|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
236-1594 |
4.17e-124 |
|
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: 432.13 E-value: 4.17e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 236 VYFISLNVT----KERKKSKNLMKVMGLQDSAFWLSWGLIYAGFIFIISIFITIVITFTEIIVMTGFMVIFILFFLYGLS 311
Cdd:TIGR01257 664 IYSVSMTVKsivlEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTA 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 312 LVALVFLMSVLLKKAVLTNLV--VFLLTLFWGCLGFTVFYEQLPSSLGWILSICSPFAFTAGMTQIIKLDYNLNGV---- 385
Cdd:TIGR01257 744 TIMQCFLLSTFFSKASLAAACsgVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLqwsn 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 386 IFPDP-SGDSYTMIATFSILLLDGFIYLLLALYFDKILPyGDERRYSPLFFL-NSSSCFQHQGTDNK----------VIE 453
Cdd:TIGR01257 824 IGNSPlEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFP-GDYGTPLPWYFLlQESYWLGGEGCSTReeralektepLTE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 454 KEIDAEHP---SDDYFEPVAPEFQgkEAIRIRNVKKEYKgKSGKvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG 530
Cdd:TIGR01257 903 EMEDPEHPegiNDSFFERELPGLV--PGVCVKNLVKIFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTG 978
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 531 LSVPTEGSVTIYNKNLSemQDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQD 610
Cdd:TIGR01257 979 LLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRN 1056
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 611 NLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNG 690
Cdd:TIGR01257 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 691 RLKCAGSSIFLKRRWGLGYHLSLHRN------------------------------EICNPEQI--------TSFITHHI 732
Cdd:TIGR01257 1137 RLYCSGTPLFLKNCFGTGFYLTLVRKmkniqsqrggcegtcsctskgfstrcparvDEITPEQVldgdvnelMDLVYHHV 1216
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 733 PDAKLKTKNKEKLVYTLPLE--RTNIFPDLFSNLDKC-SDQGVTGYDISMSTLNEIFMKLEGQST--------TKQDFKQ 801
Cdd:TIGR01257 1217 PEAKLVECIGQELIFLLPNKnfKQRAYASLFRELEETlADLGLSSFGISDTPLEEIFLKVTEDADsgslfaggAQQKREN 1296
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 802 VEM----IRDSESLNEMELAHSSFSEMQTAV------------------SDMHLWRMQVFAMARLRFLKLKRQTK----- 854
Cdd:TIGR01257 1297 ANLrhpcSGPTEKAGQTPQASHTCSPGQPAAhpegqpppepedpgvplnTGARLILQHVQALLVKRFQHTIRSHKdflaq 1376
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 855 VLLTLLLVFGIAMFPLIVENI-----------MYA----------------------MLNE--------KIDW--EFK-- 889
Cdd:TIGR01257 1377 IVLPATFVFLALMLSIIIPPFgeypaltlhpwMYGqqytffsmdepnsehlevladvLLNKpgfgnrclKEEWlpEYPcg 1456
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 890 --------------TELY--------FLSPG----------QLPQEP-------------RTSLLIINNTESNIEDFI-- 922
Cdd:TIGR01257 1457 nstpwktpsvspniTHLFqkqkwtaaHPSPScrcstrekltMLPECPegagglpppqrtqRSTEILQDLTDRNISDFLvk 1536
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 923 -------KSLKHQnilLEVDdfENRNGtdGLSYNG---AIIVSGK----------------------------------- 957
Cdd:TIGR01257 1537 typalirSSLKSK---FWVN--EQRYG--GISIGGklpAIPITGEalvgflsdlgqmmnvsggpvtreaskempdflkhl 1609
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 958 QKDYRFSVVCNTKRLHCFPILMNIISNGLLRMLNHTQH------IRIESSPF-----PLSHIGLWTGLPDGS------FF 1020
Cdd:TIGR01257 1610 ETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRdpeeygITVISQPLnltkeQLSEITVLTTSVDAVvaicviFA 1689
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1021 LFLVLCSISPYItmgsISDYKKNAKSQLWISGLYTSAYWCGQALVDVSFFIlILLAMYLIFYIENMQYLLITSQIVFALV 1100
Cdd:TIGR01257 1690 MSFVPASFVLYL----IQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYA-VSAGLVVGIFIGFQKKAYTSPENLPALV 1764
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1101 IVTPGYAASLVFLIYMISFIFRKRRKNSALWSFYFFF----ASIIMFVTALISN----FDLSILITTMVLVPSYTLLGfK 1172
Cdd:TIGR01257 1765 ALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFiginSSAITFVLELFENnrtlLRFNAMLRKLLIVFPHFCLG-R 1843
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1173 TFLEMRDQQ-------HYRESPEAN---FKLSATDFLVCFIP---YFqtLLFIFVLRCMELKYGKKRMRKDPVFrispqs 1239
Cdd:TIGR01257 1844 GLIDLALSQavtdvyaQFGEEHSANpfqWDLIGKNLVAMAVEgvvYF--LLTLLIQHHFFLSRWIAEPAKEPIF------ 1915
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1240 rdakpnpeepiDEDEDVQAERIRTATAlttsiLDEKPVIIASCLHKEYAGQKKScfskrkkkiAARNISFCVQEGEILGL 1319
Cdd:TIGR01257 1916 -----------DEDDDVAEERQRIISG-----GNKTDILRLNELTKVYSGTSSP---------AVDRLCVGVRPGECFGL 1970
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1320 LGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHLGYCPQENVLWPMLTAREHLEVYAAVKGLRKVDARLA 1393
Cdd:TIGR01257 1971 LGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltnISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKV 2050
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1394 ITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNtERGVLLTTHN 1473
Cdd:TIGR01257 2051 ANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHS 2129
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1474 LAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYILELKVKEPSQVTL-----VHTEILKLFPQAAGQERYSSLLTYK 1548
Cdd:TIGR01257 2130 MEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDLLpdlnpVEQFFQGNFPGSVQRERHYNMLQFQ 2209
|
1610 1620 1630 1640
....*....|....*....|....*....|....*....|....*.
gi 1622880985 1549 LPVADvypLSQAFHKLEAVKHNFNLEEYSLSQCTLEKVFLELSKEQ 1594
Cdd:TIGR01257 2210 VSSSS---LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1297-1502 |
4.57e-83 |
|
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: 271.69 E-value: 4.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1297 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWPML 1370
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdrkAARQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 TAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1450
Cdd:cd03263 91 TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1451 QMWQAIQAVVKNteRGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLK 1502
Cdd:cd03263 171 AIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
479-702 |
2.08e-79 |
|
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: 261.29 E-value: 2.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLseMQDLEEIRKI 558
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSIFLK 702
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1296-1513 |
1.49e-70 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 236.50 E-value: 1.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWP 1368
Cdd:COG1131 7 TKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1448
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1449 QQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYILEL 1513
Cdd:COG1131 167 RRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLEL 230
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
479-697 |
1.40e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 230.72 E-value: 1.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqDLEEIRKI 558
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRAD-HVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1277-1508 |
1.99e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 196.23 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1277 VIIASCLHKEYagqkkscfskrKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSS---- 1352
Cdd:COG4555 1 MIEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkep 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1353 --VLGHLGYCPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLG 1430
Cdd:COG4555 70 reARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1431 NSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKD 1508
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
479-697 |
2.48e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 195.85 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqDLEEIRKI 558
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK--EPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRA-DHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1296-1492 |
1.49e-53 |
|
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: 185.29 E-value: 1.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWP 1368
Cdd:cd03230 7 SKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDikkepeEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLevyaavkglrkvdarlaitrlvsafklheqlnvpvqKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1448
Cdd:cd03230 87 NLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622880985 1449 QQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03230 131 RREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1303-1590 |
6.17e-53 |
|
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: 188.37 E-value: 6.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcsSVLGH------------LGYCPQENVLWPML 1370
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTA------RVAGYdvvreprkvrrsIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 TAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1450
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1451 QMWQAIQAVVKnTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYILELKVKEPSQVTLVHTEILK 1530
Cdd:TIGR01188 162 AIWDYIRALKE-EGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1531 LFPQAAGQERYSSLL-TYKLPVADvyPLSQAFHKLEAVKHN-FNLEEYSLSQCTLEKVFLEL 1590
Cdd:TIGR01188 241 LGETGLGLLAVTVDSdRIKILVPD--GDETVPEIVEAAIRNgIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
479-692 |
8.33e-53 |
|
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: 182.98 E-value: 8.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqDLEEIRKI 558
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLslfakikgihpqeveqevqrilleldmqniqdnlakHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKtILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1303-1502 |
2.27e-50 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 177.95 E-value: 2.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWPMLTAREHL 1376
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvreprEVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1377 EVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1456
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622880985 1457 QAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLK 1502
Cdd:cd03265 175 EKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1296-1596 |
1.48e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 178.38 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---CSSVLGHLGYCPQENVLWPMLT 1371
Cdd:COG4152 8 TKRfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGeplDPEDRRRIGYLPEERGLYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1451
Cdd:COG4152 88 VGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1452 MWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKdYILELKVKEPsqvtlvhTEIL 1529
Cdd:COG4152 168 LKDVIREL---AAKGttVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR-NTLRLEADGD-------AGWL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1530 KLFPQAAGQERYSSLLTYKLPvADVYPlsQAFhkLEAVKHNFNLEEYSLSQCTLEKVFLELSKEQEV 1596
Cdd:COG4152 237 RALPGVTVVEEDGDGAELKLE-DGADA--QEL--LRALLARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
479-697 |
4.76e-49 |
|
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: 174.44 E-value: 4.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 558
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQF-NVQFDILTVKENLSlFA-KIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLtfgiAILG---- 632
Cdd:COG1122 77 VGLVFQNpDDQLFAPTVEEDVA-FGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV----AIAGvlam 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 633 DPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
493-791 |
6.40e-49 |
|
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: 176.81 E-value: 6.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLseMQDLEEIRKITGVCPQFNVQFDIL 572
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRKVRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 TVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRD 652
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 653 QVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSIFLKRRWGlGYHLSLHRNEICNPEQITSFITHH 731
Cdd:TIGR01188 162 AIWDYIRAlKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 732 IPDAKLKTKNKEKL-----VYTLPLERTniFPDLFSNLDKcsdQGVTGYDISM--STLNEIFMKLEG 791
Cdd:TIGR01188 241 LGETGLGLLAVTVDsdrikILVPDGDET--VPEIVEAAIR---NGIRIRSISTerPSLDDVFLKLTG 302
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
480-691 |
9.40e-49 |
|
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: 173.04 E-value: 9.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 480 RIRNVKKEYKGksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKIT 559
Cdd:cd03225 1 ELKNLSFSYPD--GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 560 GVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03225 78 GLVFQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGR 691
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1277-1518 |
2.31e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 175.66 E-value: 2.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1277 VIIASCLHKEY---------AGQKKSCFSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVE 1346
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRREYREVEAvDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1347 LkgcssvlghLGYCPQEN----------V------LWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVP 1410
Cdd:COG4586 81 V---------LGYVPFKRrkefarrigvVfgqrsqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1411 VQKLTTGT-MRklC-FVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVvkNTERG--VLLTTHNLAEAEALCDRVAI 1486
Cdd:COG4586 152 VRQLSLGQrMR--CeLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRERGttILLTSHDMDDIEALCDRVIV 227
|
250 260 270
....*....|....*....|....*....|..
gi 1622880985 1487 MVSGRLRCIGSIQHLKNKLGKDYILELKVKEP 1518
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEP 259
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
479-702 |
4.26e-47 |
|
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: 168.32 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNknLSEMQDLEEIRKI 558
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAGSSIFLK 702
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
479-692 |
5.73e-47 |
|
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: 168.05 E-value: 5.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIR 556
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLseKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 --KITGVCPQFNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDP 634
Cdd:cd03255 81 rrHIGFVFQSFNL-LPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 635 QILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADiLADRKVIMSNGRL 692
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1295-1496 |
4.44e-46 |
|
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: 165.15 E-value: 4.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---SVLGHLGYCPQENVLWPML 1370
Cdd:cd03269 6 VTKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiAARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 TAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1450
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622880985 1451 QMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:cd03269 166 LLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
479-693 |
1.34e-43 |
|
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: 158.13 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGqITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDleEIRKI 558
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ--KLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQ-FNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQIL 637
Cdd:cd03264 74 IGYLPQeFGV-YPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 638 LLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRLK 693
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1295-1496 |
1.48e-43 |
|
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: 158.30 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLW 1367
Cdd:cd03266 11 FRDVKKTVQAvDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDvvkepaEARRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1447
Cdd:cd03266 91 DRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622880985 1448 GQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:cd03266 171 ATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
476-692 |
3.23e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.51 E-value: 3.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 476 KEAIRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLE 553
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLseRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 554 EIR--KItGVCPQ-FNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQK------Rkl 624
Cdd:COG1136 82 RLRrrHI-GFVFQfFNL-LPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQqrvaiaR-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 625 tfgiAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADIlADRKVIMSNGRL 692
Cdd:COG1136 158 ----ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1305-1479 |
3.65e-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: 153.79 E-value: 3.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHLGYCPQENVLWPMLTAREHLEV 1378
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 YAAVKGLRkvDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1458
Cdd:COG4133 99 WAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170 180
....*....|....*....|...
