIKApwwttkelqqqvnktldeveLTqhqhkPAGVLSGGMKRKLSIGIAFMGMSK 3963
Cdd:PRK11147 406 egkqevmvngRPRHVLgylqdfLFHPKRA--------------------MT-----PVKALSGGERNRLLLARLFLKPSN 460
|
170
....*....|..
gi 116292744 3964 TVVLDEPSSGVD 3975
Cdd:PRK11147 461 LLILDEPTNDLD 472
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3829-4000 |
4.82e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 43.40 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3829 LTLTFHRDQITALLGTNGAGKTTIISMLMGLFPPTSGTITINGknlqtdlskvreELGVCPQQdVLLDNLTVREHLMLFA 3908
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQ-AWIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 3909 SIKAPWWTTkelQQQVNKTLDEVEL----TQHQHKPAGV-LSGGMKRKLSIGIAFMGMSKTVVLDEPSSGVDPCSRRSLW 3983
Cdd:TIGR00957 724 ALNEKYYQQ---VLEACALLPDLEIlpsgDRTEIGEKGVnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180
....*....|....*....|
gi 116292744 3984 DILLKYR---EGRTIIFTTH 4000
Cdd:TIGR00957 801 EHVIGPEgvlKNKTRILVTH 820
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4729-4890 |
4.94e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4729 GVNGAGKSTTFKILNGETPPSSGYTVIRTPQGDMVdlasagkAGILIGYCPQQDALDELLTGWEHLQYYCRLRGIPkqyi 4808
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------AKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4809 pEVAADLVRRLHLESHVDKPVATYSGGTRRKLSTALALVGKPDILLLDEPSSGMDPCSKRYLWQTITQEVRDGCAAVLTS 4888
Cdd:PRK13541 102 -ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSS 180
|
..
gi 116292744 4889 HS 4890
Cdd:PRK13541 181 HL 182
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4712-4863 |
8.53e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4712 VHGIslgIPRGECFGLLGVNGAGKSTTFKILNGETPPSSGY--TVIR---TPQGDMVDLasagKAGILIgYCPQQDALDE 4786
Cdd:TIGR00956 80 MDGL---IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGveGVITydgITPEEIKKH----YRGDVV-YNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292744 4787 LLTGWEHLQYYCRLRGipkqyiPEVAADLVRRLHLESHV-DKPVATY------------------SGGTRRKLSTALALV 4847
Cdd:TIGR00956 152 HLTVGETLDFAARCKT------PQNRPDGVSREEYAKHIaDVYMATYglshtrntkvgndfvrgvSGGERKRVSIAEASL 225
|
170
....*....|....*.
gi 116292744 4848 GKPDILLLDEPSSGMD 4863
Cdd:TIGR00956 226 GGAKIQCWDNATRGLD 241
|
|
| |