gi 1622880985 1459 VVkntERG--VLLTTHNLAEAEA 1479
Cdd:COG4133 177 HL---ARGgaVLLTTHQPLELAA 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
479-696 |
3.90e-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: 154.06 E-value: 3.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIynKNLSEMQDLEEIRKI 558
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRAD-HVILFSTQSMDEADILADRKVIMSNGRLKCAG 696
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
479-692 |
5.72e-42 |
|
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: 153.14 E-value: 5.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNlseMQDLEEIRKI 558
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS---YQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGV---CPQFnvqFDILTVKENLSLFAKIKGIHpqevEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQ 635
Cdd:cd03268 74 IGAlieAPGF---YPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 636 ILLLDEPTTGLDPFSRDQVWSLLREHRAD-HVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
479-693 |
3.70e-41 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 151.47 E-value: 3.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNknlsemQDLEEIRKI 558
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG------EPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 639 LDEPTTGLDPFSR----DQVWSLLREHRadHVILFSTQSMDEADILADRKVIMSN--GRLK 693
Cdd:cd03293 155 LDEPFSALDALTReqlqEELLDIWRETG--KTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
479-692 |
1.09e-40 |
|
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: 150.42 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEIR 556
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITG-VCPQFNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRiLLEL-DMQNIQDNLAKHLSEGQKRKLTFGIAILGDP 634
Cdd:cd03258 82 RRIGmIFQHFNL-LSSRTVFENVALPLEIAGVPKAEIEERVLE-LLELvGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 635 QILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1291-1493 |
1.20e-40 |
|
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: 149.67 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1291 KKSCFSKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-----CSSVLGHLGYCPQEN 1364
Cdd:cd03268 2 KTNDLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkNIEALRRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1365 VLWPMLTAREHLEVYAAVKGLRKVDarlaITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGI 1444
Cdd:cd03268 82 GFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622880985 1445 DPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLR 1493
Cdd:cd03268 158 DPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
479-691 |
1.24e-39 |
|
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: 146.47 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemQDLEEIRKI 558
Cdd:COG4133 3 LEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--DAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEveQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADH-VILFSTQsmDEADILADRKVIMSNGR 691
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGgAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1296-1493 |
1.54e-39 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 146.57 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGeILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWP 1368
Cdd:cd03264 7 TKRyGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqKLRRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1448
Cdd:cd03264 86 NFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1449 QQQMWQAIQAVVKNteRGVLLTTHNLAEAEALCDRVAIMVSGRLR 1493
Cdd:cd03264 166 RIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
479-692 |
1.71e-39 |
|
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: 146.94 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL-----SVPTEGSVTIYNKNLSEMQ-DL 552
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDvDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 553 EEIRKITGVCPQFNVQFDiLTVKENLSLFAKIKGIHPQEVEQEVQRILLE---LDmQNIQDNL-AKHLSEGQKRKLTFGI 628
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRkaaLW-DEVKDRLhALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
458-799 |
1.99e-39 |
|
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: 161.33 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 458 AEHPSDDYFEPVAPEFQ-------GKEAIRIRNVKKEYKGKSGKveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG 530
Cdd:TIGR01257 1910 AKEPIFDEDDDVAEERQriisggnKTDILRLNELTKVYSGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 531 LSVPTEGSVTIYNKNLseMQDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQD 610
Cdd:TIGR01257 1988 DTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYAD 2065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 611 NLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVW----SLLREHRAdhvILFSTQSMDEADILADRKVI 686
Cdd:TIGR01257 2066 RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWntivSIIREGRA---VVLTSHSMEECEALCTRLAI 2142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 687 MSNGRLKCAGSSIFLKRRWGLGYHLSLhrnEICNPEQ--------ITSFITHHIPDAKLKTKNKEKLVYTLPLER-TNIF 757
Cdd:TIGR01257 2143 MVKGAFQCLGTIQHLKSKFGDGYIVTM---KIKSPKDdllpdlnpVEQFFQGNFPGSVQRERHYNMLQFQVSSSSlARIF 2219
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622880985 758 PDLFSNLDKCSdqgVTGYDISMSTLNEIFMKLEGQSTTKQDF 799
Cdd:TIGR01257 2220 QLLISHKDSLL---IEEYSVTQTTLDQVFVNFAKQQTETYDL 2258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1278-1492 |
7.45e-39 |
|
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: 145.55 E-value: 7.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1278 IIASCLHKEYA---------GQKKSCFSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL 1347
Cdd:cd03267 1 IEVSNLSKSYRvyskepgliGSLKSLFKRKYREVEAlKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1348 KG-------------CSSVLGhlgycpQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKL 1414
Cdd:cd03267 81 AGlvpwkrrkkflrrIGVVFG------QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1415 TTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
479-749 |
1.04e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 146.44 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEY-KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL--SEMQDLEEI 555
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 RKITGVCPQF--------NVQFDILTVKENLslfakikGIHPQEVEQEVQRILlelDMQNIQDNLAKH----LSEGQKRK 623
Cdd:TIGR04521 81 RKKVGLVFQFpehqlfeeTVYKDIAFGPKNL-------GLSEEEAEERVKEAL---ELVGLDEEYLERspfeLSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 624 ltfgIAILG----DPQILLLDEPTTGLDPFSRDQVWSLLRE-HRA-DHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:TIGR04521 151 ----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 698 S--IFLKRRWGLGYHLSLhrneicnPeQITSFIThhipdaKLKTKNKE--KLVYTL 749
Cdd:TIGR04521 227 PreVFSDVDELEKIGLDV-------P-EITELAR------KLKEKGLPvpKDPLTV 268
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
498-644 |
1.53e-38 |
|
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: 141.25 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSeMQDLEEIRKITGVCPQFNVQFDILTVKEN 577
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 578 LSLFAKIKGIHPQEVEQEVQRILLELDMQNI----QDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTT 644
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
478-786 |
4.88e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 145.25 E-value: 4.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLsemqDLEEIRK 557
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 I------TGVCPQfnvqfdiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAIL 631
Cdd:COG4152 73 IgylpeeRGLYPK-------MKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 632 GDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGSSIFLKRRWGlgyh 710
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTtVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG---- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 711 lslHRNEICNPEQITSFItHHIPDAKLKTKNKEKLVYTLPLERTNifPDLFSNLdkcSDQG-VTGYDISMSTLNEIF 786
Cdd:COG4152 222 ---RNTLRLEADGDAGWL-RALPGVTVVEEDGDGAELKLEDGADA--QELLRAL---LARGpVREFEEVRPSLNEIF 289
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
478-693 |
5.09e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 143.69 E-value: 5.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsemqDLEEIRK 557
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK------PVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLtfGIA--ILGDPQ 635
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV--AIAraLANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 636 ILLLDEPTTGLDPFSRDQVWSLLRE-HRADHV-ILFSTQSMDEADILADRKVIMSN--GRLK 693
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRlWQETGKtVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
479-700 |
7.06e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 143.72 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVC---P--QF---NVQFDILTVKENLslfakikGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKltfgIAI 630
Cdd:TIGR04520 79 VGMVfqnPdnQFvgaTVEDDVAFGLENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR----VAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 631 LG----DPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEAdILADRKVIMSNGRLKCAGS--SIF 700
Cdd:TIGR04520 148 AGvlamRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMNKGKIVAEGTprEIF 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
479-696 |
9.18e-38 |
|
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: 141.26 E-value: 9.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqdleEIRKI 558
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAG 696
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKtVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
480-691 |
3.25e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 480 RIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKIT 559
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-PLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 560 GVCPQfnvqfdiltvkenlslfakikgihpqeveqevqrilleldmqniqdnlakhLSEGQKRKLTFGIAILGDPQILLL 639
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 640 DEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGR 691
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1301-1591 |
3.93e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 142.64 E-value: 3.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1301 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGH-------LGYCPQENVLWPMLTAR 1373
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRarharqrVGVVPQFDNLDPDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1453
Cdd:PRK13537 99 ENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1454 QAIQAVVKnteRG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL-KNKLGKDYIlelKVKEPSQVTLVHTeilk 1530
Cdd:PRK13537 179 ERLRSLLA---RGktILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCDVI---EIYGPDPVALRDE---- 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1531 LFPQAAGQE-RYSSLLTYklpVADVYPLSQAFHKLEAVKhnfnleeYSLSQCTLEKVFLELS 1591
Cdd:PRK13537 249 LAPLAERTEiSGETLFCY---VRDPEPLHARLKGRAGLR-------YLHRPANLEDVFLRLT 300
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
479-691 |
4.03e-37 |
|
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: 137.90 E-value: 4.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 558
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDiLTVKENLslfakikgihpqeveqevqrilleldmqniqdnlakhLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03228 78 IAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADiLADRKVIMSNGR 691
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
479-692 |
6.45e-37 |
|
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: 139.56 E-value: 6.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEIR 556
Cdd:cd03261 1 IELRGLTKSFGGR--TV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQFNVQFDILTVKENLSLFAKikgIHPQEVEQEVQRILLE-LDMQNI---QDNLAKHLSEGQKRKLTFGIAILG 632
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLR---EHTRLSEEEIREIVLEkLEAVGLrgaEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 633 DPQILLLDEPTTGLDPFSRDQVWSLLREHRA--DHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1306-1599 |
1.28e-36 |
|
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: 152.48 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFcvQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHLGYCPQENVLWPMLTAREHLEVY 1379
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1380 AAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIqaV 1459
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--L 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1460 VKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYILEL-------------------------K 1514
Cdd:TIGR01257 1106 KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrkmkniqsqrggcegtcsctskgfS 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1515 VKEPSQVTLVHTE-------------ILKLFPQAAGQERYSSLLTYKLPVADVYPLSQA--FHKLEAVKHNFNLEEYSLS 1579
Cdd:TIGR01257 1186 TRCPARVDEITPEqvldgdvnelmdlVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYAslFRELEETLADLGLSSFGIS 1265
|
330 340
....*....|....*....|
gi 1622880985 1580 QCTLEKVFLELSKEQEVGNF 1599
Cdd:TIGR01257 1266 DTPLEEIFLKVTEDADSGSL 1285
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
479-692 |
2.19e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 141.37 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIR 556
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALseRELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQfnvQFDIL---TVKENLSLFAKIKGIHPQEVEQEVQRiLLEL-DMQNIQDNLAKHLSEGQKRKLtfGIA--I 630
Cdd:COG1135 82 RKIGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRKRVAE-LLELvGLSDKADAYPSQLSGGQKQRV--GIAraL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 631 LGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
479-692 |
3.77e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGkveaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 558
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDiLTVKENLSLFAKIKGIHPQEveQEVQRILLELDMQniQDNLAK---HLSEGQKRKLTFGIAILGDPQ 635
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLP--PDILDKpveRLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 636 ILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
479-692 |
1.20e-35 |
|
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: 135.34 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemqDLEEIRKI 558
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLRE-HRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03259 154 LDEPLSALDAKLREELREELKElQRELGItTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
479-691 |
4.36e-35 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 132.31 E-value: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIR 556
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQFNVqFDILTVKENLSLfakikgihpqeveqevqrilleldmqniqdnlakHLSEGQKRKLTFGIAILGDPQI 636
Cdd:cd03229 77 RIGMVFQDFAL-FPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGR 691
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1305-1503 |
4.62e-35 |
|
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: 134.10 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLGH------LGYCPQENVLWPMLTAREHL 1376
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrdITGLPPHeraragIGYVPEGRRIFPELTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1377 EVYAAVKGLRKVDARLAitRLVSAF-KLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1455
Cdd:cd03224 97 LLGAYARRRAKRKARLE--RVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622880985 1456 IQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1503
Cdd:cd03224 175 IRE-LRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1286-1491 |
4.76e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 137.65 E-value: 4.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1286 EYAGQKKScfskRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcsSVLG---------- 1355
Cdd:PRK13536 43 DLAGVSKS----YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI------TVLGvpvpararla 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1356 --HLGYCPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSP 1433
Cdd:PRK13536 113 raRIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1434 VLLLDEPSTGIDPTGQQQMWQAIQAVVKnteRG--VLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLA---RGktILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
478-691 |
6.09e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 137.27 E-value: 6.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRK 557
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA--RA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQIL 637
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 638 LLDEPTTGLDPFSRDQVWSLLREHRA-DHVILFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
479-692 |
1.29e-34 |
|
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: 133.19 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 558
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRI--LLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQI 636
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELlaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWS-LLREHRADH-VILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEeFKRLQQELGkTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
476-692 |
8.52e-34 |
|
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: 130.92 E-value: 8.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 476 KEAIRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIyNKNLSEMQDLEEI 555
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-AGLVPWKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 RKITGVCPQFN-VQFDiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDP 634
Cdd:cd03267 94 RRIGVVFGQKTqLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 635 QILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
478-697 |
1.13e-33 |
|
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: 130.48 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEI 555
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 RKITGVCPQFNVQFDILTVKENLSLFAKI-KGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLtfGIA--ILG 632
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRV--ALAraLAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 633 DPQILLLDEPTTGLDPFSRDQVWSLLREHRADH-----VIlfsTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsvVV---THDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
478-691 |
1.27e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 132.62 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRk 557
Cdd:PRK13537 7 PIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 iTGVCPQF-NVQFDiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQI 636
Cdd:PRK13537 82 -VGVVPQFdNLDPD-FTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWSLLREHRA-DHVILFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
467-698 |
1.49e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 137.34 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 467 EPVAPEFQGKEAIRIRNVKKEYKGKS-GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKN 545
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 546 LSEM--QDLEEIRKITGVCPQF-NVQFD-ILTVKENLSLFAKIKGIHP-QEVEQEVQRIL----LELDMqniqdnLAKH- 615
Cdd:COG1123 329 LTKLsrRSLRELRRRVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLLSrAERRERVAELLervgLPPDL------ADRYp 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 616 --LSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHV--ILFSTQSMDEADILADRKVIMSNGR 691
Cdd:COG1123 403 heLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGltYLFISHDLAVVRYIADRVAVMYDGR 482
|
....*..
gi 1622880985 692 LKCAGSS 698
Cdd:COG1123 483 IVEDGPT 489
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
478-697 |
2.03e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.96 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPT---EGSVTIYNKNLSEMQDLEE 554
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 555 IRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDP 634
Cdd:COG1123 82 GRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 635 QILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
482-692 |
2.19e-33 |
|
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: 128.05 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 482 RNVKKEYKGKSGKVEA--LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL--SVPTEGSVTIYNKNLsemqDLEEIRK 557
Cdd:cd03213 7 RNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL----DKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNVQFDILTVKENLSLFAKIKGIhpqeveqevqrilleldmqniqdnlakhlSEGQKRKLTFGIAILGDPQIL 637
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 638 LLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFST-QSMDEADILADRKVIMSNGRL 692
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRtIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
479-691 |
4.14e-33 |
|
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: 128.32 E-value: 4.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGihPQEVEQEVQRIlLEL--DMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQI 636
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERV-YELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGR 691
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVtILLVEQNARFALEIADRAYVLERGR 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
451-711 |
4.90e-33 |
|
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: 136.82 E-value: 4.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 451 VIEKEIDAEHPSDDYFEPVAPefqgkeAIRIRNVKKEYKGksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG 530
Cdd:COG4987 312 LLDAPPAVTEPAEPAPAPGGP------SLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 531 LSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDIlTVKENLsLFAKikgihPQEVEQEVQRIL----LELDMQ 606
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDL-DEDDLRRRIAVVPQRPHLFDT-TLRENL-RLAR-----PDATDEELWAALervgLGDWLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 607 NIQDNL-------AKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADi 679
Cdd:COG4987 456 ALPDGLdtwlgegGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE- 534
|
250 260 270
....*....|....*....|....*....|..
gi 1622880985 680 LADRKVIMSNGRLKCAGSSIFLKRRWGLGYHL 711
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
479-692 |
5.32e-33 |
|
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: 128.39 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD--LEEIR 556
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQ-----FNvqfDILTVKEnlSLFAKIKGIHPQEVEQEVQRILLELDMQ-----NIQDNLAKHLSEGQKRKLTF 626
Cdd:cd03257 82 KEIQMVFQdpmssLN---PRMTIGE--QIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 627 GIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
479-692 |
5.98e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.86 E-value: 5.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDlEEI--- 555
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR-REIpyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 -RKItGVCPQ-FNVQFDiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLtfGI--AIL 631
Cdd:COG2884 78 rRRI-GVVFQdFRLLPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV--AIarALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 632 GDPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
478-692 |
1.36e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 127.87 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEI 555
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 RKITGVCPQfnvQFDI---LTVKEN--------LSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKL 624
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 625 tfGIA--ILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:COG3638 156 --AIAraLVQEPKLILADEPVASLDPKTARQVMDLLRRiAREDGItVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1305-1442 |
1.88e-32 |
|
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: 123.91 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMLTAREHLE 1377
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltddeRKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 1378 VYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTT----GTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1296-1497 |
3.29e-32 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 126.12 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---------SVLGhLGYCPQENV 1365
Cdd:cd03218 7 SKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrARLG-IGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1366 LWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGID 1445
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1446 PTGQQQmwqaIQAVVKN-TER--GVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:cd03218 166 PIAVQD----IQKIIKIlKDRgiGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1295-1496 |
3.33e-32 |
|
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: 125.32 E-value: 3.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSV---LGHLGYCPQENVLWP 1368
Cdd:cd03259 6 LSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdVTGVppeRRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLeVYA-AVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1447
Cdd:cd03259 86 HLTVAENI-AFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622880985 1448 GQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
478-697 |
5.10e-32 |
|
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: 126.31 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 557
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL-SRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFN-VQFDiLTVKENLSLfakikGIHP---------QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFG 627
Cdd:COG1120 76 RIAYVPQEPpAPFG-LTVRELVAL-----GRYPhlglfgrpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 628 IAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
478-704 |
1.74e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 125.23 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRK 557
Cdd:PRK13647 4 IIEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKltfgIAILG---- 632
Cdd:PRK13647 80 KVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR----VAIAGvlam 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 633 DPQILLLDEPTTGLDPFSRDQVWSLL-REHRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSIFLKRR 704
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
479-692 |
2.65e-31 |
|
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: 122.64 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS-EMQDLEEIRK 557
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITG-VCPQFNVqFDILTVKENLSL-FAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQ 635
Cdd:cd03262 77 KVGmVFQQFNL-FPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 636 ILLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
449-711 |
5.62e-31 |
|
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: 131.88 E-value: 5.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 449 NKVIEKEIdaEHPSDDYFEPVaPEFQGkeAIRIRNVKKEYKGKSgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNIL 528
Cdd:COG2274 449 DDILDLPP--EREEGRSKLSL-PRLKG--DIELENVSFRYPGDS--PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 529 NGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDIlTVKENLSLF------------AKIKGIHpqeveQEV 596
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQI-DPASLRRQIGVVLQDVFLFSG-TIRENITLGdpdatdeeiieaARLAGLH-----DFI 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 597 QRILLELDMQnIQDNlAKHLSEGQKRKLtfGIA--ILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSM 674
Cdd:COG2274 595 EALPMGYDTV-VGEG-GSNLSGGQRQRL--AIAraLLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL 670
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622880985 675 DEADiLADRKVIMSNGRLKCAGSSIFLKRRWGLGYHL 711
Cdd:COG2274 671 STIR-LADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1305-1500 |
6.30e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 6.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS--SVLGHLGYCPQ-ENVLW--PMlTARE----- 1374
Cdd:COG1121 23 EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprRARRRIGYVPQrAEVDWdfPI-TVRDvvlmg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 ---HLevyAAVKGLRKVDaRLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1451
Cdd:COG1121 102 rygRR---GLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622880985 1452 MWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVaIMVSGRLRCIGSIQH 1500
Cdd:COG1121 178 LYELLRELRRE-GKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
493-696 |
9.79e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.10 E-value: 9.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqdleeiRKITGVCPQ---FNVQF 569
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVPQrrsIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 570 DIlTVKE--NLSLFAKIKGIHP--QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTG 645
Cdd:cd03235 84 PI-SVRDvvLMGLYGHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 646 LDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRkVIMSNGRLKCAG 696
Cdd:cd03235 163 VDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
478-697 |
2.34e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdleeiRK 557
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVcPQ---FNVQFDIlTVKE--NLSLFAKIK--GIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAI 630
Cdd:COG1121 77 IGYV-PQraeVDWDFPI-TVRDvvLMGRYGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 631 LGDPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRkVIMSNGRLKCAGS 697
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGP 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1297-1496 |
2.42e-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: 120.33 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1297 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLGhLGYCPQenvlwPMLTAREH 1375
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrVSSLLG-LGGGFN-----PELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1376 LEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEP-STGiDPTGQQQMWQ 1454
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 1455 AIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:cd03220 184 RLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
479-692 |
3.15e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.76 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIR 556
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQfnvQFDIL---TVKENLSLFAKIKGIHPQEVEQEVQRiLLEL-DMQNIQDNLAKHLSEGQKRKLtfGIA--I 630
Cdd:PRK11153 82 RQIGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKARVTE-LLELvGLSDKADRYPAQLSGGQKQRV--AIAraL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 631 LGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
478-697 |
3.51e-30 |
|
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: 120.52 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEiRK 557
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-PVQE-RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ItGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRI---LLEL-DMQNIQDNLAKHLSEGQKRKLTFGIAILGD 633
Cdd:cd03296 76 V-GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKvheLLKLvQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 634 PQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1296-1498 |
4.18e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 120.57 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLGH-LGYCPQenvlwpmLTAR 1373
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrVSALLELgAGFHPE-------LTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHLEVYAAVKGLRKVDARlAITRLVSAF-KLHEQLNVPVQKLTTGtMR-KLCFVLSLLGNSPVLLLDEP-STGiDPTGQQ 1450
Cdd:COG1134 107 ENIYLNGRLLGLSRKEID-EKFDEIVEFaELGDFIDQPVKTYSSG-MRaRLAFAVATAVDPDILLVDEVlAVG-DAAFQK 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622880985 1451 QMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSI 1498
Cdd:COG1134 184 KCLARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1296-1503 |
4.80e-30 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 120.07 E-value: 4.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---------SVLGhLGYCPQENV 1365
Cdd:TIGR04406 8 IKSyKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDithlpmherARLG-IGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1366 LWPMLTAREHLEvyaAVKGLRKVDARLAITR----LVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPS 1441
Cdd:TIGR04406 87 IFRKLTVEENIM---AVLEIRKDLDRAEREErleaLLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1442 TGIDPTGQQQmwqaIQAVVKN-TER--GVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1503
Cdd:TIGR04406 164 AGVDPIAVGD----IKKIIKHlKERgiGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
474-692 |
5.00e-30 |
|
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: 120.83 E-value: 5.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 474 QGKEAIRIR---NVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM- 549
Cdd:cd03294 13 NPQKAFKLLakgKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMs 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 550 -QDLEEIR--KITGVCPQFNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF 626
Cdd:cd03294 93 rKELRELRrkKISMVFQSFAL-LPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 627 GIAILGDPQILLLDEPTTGLDPFSR----DQVWSLLREHRadHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRremqDELLRLQAELQ--KTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1305-1503 |
5.62e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 119.70 E-value: 5.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGH---------LGYCPQENVLWPMLTAREH 1375
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG-EDITGLpphriarlgIGYVPEGRRIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1376 LEVYA-AVKGLRKVDARLAitRLVSAF-KLHEQLNVPVqklttGTmrklcfvLS------------LLGNSPVLLLDEPS 1441
Cdd:COG0410 99 LLLGAyARRDRAEVRADLE--RVYELFpRLKERRRQRA-----GT-------LSggeqqmlaigraLMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVVkntERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1503
Cdd:COG0410 165 LGLAPLIVEEIFEIIRRLN---REGvtILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
479-692 |
7.62e-30 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 118.51 E-value: 7.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsEMQDLE-EIRK 557
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPpKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQIL 637
Cdd:cd03301 74 IAMVFQNYAL-YPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 638 LLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
479-697 |
8.77e-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: 119.08 E-value: 8.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKi 558
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 tGVCPQF-NVQ-FDILTVKENLSLFAKIKGIHP----------QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF 626
Cdd:cd03219 76 -GIGRTFqIPRlFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 627 GIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
478-697 |
1.65e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRK 557
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQI 636
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWSLLREHR--ADHVILFSTQSMDEAdILADRKVIMSNGRLKCAGS 697
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1297-1491 |
1.73e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 115.42 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1297 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQenvlwpm 1369
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdiaklplEELRRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1370 ltarehlevyaavkglrkvdarlaitrlvsafklheqlnvpvqkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1449
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 1450 QQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:cd00267 117 ERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1303-1492 |
2.05e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 118.60 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG-------HLG----YcpQENVLWPMLT 1371
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG-RDITGlpphriaRLGiartF--QNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREHLEV----------YAAVKGLRKVDARLAITR-----LVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLL 1436
Cdd:COG0411 96 VLENVLVaaharlgrglLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1437 LDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
402-697 |
2.21e-29 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 125.26 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 402 SILLLDGFIYLLLAlyfdkilpygderrysPLFFL---NSSSCFqHQGTDNK----VIEKEIDAEHPSDDYFEPVAPeFQ 474
Cdd:COG4988 271 SLTLFAALFVLLLA----------------PEFFLplrDLGSFY-HARANGIaaaeKIFALLDAPEPAAPAGTAPLP-AA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 475 GKEAIRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEE 554
Cdd:COG4988 333 GPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL-DPAS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 555 IRKITGVCPQFNVQFDiLTVKENLSLFAkikgihPQEVEQEVQRIL-----------LE--LDMQnIQDNlAKHLSEGQK 621
Cdd:COG4988 409 WRRQIAWVPQNPYLFA-GTIRENLRLGR------PDASDEELEAALeaagldefvaaLPdgLDTP-LGEG-GRGLSGGQA 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 622 RKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADiLADRKVIMSNGRLKCAGS 697
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGT 554
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1303-1503 |
2.72e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 117.92 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---------------------CSSVLGHLGycP 1361
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrtfqIPRLFPELT--V 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1362 QENVlwpMLTAREHLEVYAAVKGLRKVDARL--AITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDE 1439
Cdd:cd03219 93 LENV---MVAAQARTGSGLLLARARREEREAreRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1440 PSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1503
Cdd:cd03219 170 PAAGLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1276-1497 |
3.46e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.44 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1276 PVIIASCLHKEYagqkkscfskrKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSV-- 1353
Cdd:COG1137 2 MTLEAENLVKSY-----------GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG-EDIth 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1354 --------LGhLGYCPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFV 1425
Cdd:COG1137 70 lpmhkrarLG-IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1426 LSLLGNSPVLLLDEPSTGIDPTGQQQmwqaIQAVVKN-TER--GVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVAD----IQKIIRHlKERgiGVLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1295-1491 |
3.97e-29 |
|
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: 115.36 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---------CSSVLGHLGYCPQEN 1364
Cdd:cd03229 6 VSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledeLPPLRRRIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1365 VLWPMLTAREHLeVYAAVKGLRKvdaRLAITRlvsafklheqlnvpvqklttgtmrklcfvlSLLGNSPVLLLDEPSTGI 1444
Cdd:cd03229 86 ALFPHLTVLENI-ALGLSGGQQQ---RVALAR------------------------------ALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622880985 1445 DPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
478-692 |
6.58e-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: 120.20 E-value: 6.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNlsemqdleeirk 557
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQ-------FnvQ----FDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQK----- 621
Cdd:COG3842 69 VTGLPPEkrnvgmvF--QdyalFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrval 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 622 -RkltfgiAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:COG3842 147 aR------ALAPEPRVLLLDEPLSALDAKLREEMREELRRlQRELGItFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
479-692 |
8.02e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.49 E-value: 8.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS-EMQDLEEIRK 557
Cdd:PRK13639 2 LETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKltfgIAILG---- 632
Cdd:PRK13639 79 TVGIVFQNpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR----VAIAGilam 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 633 DPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1297-1491 |
1.19e-28 |
|
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: 115.26 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1297 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------SVLGHLGYCPQEnvlwP- 1368
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkELRRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 ----MLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGI 1444
Cdd:cd03225 86 dqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622880985 1445 DPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:cd03225 166 DPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1294-1499 |
2.05e-28 |
|
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: 115.12 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1294 CFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQ--EN 1364
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlRELRRKVGLVFQnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1365 VLWpMLTAREhlEV-YAAV-KGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCF--VLSLlgNSPVLLLDEP 1440
Cdd:COG1122 87 QLF-APTVEE--DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLVLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVvKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1499
Cdd:COG1122 162 TAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1278-1491 |
2.22e-28 |
|
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: 114.49 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1278 IIASCLHKEYAGqkkscfsKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLG 1355
Cdd:cd03293 1 LEVRNVSKTYGG-------GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1356 HLGYCPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLN-VPVQkLTTGtMRK-LCFVLSLLGNSP 1433
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENaYPHQ-LSGG-MRQrVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1434 VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMvSGR 1491
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1306-1496 |
2.27e-28 |
|
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: 114.31 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVqEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC---SSVLG--------HLGYCPQENVLWPMLTARE 1374
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKinlppqqrKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HLEvYAAVKGLRKVDaRLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQ 1454
Cdd:cd03297 95 NLA-FGLKRKRNRED-RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 1455 AIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
493-677 |
2.64e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 113.29 E-value: 2.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS-EMQDLEEIRKITGVCPQfNVQFDI 571
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDySRKGLLERRQRVGLVFQ-DPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 572 L--TVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPF 649
Cdd:TIGR01166 82 FaaDVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180 190
....*....|....*....|....*....|
gi 1622880985 650 SRDQVWSLLREHRAD--HVIlFSTQSMDEA 677
Cdd:TIGR01166 162 GREQMLAILRRLRAEgmTVV-ISTHDVDLA 190
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1283-1492 |
2.64e-28 |
|
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: 114.51 E-value: 2.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1283 LHKEYAGQKKscfskrkKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLG------ 1355
Cdd:cd03255 6 LSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiSKLSekelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1356 ----HLGYCPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGN 1431
Cdd:cd03255 79 frrrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1432 SPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLaEAEALCDRVAIMVSGRL 1492
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
480-696 |
2.76e-28 |
|
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: 112.91 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 480 RIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKIT 559
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-SPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 560 GVCPQfnvqfdiltvkenlslfakikgihpqeveqevqrILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLL 639
Cdd:cd03214 76 AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 640 DEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAG 696
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
479-697 |
3.46e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.30 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEY-KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ-DLEEIR 556
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRI--LLELDMQNIQDNLAKHLSEGQKRKltfgIAILG- 632
Cdd:PRK13637 83 KKVGLVFQYpEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRR----VAIAGv 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 633 ---DPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK13637 159 vamEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1301-1496 |
3.49e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 113.78 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1301 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLGHLGYCPQ-ENVLWPM-LTARE-- 1374
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkpLEKERKRIGYVPQrRSIDRDFpISVRDvv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 ------HLEvyaAVKGLRKVDARLAITRL--VSAFKLHEQlnvPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDP 1446
Cdd:cd03235 92 lmglygHKG---LFRRLSKADKAKVDEALerVGLSELADR---QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1447 TGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVaIMVSGRLRCIG 1496
Cdd:cd03235 166 KTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
480-693 |
3.59e-28 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 113.51 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 480 RIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqdlEEIRKIT 559
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 560 GVCPQfNVQFDIL--TVKENLSLFAKIKGIHPQEVEQevqrILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQIL 637
Cdd:cd03226 74 GYVMQ-DVDYQLFtdSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 638 LLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRLK 693
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
478-692 |
3.82e-28 |
|
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: 113.84 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKsgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 557
Cdd:cd03245 2 RIEFRNVSFSYPNQ--EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQfNVQFDILTVKENLSLFAkikgihpQEVEQEvqRILLELDMQNIQDNLAKH--------------LSEGQKRK 623
Cdd:cd03245 79 NIGYVPQ-DVTLFYGTLRDNITLGA-------PLADDE--RILRAAELAGVTDFVNKHpngldlqigergrgLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 624 LTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFST--QSMDEadiLADRKVIMSNGRL 692
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIThrPSLLD---LVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
476-700 |
4.34e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.50 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 476 KEAIRIRNVKKEYKGKSGKveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEI 555
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE-ETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 RKITGVCPQfNV--QFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKltfgIAILG- 632
Cdd:PRK13635 80 RRQVGMVFQ-NPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQR----VAIAGv 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 633 ---DPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVI--LFSTQSMDEAdILADRKVIMSNGRLKCAG--SSIF 700
Cdd:PRK13635 155 lalQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItvLSITHDLDEA-AQADRVIVMNKGEILEEGtpEEIF 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
479-697 |
4.64e-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: 114.26 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNlsemqdleeirkI 558
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD------------I 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCP---QFNVQFDI------LTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIA 629
Cdd:cd03300 65 TNLPPhkrPVNTVFQNyalfphLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQvwsLLREHRADH-----VILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKD---MQLELKRLQkelgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
483-692 |
7.24e-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: 113.52 E-value: 7.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 483 NVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLsVP----TEGSVTIYNKNLSEmqdlEEIRKI 558
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEgggtTSGQILFNGQPRKP----DQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKG--IHPQEVEQEVQRILLELDMQN--IQDNLAKHLSEGQKRKLTFGIAILGDP 634
Cdd:cd03234 83 VAYVRQDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRDLALtrIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 635 QILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQlaRRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1298-1497 |
7.45e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 113.99 E-value: 7.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLG---------HLGYCPQENVLWP 1368
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD--LAslsrrelarRIAYVPQEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTARE--------HLevyAAVKGLRKVDaRLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEP 1440
Cdd:COG1120 89 GLTVRElvalgrypHL---GLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:COG1120 165 TSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
493-698 |
9.97e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 113.15 E-value: 9.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEI-RKitGV--CPQF-NVq 568
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIaRL--GIgyVPEGrRI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 569 FDILTVKENLSLFAKIKGiHPQEVEQEVQRILlEL-----DMQNiqdNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPT 643
Cdd:COG0410 90 FPSLTVEENLLLGAYARR-DRAEVRADLERVY-ELfprlkERRR---QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 644 TGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGSS 698
Cdd:COG0410 165 LGLAPLIVEEIFEIIRRLNREGVtILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
508-696 |
1.32e-27 |
|
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: 112.20 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 508 GQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRKITGVCPQFNVqFDILTVKENLSLfAKIKGI 587
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNL-FAHLTVEQNVGL-GLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 588 HPQEVEQE-VQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH- 665
Cdd:cd03298 100 KLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETk 179
|
170 180 190
....*....|....*....|....*....|..
gi 1622880985 666 -VILFSTQSMDEADILADRKVIMSNGRLKCAG 696
Cdd:cd03298 180 mTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
478-692 |
1.67e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.80 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI------YNKNLSEMQD 551
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 552 LEEIRKITGVCPQFNVqFDILTVKENLsLFAKIK--GIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIA 629
Cdd:COG4161 78 RLLRQKVGMVFQQYNL-WPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRA---DHVILfsTQSMDEADILADRKVIMSNGRL 692
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIV--THEVEFARKVASQVVYMEKGRI 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
479-648 |
2.25e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 112.39 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM-QDLEEIRK 557
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITG-VCPQFNVqFDILTVKENLSLfA--KIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQK-RkltfgIAI--- 630
Cdd:COG1126 78 KVGmVFQQFNL-FPHLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQqR-----VAIara 150
|
170
....*....|....*....
gi 1622880985 631 LG-DPQILLLDEPTTGLDP 648
Cdd:COG1126 151 LAmEPKVMLFDEPTSALDP 169
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
477-696 |
2.45e-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: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 477 EAIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEG-SVTIYNKNLSEMqDLEEI 555
Cdd:COG1119 2 PLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGE-DVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 RKITG-VCPQFNVQFDI-LTVKEN-LS-LFAKIkGIHPQ---EVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGI 628
Cdd:COG1119 77 RKRIGlVSPALQLRFPRdETVLDVvLSgFFDSI-GLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEadILA--DRKVIMSNGRLKCAG 696
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
479-692 |
3.25e-27 |
|
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: 111.47 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEY------------------KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT 540
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 541 IYNKnlsemqdleeirkitgVCP--QFNVQFD-ILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLS 617
Cdd:cd03220 81 VRGR----------------VSSllGLGGGFNpELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 618 EGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVIL-FSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTViLVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
479-691 |
3.30e-27 |
|
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: 111.89 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEIR 556
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQfnvQFDI---LTVKEN--------LSLFAKIKGIHPqevEQEVQRILLELDMQNIQDNL---AKHLSEGQKR 622
Cdd:cd03256 78 RQIGMIFQ---QFNLierLSVLENvlsgrlgrRSTWRSLFGLFP---KEEKQRALAALERVGLLDKAyqrADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 623 KLtfGIA--ILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGR 691
Cdd:cd03256 152 RV--AIAraLMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1295-1492 |
3.40e-27 |
|
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: 111.44 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG-----------HLGYCPQ 1362
Cdd:cd03257 11 FPTGGGSVKAlDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDG-KDLLKlsrrlrkirrkEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1363 E--NVLWPMLTAREHL-EVYAAVKGLRKVDARLAITRLV-SAFKLHEQL--NVPVQkLTTGTMRKLCFVLSLLGNSPVLL 1436
Cdd:cd03257 90 DpmSSLNPRMTIGEQIaEPLRIHGKLSKKEARKEAVLLLlVGVGLPEEVlnRYPHE-LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1437 LDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
478-729 |
6.26e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 113.26 E-value: 6.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYK------GKSG-----------KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT 540
Cdd:COG4586 1 IIEVENLSKTYRvyekepGLKGalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 541 IYNKNLSEmQDLEEIRKITGVCPQFNvQ--FDiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSE 618
Cdd:COG4586 81 VLGYVPFK-RRKEFARRIGVVFGQRS-QlwWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 619 GQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH---VILfsTqSMDEADI--LADRKVIMSNGRLK 693
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgttILL--T-SHDMDDIeaLCDRVIVIDHGRII 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622880985 694 CAGSSIFLKRRWGLGYHLSLHRNEICNPEQITSFIT 729
Cdd:COG4586 235 YDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE 270
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1275-1491 |
8.09e-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: 111.33 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1275 KPVIIASCLHKEYAgqkkscfSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVL 1354
Cdd:COG1116 5 APALELRGVSKRFP-------TGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1355 G---HLGYCPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLheqlnvpvqkltTGTMRKLCFVLS---- 1427
Cdd:COG1116 77 GpgpDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGL------------AGFEDAYPHQLSggmr 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1428 --------LLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMvSGR 1491
Cdd:COG1116 145 qrvaiaraLANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL-SAR 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
478-697 |
8.22e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.15 E-value: 8.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYK-GKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYN---KNLSEMQDLE 553
Cdd:PRK13649 2 GINLQNVSYTYQaGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtliTSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 554 EIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRillELDMQNIQDNLAK----HLSEGQKRKltfgI 628
Cdd:PRK13649 82 QIRKKVGLVFQFpESQLFEETVLKDVAFGPQNFGVSQEEAEALARE---KLALVGISESLFEknpfELSGGQMRR----V 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 629 AILG----DPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK13649 155 AIAGilamEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
480-692 |
9.01e-27 |
|
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: 111.28 E-value: 9.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 480 RIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDleeiRKIT 559
Cdd:COG0411 6 EVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP----HRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 560 --GVCPQF-NVQ-FDILTVKENL----------SLFAKIKGIHP-----QEVEQEVQRILLELDMQNIQDNLAKHLSEGQ 620
Cdd:COG0411 78 rlGIARTFqNPRlFPELTVLENVlvaaharlgrGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 621 KRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH---VILFstqsmdEADI-----LADRKVIMSNGRL 692
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgitILLI------EHDMdlvmgLADRIVVLDFGRV 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
478-692 |
1.09e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.49 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK--NLSEMQDLEEI 555
Cdd:PRK11124 2 SIQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 R----KITGVCPQFNVqFDILTVKENLsLFA--KIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIA 629
Cdd:PRK11124 78 RelrrNVGMVFQQYNL-WPHLTVQQNL-IEApcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH---VILfsTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGitqVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
479-692 |
1.43e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.42 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD--LEEIR 556
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQI 636
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
479-698 |
1.74e-26 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 109.55 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGSS 698
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
479-692 |
2.03e-26 |
|
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: 107.13 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsemqdleeirki 558
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 tgvcpqfnvQFDILTVKEnlSLFAKIKGIHpQeveqevqrilleldmqniqdnlakhLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03216 63 ---------EVSFASPRD--ARRAGIAMVY-Q-------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
479-713 |
2.11e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.88 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSG-KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS---EMQDLEE 554
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 555 IRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQniQDNLAK---HLSEGQKRKltfgIAI 630
Cdd:PRK13634 83 LRKKVGIVFQFpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP--EELLARspfELSGGQMRR----VAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 631 LG----DPQILLLDEPTTGLDPFSR----DQVWSLLREHraDHVILFSTQSMDEADILADRKVIMSNGRLKCAGS--SIF 700
Cdd:PRK13634 157 AGvlamEPEVLVLDEPTAGLDPKGRkemmEMFYKLHKEK--GLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIF 234
|
250
....*....|...
gi 1622880985 701 LKRRWGLGYHLSL 713
Cdd:PRK13634 235 ADPDELEAIGLDL 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1298-1480 |
2.12e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 108.42 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLG----YCPQENVLWPMLTAR 1373
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHLEVYAAVKGlrkvDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1453
Cdd:PRK13539 92 ENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170 180 190
....*....|....*....|....*....|..
gi 1622880985 1454 QAIQAvvkNTERG--VLLTTHN---LAEAEAL 1480
Cdd:PRK13539 168 ELIRA---HLAQGgiVIAATHIplgLPGAREL 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
478-706 |
2.74e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 117.53 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEirk 557
Cdd:NF033858 1 VARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 itgVCPQF---------NVQFDiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGI 628
Cdd:NF033858 74 ---VCPRIaympqglgkNLYPT-LSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSL---LREHRADHVILFSTQSMDEADILaDRKVIMSNGRLKCAGSSIFLKRRW 705
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELidrIRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLART 228
|
.
gi 1622880985 706 G 706
Cdd:NF033858 229 G 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
478-712 |
2.78e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.69 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYK-GKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM---QDLE 553
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 554 EIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELdmqNIQDNLAKH----LSEGQKRKLTFGI 628
Cdd:PRK13641 82 KLRKKVSLVFQFpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV---GLSEDLISKspfeLSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSLLREH-RADHVILFSTQSMDEADILADRKVIMSNGRL--KCAGSSIFLKRRW 705
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEW 238
|
....*..
gi 1622880985 706 GLGYHLS 712
Cdd:PRK13641 239 LKKHYLD 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
475-697 |
4.02e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 475 GKEAIRIRNVKKEYKGKSGKVE--ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDL 552
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 553 EEIRKITGVCPQfN---------VQFDILTVKENLslfakikGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRK 623
Cdd:PRK13633 81 WDIRNKAGMVFQ-NpdnqivatiVEEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 624 ltfgIAILG----DPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEAdILADRKVIMSNGRLKCAGS 697
Cdd:PRK13633 153 ----VAIAGilamRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
470-692 |
5.00e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.97 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 470 APEFQGKEAIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS--VP---TEGSVTIYNK 544
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 545 NLSEMQ-DLEEIRKITGVCPQ----FNvqfdiLTVKENLSLFAKIKGIHP-QEVEQEVQRILLELDMQN-IQDNL---AK 614
Cdd:COG1117 79 DIYDPDvDVVELRRRVGMVFQkpnpFP-----KSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAALWDeVKDRLkksAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 615 HLSEGQKRKLTfgIA--ILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:COG1117 154 GLSGGQQQRLC--IAraLAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
479-692 |
7.97e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 108.15 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEIR 556
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITG-VCPQFNVqFDILTVKEN-----LSLFAKIKGIHPQEVEQEVQRILLELDMQNIQD---NLAKHLSEGQKRKLTFG 627
Cdd:TIGR02315 79 RRIGmIFQHYNL-IERLTVLENvlhgrLGYKPTWRSLLGRFSEEDKERALSALERVGLADkayQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 628 IAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
503-696 |
8.37e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 107.00 E-value: 8.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIyEGQITAILGHSGAGKSSLLNILNGLSVPTEGSV----TIY-----NKNLSEMQdleeiRKItGVCPQFNVQFDILT 573
Cdd:cd03297 19 FDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLfdsrkKINLPPQQ-----RKI-GLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 574 VKENLsLFAkIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQ 653
Cdd:cd03297 92 VRENL-AFG-LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 654 VWSLLREHRADHVI--LFSTQSMDEADILADRKVIMSNGRLKCAG 696
Cdd:cd03297 170 LLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
479-713 |
8.45e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.10 E-value: 8.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEY-KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSV-----TIYNKnlSEMQDL 552
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvddiTITHK--TKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 553 EEIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDM-QNIQDNLAKHLSEGQKRKLTFgIAI 630
Cdd:PRK13646 81 RPVRKRIGMVFQFpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAI-VSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 631 LG-DPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRL--KCAGSSIFLKRRW 705
Cdd:PRK13646 160 LAmNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKK 239
|
....*...
gi 1622880985 706 GLGYHLSL 713
Cdd:PRK13646 240 LADWHIGL 247
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
479-696 |
1.02e-25 |
|
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: 105.47 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDleEIRKI 558
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQfnvqfdiltvkeNLSLFAkikgihpqeveqevqrilleldmQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03247 77 ISVLNQ------------RPYLFD-----------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHVILFST---QSMDEadilADRKVIMSNGRLKCAG 696
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWIThhlTGIEH----MDKILFLENGKIIMQG 178
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
479-692 |
1.66e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.89 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:PRK11614 6 LSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSL---FAKikgihPQEVEQEVQRI------LLELDMQNiqdnlAKHLSEGQKRKLTFGIA 629
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMggfFAE-----RDQFQERIKWVyelfprLHERRIQR-----AGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFST-QSMDEADILADRKVIMSNGRL 692
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
496-715 |
1.84e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 496 EALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS-EMQDLEEIRKITGVCPQF-NVQFDILT 573
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLRESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 574 VKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQ 653
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 654 VWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAG--SSIFLKRRWGLGYHLSLHR 715
Cdd:PRK13636 180 IMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLRLPR 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
493-692 |
3.54e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.40 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS-----VPTEGSVTIYNKNL-SEMQDLEEIRKITGVCPQFN 566
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSIVYNGHNIySPRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 567 VQFDiLTVKENLSLFAKIKGIHPQEV-EQEVQRILLELDMQN-IQDNL---AKHLSEGQKRKLTFGIAILGDPQILLLDE 641
Cdd:PRK14239 96 NPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDeVKDRLhdsALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 642 PTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
479-693 |
5.57e-25 |
|
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: 104.79 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 558
Cdd:TIGR03740 1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVqfdiLTVKENLSLFAKIKGIHpqevEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:TIGR03740 76 IESPPLYEN----LTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRLK 693
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
479-702 |
1.20e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 105.66 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 558
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQfNVQFDIL--TVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQI 636
Cdd:PRK13652 80 VGLVFQ-NPDDQIFspTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS--SIFLK 702
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQ 228
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
497-697 |
1.35e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 104.43 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 497 ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRkiTGVCPQF---NVqFDILT 573
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIAR--LGIGRKFqkpTV-FEELT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 574 VKENL------------SLFAKIKGihpqEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDE 641
Cdd:COG4674 102 VFENLelalkgdrgvfaSLFARLTA----EERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 642 PTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:COG4674 178 PVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
479-697 |
1.37e-24 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 103.73 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 558
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDiLTVKENLSLFakikGIHPQE----------VEQEVQRILLELDMQnIQDNlAKHLSEGQKRKLTFGI 628
Cdd:cd03244 80 ISIIPQDPVLFS-GTIRSNLDPF----GEYSDEelwqalervgLKEFVESLPGGLDTV-VEEG-GENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEadIL-ADRKVIMSNGRLKCAGS 697
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDT--IIdSDRILVLDKGRVVEFDS 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1275-1501 |
1.49e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 109.99 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1275 KPVIIASCLHKEYAGQKKScfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTA---GEVELKGCS 1351
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP---------AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1352 ------SVLG-HLGYCPQEnvlwPM-----LTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTM 1419
Cdd:COG1123 73 llelseALRGrRIGMVFQD----PMtqlnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1420 RKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1499
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
..
gi 1622880985 1500 HL 1501
Cdd:COG1123 229 EI 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
479-691 |
2.26e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.40 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKE-YKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRK 557
Cdd:COG1101 2 LELKNLSKTfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 I--------TGVCPQfnvqfdiLTVKENLSLFAK-------IKGIHPQEVEQEVQRI-LLELDMQNIQDNLAKHLSEGQK 621
Cdd:COG1101 82 IgrvfqdpmMGTAPS-------MTIEENLALAYRrgkrrglRRGLTKKRRELFRELLaTLGLGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 622 RKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVI--LFSTQSMDEADILADRKVIMSNGR 691
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLttLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1273-1501 |
3.22e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.84 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1273 DEKPVIIASCLHKEYAGqkkscfSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--- 1349
Cdd:COG1123 256 AAEPLLEVRNLSKRYPV------RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1350 -------CSSVLGHLGYCPQ--ENVLWPMLTAREHL-EVYAAVKGLRKVDARLAITRLVSAFKLHEQLnvpvqklttgtM 1419
Cdd:COG1123 330 tklsrrsLRELRRRVQMVFQdpYSSLNPRMTVGDIIaEPLRLHGLLSRAERRERVAELLERVGLPPDL-----------A 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1420 RKLCFVLS------------LLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIM 1487
Cdd:COG1123 399 DRYPHELSggqrqrvaiaraLALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVM 478
|
250
....*....|....
gi 1622880985 1488 VSGRLRCIGSIQHL 1501
Cdd:COG1123 479 YDGRIVEDGPTEEV 492
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1300-1496 |
7.19e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 100.20 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1300 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------SVLGHLGYCPQenVLwpmlta 1372
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkELARKIAYVPQ--AL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 rehlevyaavkglrkvdARLAITRLvsAFKlheqlnvPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQM 1452
Cdd:cd03214 83 -----------------ELLGLAHL--ADR-------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622880985 1453 WQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
478-702 |
1.02e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVP---TEGSVTIYNKNLSEmQDLEE 554
Cdd:PRK13640 5 IVEFKHVSFTYP--DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTA-KTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 555 IRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKltfgIAILG- 632
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR----VAIAGi 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 633 ---DPQILLLDEPTTGLDPFSRDQVWSLLREHRAD-HVILFS-TQSMDEADiLADRKVIMSNGRLKCAGS--SIFLK 702
Cdd:PRK13640 158 lavEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSpvEIFSK 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
479-696 |
1.10e-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: 101.64 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkveaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdlEEIRKI 558
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP--PEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 tGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03299 74 -SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAG 696
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
456-692 |
1.69e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 456 IDAEHPSDDYFEPVAPEfQGKEAIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPT 535
Cdd:COG1132 318 LDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 536 EGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDiLTVKENLSLFAkikgihPQEVEQEVQRIlleLDMQNIQDNLAK- 614
Cdd:COG1132 394 SGRILIDGVDIRDL-TLESLRRQIGVVPQDTFLFS-GTIRENIRYGR------PDATDEEVEEA---AKAAQAHEFIEAl 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 615 -------------HLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH-VIL----FSTqsmde 676
Cdd:COG1132 463 pdgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRtTIViahrLST----- 537
|
250
....*....|....*..
gi 1622880985 677 adIL-ADRKVIMSNGRL 692
Cdd:COG1132 538 --IRnADRILVLDDGRI 552
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
498-690 |
2.69e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 100.23 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIynknlsemqdleEIRKITGVCPQFNVQFD------I 571
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL------------EGKQITEPGPDRMVVFQnysllpW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 572 LTVKENLSLfaKIKGIHPQEVEQEVQRILLE-LDMQNIQDNLAK---HLSEGQKRKLTFGIAILGDPQILLLDEPTTGLD 647
Cdd:TIGR01184 69 LTVRENIAL--AVDRVLPDLSKSERRAIVEEhIALVGLTEAADKrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622880985 648 PFSR----DQVWSLLREHRADHVILfsTQSMDEADILADRKVIMSNG 690
Cdd:TIGR01184 147 ALTRgnlqEELMQIWEEHRVTVLMV--THDVDEALLLSDRVVMLTNG 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1295-1492 |
2.86e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 99.16 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTA--GEVELKGCSSVL----GHLGYCPQENVLWP 1368
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKrsfrKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLEVYAAVKGLRkvdarlaitrlvsafklheqlnvpvqkltTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1448
Cdd:cd03213 96 TLTVRETLMFAAKLRGLS-----------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1449 QQQMWQAIQAVVkNTERGVLLTTHNL-AEAEALCDRVAIMVSGRL 1492
Cdd:cd03213 147 ALQVMSLLRRLA-DTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
478-682 |
3.21e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.88 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS-----VPTEGSVTIYNKNLSEMQ-D 551
Cdd:PRK14258 7 AIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERRvN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 552 LEEIRK-ITGVCPQFNVqFDiLTVKENLSLFAKIKGIHPQ-EVEQEVQRILLELDM-QNIQDNLAK---HLSEGQKRKLT 625
Cdd:PRK14258 83 LNRLRRqVSMVHPKPNL-FP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwDEIKHKIHKsalDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 626 FGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREH--RADHVILFSTQSMDEADILAD 682
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSD 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
477-697 |
6.51e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 477 EAIRIRNVKKEY------------------KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGS 538
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 539 VTIyNKNLSEMqdLEeirkitgvcpqFNVQFD-ILTVKENLSLFAKIKGIHPQEVEQEVQRIL----LE--LDMQniqdn 611
Cdd:COG1134 83 VEV-NGRVSAL--LE-----------LGAGFHpELTGRENIYLNGRLLGLSRKEIDEKFDEIVefaeLGdfIDQP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 612 lAKHLSEGQKRKLTFGIAILGDPQILLLDEPT-TGlDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSN 689
Cdd:COG1134 144 -VKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESGRtVIFVSHSMGAVRRLCDRAIWLEK 221
|
....*...
gi 1622880985 690 GRLKCAGS 697
Cdd:COG1134 222 GRLVMDGD 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1291-1510 |
6.53e-23 |
|
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: 100.41 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1291 KKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------------------CSS 1352
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkkISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1353 VLGHLGYCPQENVLwpmltarEHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNS 1432
Cdd:cd03294 107 VFQSFALLPHRTVL-------ENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1433 PVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYI 1510
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYV 257
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
479-697 |
8.22e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:PRK13644 2 IRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQIL 637
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 638 LLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADIlADRKVIMSNGRLKCAGS 697
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
485-691 |
1.26e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.74 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 485 KKEYKGKSGKVEALKGLLFDI----YEGQITAILGHSGAGKSSLLNILNGLS---VPTEGSVTIYNKNLsemqDLEEIRK 557
Cdd:TIGR00955 24 VSRLRGCFCRERPRKHLLKNVsgvaKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPI----DAKEMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNVQFDILTVKENLSLFA--KIKGIHPQEVEQE-VQRILLELDMQNIQD------NLAKHLSEGQKRKLTFGI 628
Cdd:TIGR00955 100 ISAYVQQDDLFIPTLTVREHLMFQAhlRMPRRVTKKEKRErVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGR 691
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlaQKGKTIICTIHQPSSELFELFDKIILMAEGR 244
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
479-648 |
1.28e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.45 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 558
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDIlTVKENLSLFakikgiHPQEVEQEVQRILLELDMQNIQDNL-----------AKHLSEGQKRKLTFG 627
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLpngydtvlgenGGNLSQGERQLLAIA 151
|
170 180
....*....|....*....|.
gi 1622880985 628 IAILGDPQILLLDEPTTGLDP 648
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDT 172
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
477-697 |
2.27e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 477 EAIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdLEEIR 556
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQ-FNVQFDiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQK------RKLTFGIA 629
Cdd:PRK13548 76 RRRAVLPQhSSLSFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRE---HRADHVILfstqsmdeadIL---------ADRKVIMSNGRLKCAGS 697
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLARQlahERGLAVIV----------VLhdlnlaaryADRIVLLHQGRLVADGT 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1296-1497 |
2.38e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 100.56 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG------HLGYCPQENVLWP 1368
Cdd:COG3842 12 SKRyGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG-RDVTGlppekrNVGMVFQDYALFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTM------RKLcfVlsllgNSP-VLLLDEPS 1441
Cdd:COG3842 91 HLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrvalaRAL--A-----PEPrVLLLDEPL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:COG3842 164 SALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
479-700 |
3.61e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.28 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtIYNKNLSEMQDLEEIRKI 558
Cdd:PRK13648 8 IVFKNVSFQYQSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVC---P--QF---NVQFDILTVKENLSlfakikgIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKltfgIAI 630
Cdd:PRK13648 85 IGIVfqnPdnQFvgsIVKYDVAFGLENHA-------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQR----VAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 631 LG----DPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEAdILADRKVIMSNGRLKCAGS--SIF 700
Cdd:PRK13648 154 AGvlalNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTptEIF 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
479-697 |
3.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEAdILADRKVIMSNGRLKCAGS 697
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1305-1472 |
4.63e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGHLGYCPQENVLW--------PMLTAREHL 1376
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG--EPIRRQRDEYHQDLLYlghqpgikTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1377 EVYAAVKGLRKVDARLAITRLVSafkLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1456
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEALAQVG---LAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*...
gi 1622880985 1457 QAvvkNTERG--VLLTTH 1472
Cdd:PRK13538 173 AQ---HAEQGgmVILTTH 187
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
478-692 |
5.23e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI------YNKNLSEMQD 551
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 552 L-EEIRKITG-VCPQFNVqFDILTVKENLSLFAKI-KGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGI 628
Cdd:PRK11264 79 LiRQLRQHVGfVFQNFNL-FPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSLLR---EHRADHVILfsTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRqlaQEKRTMVIV--THEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1296-1499 |
6.59e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 96.25 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-----CSSVLGHLGYCPQENVLWPML 1370
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnLPPEKRDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 TAREHLEVyaavkGLRKVDA-RLAITRLVS--AFKLH--EQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGID 1445
Cdd:cd03299 87 TVYKNIAY-----GLKKRKVdKKEIERKVLeiAEMLGidHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1446 PTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1499
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1306-1484 |
8.02e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 96.72 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQENVLWPM--LTAREHLEVYAAVK 1383
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI----GYVPQKLYLDTTlpLTVNRFLRLRPGTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1384 glrKVDARLAITRlVSAFKLHEQlnvPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNT 1463
Cdd:PRK09544 98 ---KEDILPALKR-VQAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREL 170
|
170 180
....*....|....*....|.
gi 1622880985 1464 ERGVLLTTHNLAEAEALCDRV 1484
Cdd:PRK09544 171 DCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
493-663 |
8.54e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.33 E-value: 8.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNlsemQDLEEIR-KITGVCPQfNVQFDI 571
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAeACHYLGHR-NAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 572 LTVKENLSLFAKIKGIHPQEVEQEVQRIllelDMQNIQDNLAKHLSEGQKRKLtfGIAIL---GDPqILLLDEPTTGLDP 648
Cdd:PRK13539 88 LTVAENLEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRV--ALARLlvsNRP-IWILDEPTAALDA 160
|
170
....*....|....*
gi 1622880985 649 FSRDQVWSLLREHRA 663
Cdd:PRK13539 161 AAVALFAELIRAHLA 175
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
493-680 |
1.01e-21 |
|
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: 94.73 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDL--EEIRKI---TGVCPQfnv 567
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENILYLghlPGLKPE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 568 qfdiLTVKENLSLFAKIKGIHPQEVEQEvqriLLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLD 647
Cdd:TIGR01189 88 ----LSALENLHFWAAIHGGAQRTIEDA----LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622880985 648 PFSRDQVWSLLREH--RADHVILFSTQSM--DEADIL 680
Cdd:TIGR01189 160 KAGVALLAGLLRAHlaRGGIVLLTTHQDLglVEAREL 196
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
478-687 |
1.51e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 100.82 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 557
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA-DADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNVQFDIlTVKENLsLFAKiKGIHPQEVEQEVQRI-LLELDM---QNIQDNLAKH---LSEGQKRKLTFGIAI 630
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENI-RLAR-PDASDAEIREALERAgLDEFVAalpQGLDTPIGEGgagLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 631 LGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSmDEADILADRKVIM 687
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
476-692 |
1.66e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.68 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 476 KEAIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL-----SVPTEGSVTIYNKNL-SEM 549
Cdd:PRK14267 2 KFAIETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIySPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 550 QDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKGIH------PQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRK 623
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkskkelDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 624 LTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
479-697 |
1.74e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSG-KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYN---KNLSEMQDLEE 554
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 555 IRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRillELDMQNIQDNLAK----HLSEGQKRKLTFGIA 629
Cdd:PRK13643 82 VRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEkspfELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1277-1497 |
2.23e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.96 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1277 VIIASCLHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL--KGCSSVL 1354
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddEDISLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1355 GH------LGYCPQENVLWPMLTAREHL-EVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLS 1427
Cdd:PRK10895 72 LHararrgIGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1428 LLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
478-697 |
2.69e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.46 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRK 557
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ItGVCPQFNVQFDILTVKEN----LSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGD 633
Cdd:PRK10851 76 V-GFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 634 PQILLLDEPTTGLDPFSRDQVWSLLRE-HRA-DHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQlHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1303-1492 |
2.70e-21 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 92.49 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcssvlghlgycpqenvlwpmltarehlevyAAV 1382
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------------------KEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1383 KGLRKVDARLAITRLVSafklheQLNVPVQKLTTgTMRklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKN 1462
Cdd:cd03216 65 SFASPRDARRAGIAMVY------QLSVGERQMVE-IAR------ALARNARLLILDEPTAALTPAEVERLFKVIRR-LRA 130
|
170 180 190
....*....|....*....|....*....|
gi 1622880985 1463 TERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03216 131 QGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
503-697 |
3.96e-21 |
|
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: 97.09 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLsemQDLE-------EIRKItGVCPQfnvQ---FDIL 572
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL---QDSArgiflppHRRRI-GYVFQ---EarlFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 TVKENLsLFAkIKGIHPQEVEQEVQRIlleLDMQNIQDNLAK---HLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPF 649
Cdd:COG4148 93 SVRGNL-LYG-RKRAPRAERRISFDEV---VELLGIGHLLDRrpaTLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 650 SRDQVWSLL-REHRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:COG4148 168 RKAEILPYLeRLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
452-659 |
4.31e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 99.36 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 452 IEKEIDAEHPSDDYFEPVA-PEFQGKEAIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG 530
Cdd:TIGR02868 307 IVEVLDAAGPVAEGSAPAAgAVGLGKPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 531 LSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDIlTVKENLsLFAKiKGIHPQEVEQEVQRILLELDMQNIQD 610
Cdd:TIGR02868 384 LLDPLQGEVTLDGVPVSSL-DQDEVRRRVSVCAQDAHLFDT-TVRENL-RLAR-PDATDEELWAALERVGLADWLRALPD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 611 NL-------AKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLR 659
Cdd:TIGR02868 460 GLdtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL 515
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
479-691 |
4.69e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.67 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkvealkgLLFD--IYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiR 556
Cdd:COG3840 2 LRLDDLTYRYGDFP--------LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCpQFNVQFDILTVKENLSLfakikGIHP-----QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAIL 631
Cdd:COG3840 72 PVSMLF-QENNLFPHLTVAQNIGL-----GLRPglkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 632 GDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGR 691
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
479-696 |
4.72e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.09 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENL----SLFAKIKGIHP---QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAIL 631
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigrHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 632 GDPQILLLDEPTTGLDPFSRDQVWSLLREHRAD-HVILFSTQSMDEADILADRKVIMSNGRLKCAG 696
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1307-1472 |
8.79e-21 |
|
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: 92.17 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGHLGYCPQENVLW--------PMLTAREHLEV 1378
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG--GPLDFQRDSIARGLLYlghapgikTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 YAAVKGLRKVDARLAITRLvSAFKlheqlNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1458
Cdd:cd03231 97 WHADHSDEQVEEALARVGL-NGFE-----DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
170
....*....|....*.
gi 1622880985 1459 vvkNTERG--VLLTTH 1472
Cdd:cd03231 171 ---HCARGgmVVLTTH 183
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
482-693 |
1.01e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.96 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 482 RNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLE--EIR-KI 558
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILaDRKVIMSNGRLK 693
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
442-697 |
1.03e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 442 FQHQGTD-------NKVIEKEIDAEHPSDDYFEPVAPefqgkeAIRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAIL 514
Cdd:PRK11160 301 FQHLGQViasarriNEITEQKPEVTFPTTSTAAADQV------SLTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 515 GHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDlEEIRKITGVCPQ----FNVqfdilTVKENLsLFAKikgihPQ 590
Cdd:PRK11160 373 GRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQAISVVSQrvhlFSA-----TLRDNL-LLAA-----PN 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 591 EVEQEVQRILLELDMQNIQDNLA----------KHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE 660
Cdd:PRK11160 441 ASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622880985 661 HRADHVILFST------QSMdeadilaDRKVIMSNGRLKCAGS 697
Cdd:PRK11160 521 HAQNKTVLMIThrltglEQF-------DRICVMDNGQIIEQGT 556
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1296-1496 |
1.51e-20 |
|
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: 91.93 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------------CSSVLghlgycpQ 1362
Cdd:cd03301 7 TKRfGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrdIAMVF-------Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1363 ENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1443 GIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
480-692 |
1.79e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.90 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 480 RIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYnknlsemqdlEEIRKIT 559
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID----------GQEMRFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 560 GVCPQFNVQFDI----------LTVKENL---SLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF 626
Cdd:PRK11288 72 STTAALAAGVAIiyqelhlvpeMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 627 GIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRAD-HVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
485-697 |
1.94e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 485 KKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD--LEEIR--KITG 560
Cdd:PRK10070 31 KEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaeLREVRrkKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 561 VCPQFNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLD 640
Cdd:PRK10070 111 VFQSFAL-MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 641 EPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
503-677 |
2.05e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.27 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLsEMQDLEeIRKITGVCPQFnvqFDI---LTVKENLS 579
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIA-TRRRVGYMSQA---FSLygeLTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 580 LFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLR 659
Cdd:NF033858 362 LHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLI 441
|
170 180
....*....|....*....|
gi 1622880985 660 E-HRADHVILF-STQSMDEA 677
Cdd:NF033858 442 ElSREDGVTIFiSTHFMNEA 461
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
478-692 |
3.27e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM-------- 549
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsprdaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 550 ------QDLeeirkitGVCPQfnvqfdiLTVKENLSL---FAKIKGIHPQEVEQEVQRILLELDMqNIQ-DNLAKHLSEG 619
Cdd:COG1129 80 giaiihQEL-------NLVPN-------LSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 620 QK------RkltfgiAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:COG1129 145 QQqlveiaR------ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1301-1497 |
3.48e-20 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 91.14 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1301 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG------HLGYCPQENVLWPmltare 1374
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-KDITNlpphkrPVNTVFQNYALFP------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HLEVYAAV------KGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1448
Cdd:cd03300 86 HLTVFENIafglrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622880985 1449 QQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-692 |
3.56e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.90 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL-----SVPTEGSVTIYNKNLSEMqDLE 553
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-DVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 554 EIRKITGVCPQFNVQFDILTVKENLSLFAKIKGI--HPQEVEQEVQRIL----LELDMQNIQDNLAKHLSEGQKRKLTFG 627
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALekaqLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 628 IAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
448-692 |
4.06e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.02 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 448 DNKVIEKEIDAEHPSDDYFEPVaPEF-------QGKEAIRIRNVKKEYKG-KSGKVEALKGLLFDIYEGQITAILGHSGA 519
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAVFMEGV-SEVekeceveVGEPIIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 520 GKSSLLNILNGLSVPTEGSVTI-YNKNLSEMQDLE-----EIRKITGVCPQFNVQFDILTVKENL----SL-----FAKI 584
Cdd:TIGR03269 322 GKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKPGpdgrgRAKRYIGILHQEYDLYPHRTVLDNLteaiGLelpdeLARM 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 585 KGIHPQEV----EQEVQRILleldmqniqDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVW-SLL- 658
Cdd:TIGR03269 402 KAVITLKMvgfdEEKAEEIL---------DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILk 472
|
250 260 270
....*....|....*....|....*....|....*
gi 1622880985 659 -REHRADHVILFStQSMDEADILADRKVIMSNGRL 692
Cdd:TIGR03269 473 aREEMEQTFIIVS-HDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
475-692 |
4.30e-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: 89.41 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 475 GKEAIRIRNVkkeykgkSGKvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK-----NLSEM 549
Cdd:cd03215 1 GEPVLEVRGL-------SVK-GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 550 QDL------EEiRKITGVCPQFnvqfdilTVKENLSLfakikgihpqeveqevqrilleldmqniqdnlAKHLSEGQKRK 623
Cdd:cd03215 73 IRAgiayvpED-RKREGLVLDL-------SVAENIAL--------------------------------SSLLSGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 624 LTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQsMDEADILADRKVIMSNGRL 692
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGkaVLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
478-692 |
4.53e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIynknlsemqDLEEIRk 557
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI---------DGKPVR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGvcPQ-------------FNVqFDILTVKENLSLFAKIKG---IHPQEVEQEVQRIL----LELDMqniqDNLAKHLS 617
Cdd:COG3845 71 IRS--PRdaialgigmvhqhFML-VPNLTVAENIVLGLEPTKggrLDRKAARARIRELSerygLDVDP----DAKVEDLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 618 EGQKRKLTfgI--AILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRAD-HVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:COG3845 144 VGEQQRVE--IlkALYRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1306-1501 |
4.99e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.97 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlgHLGYCP---------QENVLWPmltareHL 1376
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD----LTALPPaerpvsmlfQENNLFP------HL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1377 EVYAAVK-GLRKvDARL---AITRLVSAFklhEQLNVpvqkltTGTMRKLCFVLS------------LLGNSPVLLLDEP 1440
Cdd:COG3840 87 TVAQNIGlGLRP-GLKLtaeQRAQVEQAL---ERVGL------AGLLDRLPGQLSggqrqrvalarcLVRKRPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
478-690 |
7.65e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.91 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSE--------M 549
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvvF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 550 QDleeirkiTGVCPQFNVQfdiltvkENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIA 629
Cdd:PRK11248 77 QN-------EGLLPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNG 690
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1302-1492 |
8.06e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1302 IAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSV----------LGhLGYCPQENVLWPMLT 1371
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-KPVrirsprdaiaLG-IGMVHQHFMLVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREHLEVYAAVKGLRKVD---ARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPtg 1448
Cdd:COG3845 97 VAENIVLGLEPTKGGRLDrkaARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP-- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1449 qqqmwQAIQ---AVVKN-TERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG3845 175 -----QEADelfEILRRlAAEGksIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
479-700 |
8.59e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.31 E-value: 8.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKgKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:PRK13642 5 LEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEAdILADRKVIMSNGRL--KCAGSSIF 700
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1269-1490 |
9.64e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 9.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1269 TSILDEKPVIIASCLHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELK 1348
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSGVE-----------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1349 G-----CSSVLGH-LG-Y-CPQENVLWPMLTAREH--LEVYAAVKGLRKVDARLAitRLVSAFKLHEQ---LNVPVQKLT 1415
Cdd:PRK15439 72 GnpcarLTPAKAHqLGiYlVPQEPLLFPNLSVKENilFGLPKRQASMQKMKQLLA--ALGCQLDLDSSagsLEVADRQIV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1416 TgTMRklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSG 1490
Cdd:PRK15439 150 E-ILR------GLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
479-691 |
9.95e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 9.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRKI 558
Cdd:PRK11607 20 LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:PRK11607 94 NMMFQSYAL-FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 639 LDEPTTGLDPFSRD----QVWSLLreHRADHVILFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK11607 173 LDEPMGALDKKLRDrmqlEVVDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1305-1503 |
1.00e-19 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 90.04 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS----------SVLGHLGYCPQ-----------E 1363
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglsekelyELRRRIGMLFQggalfdsltvfE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1364 NVLWPMltaREHLEVYAAVKgLRKVDARLAITRLVSAFKLH-EQLNvpvqklttGTMRK-------LcfVLsllgNSPVL 1435
Cdd:COG1127 102 NVAFPL---REHTDLSEAEI-RELVLEKLELVGLPGAADKMpSELS--------GGMRKrvalaraL--AL----DPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1436 LLDEPSTGIDPtgqqQMWQAIQAVVK--NTERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1503
Cdd:COG1127 164 LYDEPTAGLDP----ITSAVIDELIRelRDELGltSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
479-647 |
1.05e-19 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 89.91 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 558
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD-LNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDIlTVKENLSLfakikGIHPQEVEQEVQRILLeldmQNIQDNLAK--------------HLSEGQKRKL 624
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRY-----GKPDATDEEVEEAAKK----ANIHDFIMSlpdgydtlvgergsQLSGGQKQRI 148
|
170 180
....*....|....*....|...
gi 1622880985 625 TFGIAILGDPQILLLDEPTTGLD 647
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALD 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
478-691 |
2.51e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.44 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRK 557
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVcpqFnvQFDIL----TVKENLSLFAKIKGIHPQEVEQEVQ---RIL-LE--LDMQNIQdnlakhLSEGQKRKLTFG 627
Cdd:PRK11650 78 IAMV---F--QNYALyphmSVRENMAYGLKIRGMPKAEIEERVAeaaRILeLEplLDRKPRE------LSGGQRQRVAMG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 628 IAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVI-LFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRlHRRLKTTsLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
483-697 |
2.78e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 483 NVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVC 562
Cdd:PRK10895 8 NLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 563 PQFNVQFDILTVKENLSLFAKI-KGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDE 641
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 642 PTTGLDPFSRDQVWSLLrEHRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK10895 164 PFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
482-647 |
3.27e-19 |
|
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: 87.30 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 482 RNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG--LSVPTEGSVTIYNKNLSemqdlEEIRKIT 559
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD-----KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 560 GVCPQFNVQFDILTVKENLSLFAKIKGihpqeveqevqrilleldmqniqdnlakhLSEGQKRKLTFGIAILGDPQILLL 639
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFL 132
|
....*...
gi 1622880985 640 DEPTTGLD 647
Cdd:cd03232 133 DEPTSGLD 140
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
479-697 |
3.59e-19 |
|
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: 88.44 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdLEEIRKI 558
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDIlTVKENLSlFAKiKGIHPQEVEqEVQRI--LLELDMQ-------NIQDNLAKhLSEGQKRKLTFGIA 629
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA-YGR-PGATREEVE-EAARAanAHEFIMElpegydtVIGERGVK-LSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQVWSLLR---EHRADHVIL--FSTqsmdeadIL-ADRKVIMSNGRLKCAGS 697
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALErlmKNRTTFVIAhrLST-------IEnADRIVVLEDGKIVERGT 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
479-682 |
4.98e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.69 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLL---NILNGL--SVPTEGSVTIYNKNLSEMQ-DL 552
Cdd:PRK14243 11 LRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLipGFRVEGKVTFHGKNLYAPDvDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 553 EEIRKITGVCPQFNVQFDiLTVKENLSLFAKIKGiHPQEVEQEVQRILLELDM-QNIQDNL---AKHLSEGQKRKLTFGI 628
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFP-KSIYDNIAYGARING-YKGDMDELVERSLRQAALwDEVKDKLkqsGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILAD 682
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
479-697 |
6.85e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLsLFAKIKgihPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENI-LFGLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
479-692 |
9.54e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsEMQDLEEIRKI 558
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 639 LDEPTTGLDPFSRDQVWS-LLREH-RADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIeISRLHkRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1303-1497 |
1.19e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 89.44 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLG--------HLGYCPQENVLWPMLTARE 1374
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFtnlpprerRVGFVFQHYALFPHMTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNV-PVQklttgtmrklcfvLS--------L---LGNSP-VLLLDEPS 1441
Cdd:COG1118 95 NIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRyPSQ-------------LSggqrqrvaLaraLAVEPeVLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1295-1497 |
1.28e-18 |
|
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: 86.97 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------SVLGHLGYCPQENVLW 1367
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDireqdpvELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTAREHLevyAAVKGLRKVDARLAITRlvsAFKLHEQLNVPVQK--------LTTGTMRKLCFVLSLLGNSPVLLLDE 1439
Cdd:cd03295 88 PHMTVEENI---ALVPKLLKWPKEKIRER---ADELLALVGLDPAEfadrypheLSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1440 PSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1303-1506 |
1.30e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.41 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIrMISGITKPTAGE---------VELKGCSSVLGHlgYCPQENVLWPMLTAR 1373
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRrpwrf*twcANRRALRRTIG*--HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1453
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1454 QAIQAVVKNTERgVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLG 1506
Cdd:NF000106 185 DEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1301-1492 |
1.41e-18 |
|
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: 85.18 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1301 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGH--------LGYCP---QENVLWPM 1369
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprdairagIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1370 LTAREHlevyaavkglrkvdarLAITRLVSAfklheqlnvpvqklttGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1449
Cdd:cd03215 93 LSVAEN----------------IALSSLLSG----------------GNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622880985 1450 QQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03215 141 AEIYRLIRELADAG-KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1305-1491 |
1.42e-18 |
|
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: 87.06 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV--------------ELK---GCSSVLGHLGYCPQENVLW 1367
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgerrggedvwELRkriGLVSPALQLRFPRDETVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTARehlevYAAVkGL-RKVDA--RLAITRLVSAFKLHEQLNVPVQKLTTGTMRKlcfVL---SLLGNSPVLLLDEPS 1441
Cdd:COG1119 100 VVLSGF-----FDSI-GLyREPTDeqRERARELLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1303-1492 |
1.42e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 86.10 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVL-GHLGYCPQENVLWpMLTAREH 1375
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpADLrRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1376 LevyaAVKGLRKVDARL--AITRL-VSAF-KLHEQ-LNVPV----------QKLTTGTMRklcfvlSLLGNSPVLLLDEP 1440
Cdd:cd03245 98 I----TLGAPLADDERIlrAAELAgVTDFvNKHPNgLDLQIgergrglsggQRQAVALAR------ALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVVKntERGVLLTTHNLAeAEALCDRVAIMVSGRL 1492
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
474-697 |
1.80e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.24 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 474 QGKEAIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdlE 553
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 554 EIRKITGVCPQFNVqFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGD 633
Cdd:PRK09452 84 ENRHVNTVFQSYAL-FPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 634 PQILLLDEPTTGLDPFSRDQVWSLLREHRADHVI--LFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGItfVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1303-1487 |
1.86e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQENVL---WPmLTAREHLEV- 1378
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV----AYVPQRSEVpdsLP-LTVRDLVAMg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 -YAAVKGLRKV--DARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1455
Cdd:NF040873 82 rWARRGLWRRLtrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170 180 190
....*....|....*....|....*....|..
gi 1622880985 1456 IQAVVKnTERGVLLTTHNLAEAeALCDRVAIM 1487
Cdd:NF040873 162 LAEEHA-RGATVVVVTHDLELV-RRADPCVLL 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
475-796 |
1.90e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.02 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 475 GKEAIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAG--KSSLLNILNGlsvPTEGSVTIynKNLSEMQDL 552
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 553 EEIRKITGVC-PQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAIL 631
Cdd:NF000106 81 RALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 632 GDPQILLLDEPTTGLDPFSRDQVWSLLREH-RADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSIFLKRRWGlGYH 710
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 711 LSLHRNEICNPEQITSFITHHIPDAKL-KTKNKEKLVYTLPLERTNIFPDLFSNLdkcSDQG--VTGYDISMSTLNEIFM 787
Cdd:NF000106 240 LQIRPAHAAELDRMVGAIAQAGLDGIAgATADHEDGVVNVPIVSDEQLSAVVGML---GERGftISGHQHPSAQL*EVFL 316
|
....*....
gi 1622880985 788 KLEGQSTTK 796
Cdd:NF000106 317 AITGQKTSE 325
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
479-692 |
2.20e-18 |
|
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: 84.19 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 558
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-WDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQfnvqfDILtvkenlsLFAKikgihpqeveqevqrilleldmqNIQDNLakhLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03246 78 VGYLPQ-----DDE-------LFSG-----------------------SIAENI---LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
479-710 |
2.71e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 85.74 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 558
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-TLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDIlTVKENLSL------------FAKIKGIH------PQEVEQEV-QRILleldmqniqdnlakHLSEG 619
Cdd:cd03253 77 IGVVPQDTVLFND-TIGYNIRYgrpdatdeevieAAKAAQIHdkimrfPDGYDTIVgERGL--------------KLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 620 QKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEAdILADRKVIMSNGRLKCAGSSI 699
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHE 220
|
250
....*....|.
gi 1622880985 700 FLKRRWGLgYH 710
Cdd:cd03253 221 ELLAKGGL-YA 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
487-648 |
3.68e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 487 EYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD------------LEE 554
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 555 IR-KITGVCPQFNVqFDILTVKEN-LSLFAKIKGIHPQEVEQEVQRILLELDM-QNIQDNLAKHLSEGQKRKLTFGIAIL 631
Cdd:PRK10619 90 LRtRLTMVFQHFNL-WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALA 168
|
170
....*....|....*..
gi 1622880985 632 GDPQILLLDEPTTGLDP 648
Cdd:PRK10619 169 MEPEVLLFDEPTSALDP 185
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1305-1511 |
3.85e-18 |
|
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: 90.66 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQENVLWPMlTAREHL- 1376
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpASLRRQIGVVLQDVFLFSG-TIRENIt 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1377 ---------EVYAAvkglrkvdARLA-ITRLVSAfkLHEQLNVPV----QKLTTGTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:COG2274 571 lgdpdatdeEIIEA--------ARLAgLHDFIEA--LPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 1443 GIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYIL 1511
Cdd:COG2274 641 ALDAETEAIILENLRRLLKG--RTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1305-1503 |
4.28e-18 |
|
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: 85.25 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHL----GYCPQ-----------E 1363
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglSEAELYRLrrrmGMLFQsgalfdsltvfE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1364 NVLWPMltaREHlevyaavkglRKVDARLaITRLVsAFKLhEQLNVP--VQKLT---TGTMRK-LCFVLSLLGNSPVLLL 1437
Cdd:cd03261 97 NVAFPL---REH----------TRLSEEE-IREIV-LEKL-EAVGLRgaEDLYPaelSGGMKKrVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1438 DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1503
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
479-697 |
5.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.22 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSG-KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYN----KNLSEMQDLE 553
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 554 EIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILlelDMQNIQDNLAK----HLSEGQKRKLTFGI 628
Cdd:PRK13645 87 RLRKEIGLVFQFpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELL---KLVQLPEDYVKrspfELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSL---LREHRADHVILFsTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRIIMV-THNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
479-692 |
5.78e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.68 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEY-KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKN------------ 545
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 546 -----------LSEMQDLEEIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRI--LLELDMQNIQDN 611
Cdd:PRK13651 83 vleklviqktrFKKIKKIKEIRRRVGVVFQFaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYieLVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 612 lAKHLSEGQKRKltfgIAILG----DPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVI 686
Cdd:PRK13651 163 -PFELSGGQKRR----VALAGilamEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
....*.
gi 1622880985 687 MSNGRL 692
Cdd:PRK13651 238 FKDGKI 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1283-1501 |
6.62e-18 |
|
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: 84.55 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1283 LHKEYAGQKKscfskrkKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVL-------- 1354
Cdd:cd03258 7 VSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1355 --GHLGYCPQE-NVLWPmLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKL-HEQLNVPVQkLTTGTMRKLCFVLSLLG 1430
Cdd:cd03258 80 arRRIGMIFQHfNLLSS-RTVFENVALPLEIAGVPKAEIEERVLELLELVGLeDKADAYPAQ-LSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1431 NSPVLLLDEPSTGIDPTGQQQMWQAIQAVvkNTERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDI--NRELGltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
467-692 |
8.19e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.55 E-value: 8.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 467 EPVAPefqGKEAIRIRNVkkEYKGKSGkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL 546
Cdd:COG3845 249 APAEP---GEVVLEVENL--SVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 547 S-----EMQDL------EEiRKITGVCPQFnvqfdilTVKENLSL-------FAKIKGIHPQEVEQEVQRILLELD--MQ 606
Cdd:COG3845 323 TglsprERRRLgvayipED-RLGRGLVPDM-------SVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDvrTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 607 NIqDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKV 685
Cdd:COG3845 395 GP-DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAaVLLISEDLDEILALSDRIA 473
|
....*..
gi 1622880985 686 IMSNGRL 692
Cdd:COG3845 474 VMYEGRI 480
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1306-1499 |
8.21e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.21 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLG---------HLGYCPQENVL-WPmLTARE- 1374
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP--LAdwspaelarRRAVLPQHSSLsFP-FTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 -------HLEVYAAVKGLrkVDARLAITRLvSAFKlheqlNVPVQKLTTGTM------RKLCFVLSLLGNSPVLLLDEPS 1441
Cdd:PRK13548 97 vamgrapHGLSRAEDDAL--VAAALAQVDL-AHLA-----GRDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1499
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
503-692 |
1.24e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.86 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqdlEEIRKITGVCPQFNVQFDILTVKENLSLfa 582
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT---PPSRRPVSMLFQENNLFSHLTVAQNIGL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 583 kikGIHP-----QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSL 657
Cdd:PRK10771 95 ---GLNPglklnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622880985 658 LRE--HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK10771 172 VSQvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
510-697 |
1.86e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.08 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 510 ITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemqDLE-------EIRKItGVCPQFNVQFDILTVKENLSLfa 582
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF---DAEkgiclppEKRRI-GYVFQDARLFPHYKVRGNLRY-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 583 kikGIHPQEVEQeVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLD-PFSRDqvwsLLR-- 659
Cdd:PRK11144 100 ---GMAKSMVAQ-FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE----LLPyl 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622880985 660 EHRADHV---ILFSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK11144 172 ERLAREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
475-698 |
2.37e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 475 GKEAIRIRNVKKEYKGKSGKVeALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL------SVPTEGSVTIYNKNLSE 548
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 549 MqDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHPQE-----VEQEVQRILLELDMQNIQDNLAKHLSEGQKRK 623
Cdd:PRK14246 83 I-DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 624 LTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSS 698
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
500-674 |
2.38e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.16 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 500 GLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM-----QDLEEIRKITGVCPQfnvqfdiLTV 574
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhQDLLYLGHQPGIKTE-------LTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 575 KENLSLFAKIKGihPQEvEQEVQRILLELDMQNIQDNLAKHLSEGQKRKltfgIAI----LGDPQILLLDEPTTGLDPFS 650
Cdd:PRK13538 92 LENLRFYQRLHG--PGD-DEALWEALAQVGLAGFEDVPVRQLSAGQQRR----VALarlwLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|....*..
gi 1622880985 651 RDQVWSLLREHrADH---VILFSTQSM 674
Cdd:PRK13538 165 VARLEALLAQH-AEQggmVILTTHQDL 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
479-697 |
2.62e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 558
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TgVCPQFNVQFDILTVKE--------NLSLFAKIKgihpQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAI 630
Cdd:PRK11231 79 A-LLPQHHLTPEGITVRElvaygrspWLSLWGRLS----AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 631 LGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH----VILfstQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGktvvTVL---HDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
479-692 |
2.81e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYN-KNLSEMQDLEEIRK 557
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITG-VCPQFNVqFDILTVKENLsLFA--KIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDP 634
Cdd:PRK09493 78 EAGmVFQQFYL-FPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 635 QILLLDEPTTGLDPFSRDQVWSLLR---EHRADHVILfsTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIV--THEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
498-674 |
3.09e-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: 81.77 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDlEEIRKITGVCPQFNVQfDILTVKEN 577
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIK-TTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 578 LSLFAKIKGihpqevEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSL 657
Cdd:cd03231 94 LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*....
gi 1622880985 658 LREH--RADHVILFSTQSM 674
Cdd:cd03231 168 MAGHcaRGGMVVLTTHQDL 186
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1291-1490 |
3.11e-17 |
|
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: 81.92 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1291 KKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHL----GYCPQeNVL 1366
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksiGYVMQ-DVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1367 WPMLTAREHLEVYAAVKGLRKVDARLA-ITRLVSAFKLHEQLnvPvQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGID 1445
Cdd:cd03226 82 YQLFTDSVREELLLGLKELDAGNEQAEtVLKDLDLYALKERH--P-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1446 PTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSG 1490
Cdd:cd03226 159 YKNMERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
475-697 |
3.14e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 475 GKEAIRIRNVKKEYKGK-SGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT---IYNK------ 544
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdIYIGdkknnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 545 ------NLSEMQDLEEIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQ-NIQDNLAKHL 616
Cdd:PRK13631 98 elitnpYSKKIKNFKELRRRVSMVFQFpEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 617 SEGQKRKltfgIAILG----DPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFS-TQSMDEADILADRKVIMSNGR 691
Cdd:PRK13631 178 SGGQKRR----VAIAGilaiQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFViTHTMEHVLEVADEVIVMDKGK 253
|
....*.
gi 1622880985 692 LKCAGS 697
Cdd:PRK13631 254 ILKTGT 259
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1303-1487 |
3.84e-17 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 86.96 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMlTAREH 1375
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1376 LEVY---AAVKGLRKVDARLAITRLVSAfkLHEQLNVPVQK----LTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1448
Cdd:TIGR02857 416 IRLArpdASDAEIREALERAGLDEFVAA--LPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622880985 1449 QQQMWQAIQAVVKNteRGVLLTTHNLAEAEaLCDRVAIM 1487
Cdd:TIGR02857 494 EAEVLEALRALAQG--RTVLLVTHRLALAA-LADRIVVL 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
450-652 |
4.20e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 450 KVIEK--EIDAEHPSDD-YFEPVAPEFQGKEAIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLN 526
Cdd:COG0488 284 KALEKleREEPPRRDKTvEIRFPPPERLGKKVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 527 ILNGLSVPTEGSVTIyNKNLSemqdleeirkiTGVCPQFNVQFDI-LTVKENLSLFAkiKGIHPQEVEQEVQRILLELDM 605
Cdd:COG0488 360 LLAGELEPDSGTVKL-GETVK-----------IGYFDQHQEELDPdKTVLDELRDGA--PGGTEQEVRGYLGRFLFSGDD 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622880985 606 qniQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRD 652
Cdd:COG0488 426 ---AFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLE 469
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
479-692 |
4.24e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGksGKvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEE--IR 556
Cdd:PRK10908 2 IRFEHVSKAYLG--GR-QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQI 636
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
481-692 |
4.79e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.09 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD--LEEIRKi 558
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdaLAQLRR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 tgvcPQFNVQFDI------LTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILG 632
Cdd:PRK10535 86 ----EHFGFIFQRyhllshLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 633 DPQILLLDEPTTGLDPFSRDQVWSLLREHRAD-HVILFSTQSMDEADiLADRKVIMSNGRL 692
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
474-648 |
5.35e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 82.54 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 474 QGKEAIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL------- 546
Cdd:COG4598 4 TAPPALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 547 -----SEMQDLEEIR-KITGVCPQFNVqFDILTVKENLsLFAKI--KGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSE 618
Cdd:COG4598 80 gelvpADRRQLQRIRtRLGMVFQSFNL-WSHMTVLENV-IEAPVhvLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190
....*....|....*....|....*....|
gi 1622880985 619 GQKRKLTFGIAILGDPQILLLDEPTTGLDP 648
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1305-1492 |
5.49e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 80.34 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC------SSVLG-HLGYCPQENVLWPMlTAREhle 1377
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdPNELGdHVGYLPQDDELFSG-SIAE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 vyaavkglrkvdarlaitrlvsafklheqlNVpvqkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQ 1457
Cdd:cd03246 95 ------------------------------NI----LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*
gi 1622880985 1458 AvVKNTERGVLLTTHNLaEAEALCDRVAIMVSGRL 1492
Cdd:cd03246 141 A-LKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1296-1497 |
5.53e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 84.35 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGHLGycPQE-NV-------- 1365
Cdd:COG3839 10 SKSyGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG--RDVTDLP--PKDrNIamvfqsya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1366 LWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTM------RklcfvlSLLGNSPVLLLDE 1439
Cdd:COG3839 86 LYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRqrvalgR------ALVREPKVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1440 PSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
479-711 |
7.76e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 81.76 E-value: 7.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSeMQDLEEIRKI 558
Cdd:cd03252 1 ITFEHVRFRYKPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDiLTVKENLSL------------FAKIKGIHPQEVEqevqrilLELDMQNIQDNLAKHLSEGQKRKLTF 626
Cdd:cd03252 78 VGVVLQENVLFN-RSIRDNIALadpgmsmervieAAKLAGAHDFISE-------LPEGYDTIVGEQGAGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 627 GIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMdEADILADRKVIMSNGRLKCAGSSIFLKRRWG 706
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
....*
gi 1622880985 707 LGYHL 711
Cdd:cd03252 229 LYAYL 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1307-1496 |
8.18e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.51 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHL-GYCPQENVLWPMLTARE----- 1374
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealSARAASRRvASVPQDTSLSFEFDVRQvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 ---HLEVYAAVKGLRKVDARLAITRL-VSAFklheqLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1450
Cdd:PRK09536 102 rtpHRSRFDTWTETDRAAVERAMERTgVAQF-----ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622880985 1451 QMWQAIQAVVkNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:PRK09536 177 RTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
497-687 |
9.87e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.97 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 497 ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiynknlsemqdleeiRKITGVCPQFNVQ-------F 569
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------------RRAGGARVAYVPQrsevpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 570 DiLTVKE--NLSLFAKIK--GIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTG 645
Cdd:NF040873 71 P-LTVRDlvAMGRWARRGlwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622880985 646 LDPFSRDQVWSLLREHRADHV-ILFSTQSMDEAdILADRKVIM 687
Cdd:NF040873 150 LDAESRERIIALLAEEHARGAtVVVVTHDLELV-RRADPCVLL 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1305-1492 |
1.13e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.07 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSV----------LGhLGYCPQENVLWPMLTARE 1374
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG-EPVrfrsprdaqaAG-IAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HLEVYAAVKGLRKVDARLAITR---LVSAFKLHEQLNVPVQKLTTGTMRklcFVL---SLLGNSPVLLLDEPSTGIDPTG 1448
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRareLLARLGLDIDPDTPVGDLSVAQQQ---LVEiarALSRDARVLILDEPTASLTERE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622880985 1449 QQQMWQAIQAVvknTERGV--LLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG1129 176 VERLFRIIRRL---KAQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
479-692 |
1.46e-16 |
|
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: 80.59 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSeMQDLEEIRKI 558
Cdd:cd03248 12 VKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDiLTVKENLSL------FAKIK----GIHPQEVEQEvqrilLELDMQNIQDNLAKHLSEGQKRKLTFGI 628
Cdd:cd03248 90 VSLVGQEPVLFA-RSLQDNIAYglqscsFECVKeaaqKAHAHSFISE-----LASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 629 AILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADiLADRKVIMSNGRL 692
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
496-697 |
1.55e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.59 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 496 EALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL--SEMQDLEEIRKITGVCPQFNVQFDILT 573
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 574 VKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQ 653
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622880985 654 VWSLLRE--HRADHVILfSTQSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK13638 175 MIAIIRRivAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1297-1492 |
1.71e-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: 80.39 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1297 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISG---ITKPTAGEVELKGCSS----VLGHLGYCPQENVLWPM 1369
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRkpdqFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1370 LTAREHLeVYAAVKGLRKVDARLAITRLVSAFKL----HEQL-NVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGI 1444
Cdd:cd03234 96 LTVRETL-TYTAILRLPRKSSDAIRKKRVEDVLLrdlaLTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1445 DP-TGQQQMWQAIQAVVKNteRGVLLTTHN-LAEAEALCDRVAIMVSGRL 1492
Cdd:cd03234 175 DSfTALNLVSTLSQLARRN--RIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1311-1492 |
1.83e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 79.84 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1311 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLGYCP-----QENVLWPMLTAREHLEVyAAVKGL 1385
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPvsmlfQENNLFAHLTVEQNVGL-GLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1386 R--KVDaRLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNT 1463
Cdd:cd03298 100 KltAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178
|
170 180
....*....|....*....|....*....
gi 1622880985 1464 ERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
493-717 |
2.06e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.90 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVeALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLsVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQfNVQFDIL 572
Cdd:PRK11174 362 GKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPESWRKHLSWVGQ-NPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 TVKENLSLfAKIKgIHPQEVEQEVQR---------ILLELDMQnIQDNLAKhLSEGQKRKLTFGIAILGDPQILLLDEPT 643
Cdd:PRK11174 438 TLRDNVLL-GNPD-ASDEQLQQALENawvseflplLPQGLDTP-IGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 644 TGLDPFSRDQVWSLLREHRADHVILFSTQSMDEadiLA--DRKVIMSNGRLKCAGSSIFLKRRWGLGYHLSLHRNE 717
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRQTTLMVTHQLED---LAqwDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
477-691 |
2.33e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.17 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 477 EAIRIRNVKKEYK-----GKsgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK----NLS 547
Cdd:COG4778 3 TLLEVENLSKTFTlhlqgGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 548 EMQDLE--EIRKIT-GVCPQF-NV-----QFDIltVKEnlSLFAkiKGIHPQEVEQEVQRILLELdmqNIQDNLAkHL-- 616
Cdd:COG4778 81 QASPREilALRRRTiGYVSQFlRViprvsALDV--VAE--PLLE--RGVDREEARARARELLARL---NLPERLW-DLpp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 617 ---SEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRAD--------HvilfstqsmDEA--DILADR 683
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgtaiigifH---------DEEvrEAVADR 221
|
....*...
gi 1622880985 684 KVIMSNGR 691
Cdd:COG4778 222 VVDVTPFS 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1303-1491 |
4.20e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.41 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELkgcssvLGH------------LGYCPQENVLWPML 1370
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL------FGQpvdagdiatrrrVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 TAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGtMRKLcfvLSL----LGNSPVLLLDEPSTGIDP 1446
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLG-IRQR---LSLavavIHKPELLILDEPTSGVDP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622880985 1447 TGQQQMWQAIQAVVKntERGV--LLTTHNLAEAEaLCDRVAIMVSGR 1491
Cdd:NF033858 431 VARDMFWRLLIELSR--EDGVtiFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1295-1498 |
4.25e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 80.25 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLG-HLGYCPQenvlwpmLTAR 1373
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAiSAGLSGQ-------LTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1453
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1454 QAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSI 1498
Cdd:PRK13546 184 DKIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1295-1492 |
4.41e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 81.25 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP---TAGEVELKGcSSVLG------------HLG 1358
Cdd:COG0444 11 FPTRRGVVKAvDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDG-EDLLKlsekelrkirgrEIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1359 YCPQE--NVLWPMLTAREHL-EVYAAVKGLRKVDARLAITRLVSAFKLHEQLNV----PVQkLTTGtMR-KLCFVLSLLG 1430
Cdd:COG0444 90 MIFQDpmTSLNPVMTVGDQIaEPLRIHGGLSKAEARERAIELLERVGLPDPERRldryPHE-LSGG-MRqRVMIARALAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1431 NSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1269-1496 |
8.05e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 8.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1269 TSILDEKPVIIASCLHKEYagqkksCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELK 1348
Cdd:TIGR03269 271 CEVEVGEPIIKVRNVSKRY------ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1349 --------------GCSSVLGHLGYCPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSA-F---KLHEQLNVP 1410
Cdd:TIGR03269 345 vgdewvdmtkpgpdGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVgFdeeKAEEILDKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1411 VQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSG 1490
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
....*.
gi 1622880985 1491 RLRCIG 1496
Cdd:TIGR03269 505 KIVKIG 510
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
479-698 |
9.42e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.16 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS--VPTEGSVtIYNKNLSEMQDLEEIR 556
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IYHVALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGV-CP-------QFNVQFDILTVKENLSLFAKIkGIHPQ------------------------EVEQEVQRILLELD 604
Cdd:TIGR03269 76 SKVGEpCPvcggtlePEEVDFWNLSDKLRRRIRKRI-AIMLQrtfalygddtvldnvlealeeigyEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 605 MQNIQD---NLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH---VILFS--TQSMDE 676
Cdd:TIGR03269 155 MVQLSHritHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgisMVLTShwPEVIED 234
|
250 260
....*....|....*....|..
gi 1622880985 677 adiLADRKVIMSNGRLKCAGSS 698
Cdd:TIGR03269 235 ---LSDKAIWLENGEIKEEGTP 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1308-1501 |
2.00e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.31 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1308 SFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlgHLGYCP---------QENVLWPMLTAREHLEV 1378
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPsrrpvsmlfQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 YAAvKGLR-KVDARLAITRLVSAFKLHEQLN-VPVQkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1456
Cdd:PRK10771 95 GLN-PGLKlNAAQREKLHAIARQMGIEDLLArLPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1457 QAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1303-1504 |
2.06e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLGH-------LGYCPQENVLWPMLTARE 1374
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINyNKLDHklaaqlgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HLEV----YAAVKGLRKVD---ARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1447
Cdd:PRK09700 100 NLYIgrhlTKKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1448 GQQQMWqAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1504
Cdd:PRK09700 180 EVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1300-1508 |
2.46e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1300 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVElkgcssVLG--------------HLGYCPQ--- 1362
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE------VLGgdmadarhrravcpRIAYMPQglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1363 ENvLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKlcfvLSL---LGNSPVLL-LD 1438
Cdd:NF033858 87 KN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQK----LGLccaLIHDPDLLiLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1439 EPSTGIDPTGQQQMWQAIQAVvkNTERG---VLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLGKD 1508
Cdd:NF033858 162 EPTTGVDPLSRRQFWELIDRI--RAERPgmsVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGAD 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
479-693 |
2.51e-15 |
|
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: 76.30 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 558
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDiLTVKENLSLFAkikgihpqevEQEVQRILLELDMQNIQDNlakhLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03369 84 LTIIPQDPTLFS-GTIRSNLDPFD----------EYSDEEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEAdILADRKVIMSNGRLK 693
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTI-IDYDKILVMDAGEVK 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
498-693 |
2.61e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.13 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdlEEIR-----KITGVCPQFNVQFDIL 572
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD--EEARaklraKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 TVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRD 652
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622880985 653 QVWSLLREHRADHVILFSTQSMDEAdiLA---DRKVIMSNGRLK 693
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQ--LAarcDRRLRLVNGQLQ 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
497-691 |
3.96e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 497 ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKitGVCPQF-NVQ-FDILTV 574
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM--GVVRTFqHVRlFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 575 KENL----------SLFA---KIKGIHPQEVE------QEVQRILLeLDMQNIQdnlAKHLSEGQKRKLTFGIAILGDPQ 635
Cdd:PRK11300 98 IENLlvaqhqqlktGLFSgllKTPAFRRAESEaldraaTWLERVGL-LEHANRQ---AGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 636 ILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1298-1492 |
4.33e-15 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 76.45 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGI-----TKPTAGEVELKGcsSVLGHLGYCP----------- 1361
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDG--KDIYDLDVDVlelrrrvgmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1362 ----------QENV---LWPMLTAREHLEVYAAVKGLRKVdarlAITRLVSAfKLHeqlnvpVQKLTTGTMRKLCFVLSL 1428
Cdd:cd03260 88 qkpnpfpgsiYDNVaygLRLHGIKLKEELDERVEEALRKA----ALWDEVKD-RLH------ALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1429 LGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVvkNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
481-692 |
4.53e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.03 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDleEIRkitg 560
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE--DTR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 561 vcpqfnVQFD---IL---TVKENLSLfaKIKGIHPQEVEQEVQRILLEldmQNIQDNLAKhLSEGQKRKLTFGIAILGDP 634
Cdd:PRK11247 85 ------LMFQdarLLpwkKVIDNVGL--GLKGQWRDAALQALAAVGLA---DRANEWPAA-LSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 635 QILLLDEPTTGLDPFSR----DQVWSLLREHraDHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK11247 153 GLLLLDEPLGALDALTRiemqDLIESLWQQH--GFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1305-1492 |
4.79e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.66 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP----TAGEVELKG----CSSVLGHLGYCPQEN---VLWPMLTAR 1373
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGkpvaPCALRGRKIATIMQNprsAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EH-LEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQM 1452
Cdd:PRK10418 100 THaRETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622880985 1453 WQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK10418 180 LDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1313-1484 |
4.82e-15 |
|
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: 76.68 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1313 EGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlghLGYCPQEnvlwpmLTAREHLEVYAAvkgLRKVDARL 1392
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----VSYKPQY------IKADYEGTVRDL---LSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1393 AI-----TRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGV 1467
Cdd:cd03237 90 YThpyfkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTA 169
|
170
....*....|....*..
gi 1622880985 1468 LLTTHNLAEAEALCDRV 1484
Cdd:cd03237 170 FVVEHDIIMIDYLADRL 186
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1303-1497 |
6.34e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.72 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlghLGYCP----------QENVLWPMLTA 1372
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-----LSHVPpyqrpinmmfQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQM 1452
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1453 WQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:PRK11607 189 QLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
34-417 |
6.42e-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: 78.20 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 34 WGLSILLGLCIALFSSSMRNVQFPGMAPQNLGRVDKFNSSslkvvytpisnLTQQIMNKTALAPLLKGTSVIGAPNKTym 113
Cdd:pfam12698 4 LIITLLLPILLILLLGLIFSNAVNDPEELPVAVVDEDNSS-----------LSRQLVRALEASPTVNLVQYVDSEEEA-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 114 nEILLENFPYAMGIIFNETFSYKLTFFQGYNIPLWKEEDFSAhcwdgygefpckltkywnrGFVALQTAINTAIIEITTN 193
Cdd:pfam12698 71 -KEALKNGKIDGLLVIPKGFSKDLLKGESATVTVYINSSNLL-------------------VSKLILNALQSLLQQLNAS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 194 HPVMEELMSVTAITmktlpfISKNLLHNEIFIFFFLLHFSPLVYFISL---------NVTKER-KKSKNLMKVMGLQDSA 263
Cdd:pfam12698 131 ALVLLLEALSTSAP------IPVESTPLFNPQSGYAYYLVGLILMIIIligaaiiavSIVEEKeSRIKERLLVSGVSPLQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 264 FWLSWGLIYAGFIFIISIFITIVItFTEIIVMTGFMVIFILFFLYGLSLVALVFLMSVLLKKAVLTNLVVFLLTL-FWGC 342
Cdd:pfam12698 205 YWLGKILGDFLVGLLQLLIILLLL-FGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILlLSGF 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 343 LGFTVFYEQLPSSLGWILSICSPFAFTAGMTQIIKLDYNlngvifpdpsgdsYTMIATFSILLLDGFIYLLLALY 417
Cdd:pfam12698 284 FGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSL-------------WEIAPSLIILLLFAVVLLLLALL 345
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
448-665 |
8.54e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 80.54 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 448 DNKVIEKEIDAEHPSDDYFEPVAPEFQGKEAIRI-RNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLN 526
Cdd:TIGR00956 728 EAGEVLGSTDLTDESDDVNDEKDMEKESGEDIFHwRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLN 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 527 ILNG---LSVPTEGSVTIynkNLSEMQdlEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKgiHPQEVEQE-----VQR 598
Cdd:TIGR00956 808 VLAErvtTGVITGGDRLV---NGRPLD--SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLR--QPKSVSKSekmeyVEE 880
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 599 ILLELDMQNIQDNLAKHLSEG----QKRKLTFGIAILGDPQILL-LDEPTTGLDPFSrdqVWSLLREHR--ADH 665
Cdd:TIGR00956 881 VIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT---AWSICKLMRklADH 951
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1303-1497 |
8.60e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 75.84 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHL-----GYCPQENVLWPMLTAREHLE 1377
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqernvGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 VYAAVKGLRKVDARLAITRlvsafKLHEQLNV----------PVQkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1447
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRA-----KVHELLKLvqldwladryPAQ-LSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1448 GQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:cd03296 171 VRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1306-1492 |
9.74e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.82 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------------SVLGHLGYCPQENVLWPMLTA 1372
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpsekairLLRQKVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHL-EVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1451
Cdd:COG4161 100 MENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622880985 1452 MWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG4161 180 VVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1267-1497 |
1.45e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1267 LTTSILDEKPVIIASCLHKEYAGqkkscfskrkkKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVE 1346
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDG-----------KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1347 LKGCssVLGHLgycPQEN----------VLWPmltareHLEVYAAVK-GLR--KVDARLAITRLVSAFK---LHEQLNVP 1410
Cdd:PRK09452 73 LDGQ--DITHV---PAENrhvntvfqsyALFP------HMTVFENVAfGLRmqKTPAAEITPRVMEALRmvqLEEFAQRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1411 VQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMwqaiQAVVKNTERGVLLT----THNLAEAEALCDRVAI 1486
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM----QNELKALQRKLGITfvfvTHDQEEALTMSDRIVV 217
|
250
....*....|.
gi 1622880985 1487 MVSGRLRCIGS 1497
Cdd:PRK09452 218 MRDGRIEQDGT 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1275-1440 |
1.58e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1275 KPVIIASCLHKEYAGqkkscfskrkKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVElkgcssvL 1354
Cdd:COG0488 313 KKVLELEGLSKSYGD----------KTLL-DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-------L 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1355 GH---LGYCPQEN-VLWPMLTAREHLEVYAavKGLRKVDARlaitRLVSAFKLH-EQLNVPVQKLTTGTMRKLCFVLSLL 1429
Cdd:COG0488 375 GEtvkIGYFDQHQeELDPDKTVLDELRDGA--PGGTEQEVR----GYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLL 448
|
170
....*....|.
gi 1622880985 1430 GNSPVLLLDEP 1440
Cdd:COG0488 449 SPPNVLLLDEP 459
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
481-647 |
1.59e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIyNKNLSeM----QD----- 551
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR-IgylpQEppldd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 552 ----LEEIrkITGVCPQFNVQFDILTVKENLS-----------LFAKIKGIHPQEVEQEVQRILLELDM-QNIQDNLAKH 615
Cdd:COG0488 75 dltvLDTV--LDGDAELRALEAELEELEAKLAepdedlerlaeLQEEFEALGGWEAEARAEEILSGLGFpEEDLDRPVSE 152
|
170 180 190
....*....|....*....|....*....|..
gi 1622880985 616 LSEGQKRKLTFGIAILGDPQILLLDEPTTGLD 647
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1305-1492 |
2.08e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGH--------LGYCP---QENVLWPMLTAR 1373
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdairagIAYVPedrKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EH--LEVYAAVKGLRKVDARlAITRLVSafKLHEQLNV-------PVQKLTTGTMRKLcfVLS--LLGNSPVLLLDEPST 1442
Cdd:COG1129 349 ENitLASLDRLSRGGLLDRR-RERALAE--EYIKRLRIktpspeqPVGNLSGGNQQKV--VLAkwLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1443 GIDPTGQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAEG-KAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
479-662 |
4.38e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 70.94 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIynknlsemqdleeirki 558
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 tgvcpqfnvqfdiltvkenlslfakIKGIHPQEVEQevqrilleldmqniqdnlakhLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03221 60 -------------------------GSTVKIGYFEQ---------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180
....*....|....*....|....
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLREHR 662
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYP 117
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1283-1492 |
4.56e-14 |
|
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: 72.95 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1283 LHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---------SV 1353
Cdd:cd03262 6 LHKSFGDFH-----------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkkninEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1354 LGHLGYCPQENVLWPMLTAREHL-EVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNS 1432
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1433 PVLLLDEPSTGIDPtgqqQMWQAIQAVVKN-TERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03262 155 KVMLFDEPTSALDP----ELVGEVLDVMKDlAEEGmtMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1299-1492 |
5.57e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 71.58 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1299 KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCssvlghlgycpqenvlwPMLTAREHLEV 1378
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV-----------------PVSDLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 YAAVkglrkvdarlaITRLVSAFKLHEQLNVPVQkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1458
Cdd:cd03247 76 LISV-----------LNQRPYLFDTTLRNNLGRR-FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFE 143
|
170 180 190
....*....|....*....|....*....|....
gi 1622880985 1459 VVKNteRGVLLTTHNLAEAEALcDRVAIMVSGRL 1492
Cdd:cd03247 144 VLKD--KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1291-1510 |
5.62e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1291 KKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSV-----------LGHLGY 1359
Cdd:PRK10070 31 KEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaelrevrRKKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1360 CPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDE 1439
Cdd:PRK10070 111 VFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1440 PSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYI 1510
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1305-1440 |
7.87e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-KGCSsvlghLGYCPQENVLWPMLTARE-----HLEV 1378
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLR-----IGYLPQEPPLDDDLTVLDtvldgDAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 YAAVKGLRKVDARLA---------------------------ITRLVSAFKLH-EQLNVPVQKLTTGTMRKLCFVLSLLG 1430
Cdd:COG0488 90 RALEAELEELEAKLAepdedlerlaelqeefealggweaearAEEILSGLGFPeEDLDRPVSELSGGWRRRVALARALLS 169
|
170
....*....|
gi 1622880985 1431 NSPVLLLDEP 1440
Cdd:COG0488 170 EPDLLLLDEP 179
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1292-1499 |
8.08e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 76.47 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1292 KSCFSKRKK---KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGhlgycpQENVLWP 1368
Cdd:PRK13545 25 KDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA------ISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1448
Cdd:PRK13545 99 QLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1449 QQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1499
Cdd:PRK13545 179 TKKCLDKMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIK 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
481-704 |
9.22e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 74.76 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSE--MQDleeiRKI 558
Cdd:PRK11432 9 LKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsIQQ----RDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCpQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:PRK11432 81 CMVF-QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSIFLKRR 704
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRElqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
479-698 |
1.22e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSG-----KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLsEMQDL- 552
Cdd:PRK15112 5 LEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 553 ---EEIRKI-----TGVCPQFNVQfDILTVKENLSlfakiKGIHPQEVEQEVQRILLELDMQNIQDNLAKH-LSEGQKRK 623
Cdd:PRK15112 84 yrsQRIRMIfqdpsTSLNPRQRIS-QILDFPLRLN-----TDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 624 LTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVI--LFSTQSMDEADILADRKVIMSNGRLKCAGSS 698
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1292-1501 |
1.30e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1292 KSCFSKRK-KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPtagevELKGCSSVL--GHL----------G 1358
Cdd:TIGR00955 28 RGCFCRERpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK-----GVKGSGSVLlnGMPidakemraisA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1359 YCPQENVLWPMLTAREHLEVYAAVKGLR---------KVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLL 1429
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREHLMFQAHLRMPRrvtkkekreRVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1430 GNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVkNTERGVLLTTHN-LAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1300-1492 |
1.43e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1300 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLG-HLGYCPQENVLWPMLTA 1372
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlSSRQLArRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 RE--------HLEVYA--AVKGLRKVDARLAITRLVsafklhEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:PRK11231 94 RElvaygrspWLSLWGrlSAEDNARVNQAMEQTRIN------HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1443 GIDPTGQ-------QQMWQAIQAVVKntergVLlttHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK11231 168 YLDINHQvelmrlmRELNTQGKTVVT-----VL---HDLNQASRYCDHLVVLANGHV 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
503-692 |
1.43e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QD--------LEEIRKITGVcpqfnvqfdIL 572
Cdd:PRK10762 273 FTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspQDglangivyISEDRKRDGL---------VL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 --TVKENLSL-----FAKIKG-IHPQEVEQEVQRIlleLDMQNI----QDNLAKHLSEGQKRKLTFGIAILGDPQILLLD 640
Cdd:PRK10762 344 gmSVKENMSLtalryFSRAGGsLKHADEQQAVSDF---IRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 641 EPTTGLDPFSRDQVWSLLREHRAD--HVILFSTQsMDEADILADRKVIMSNGRL 692
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEglSIILVSSE-MPEVLGMSDRILVMHEGRI 473
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1305-1481 |
1.60e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.13 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWPMLTAREHlev 1378
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdlcTYQKQLCFVGHRSGINPYLTLREN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 yaAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1458
Cdd:PRK13540 95 --CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170 180
....*....|....*....|....*...
gi 1622880985 1459 VVKNTErGVLLTTH-----NLAEAEALC 1481
Cdd:PRK13540 173 HRAKGG-AVLLTSHqdlplNKADYEEYH 199
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1305-1497 |
1.64e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.20 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQENVLWPMlTAREHL- 1376
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltlESLRRQIGVVPQDTFLFSG-TIRENIr 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1377 ---------EVYAAvkglrkvdARLA-ITRLVSAFKlhEQLNVPV----QKLTTGTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:COG1132 436 ygrpdatdeEVEEA--------AKAAqAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDEATS 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1443 GIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGS 1497
Cdd:COG1132 506 ALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1294-1501 |
2.06e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1294 CFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLGHLGYCPQE 1363
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenireVRKFVGLVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1364 NVLWPmlTAREHLEVYAAVKGLrkvDARLAITRLVSAFKLH--EQLNVPVQKLTTGTMRKLCFVLSLLGNSP-VLLLDEP 1440
Cdd:PRK13652 90 QIFSP--TVEQDIAFGPINLGL---DEETVAHRVSSALHMLglEELRDRVPHHLSGGEKKRVAIAGVIAMEPqVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
475-692 |
4.80e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 475 GKEAIRIRNVKKEYKGKsgkveaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLE- 553
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDa 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 554 ---------EIRKITGVCPQFnvqfdilTVKENLSLFAKIK--------GIHPQEVEQ---EVQRILLELDMQNIQDNLA 613
Cdd:PRK09700 336 vkkgmayitESRRDNGFFPNF-------SIAQNMAISRSLKdggykgamGLFHEVDEQrtaENQRELLALKCHSVNQNIT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 614 KhLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREhRADH--VILFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK09700 409 E-LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDgkVILMVSSELPEIITVCDRIAVFCEGR 486
|
.
gi 1622880985 692 L 692
Cdd:PRK09700 487 L 487
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1311-1488 |
5.09e-13 |
|
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: 73.67 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1311 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVE--LKgcssvlghLGYCPQEnvlwpmLTAREHLEVYAAVKGLRK- 1387
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedLK--------ISYKPQY------ISPDYDGTVEEFLRSANTd 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1388 -VDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERG 1466
Cdd:COG1245 429 dFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
170 180
....*....|....*....|..
gi 1622880985 1467 VLLTTHNLAEAEALCDRvaIMV 1488
Cdd:COG1245 509 AMVVDHDIYLIDYISDR--LMV 528
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1306-1503 |
5.26e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGH-------------LGYCPQENVLWPMLTA 1372
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsdkairelrrnVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHL-EVYAAVKGLRKVDA---------RLAITRLVSAFKLHeqlnvpvqkLTTGTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:PRK11124 100 QQNLiEAPCRVLGLSKDQAlaraeklleRLRLKPYADRFPLH---------LSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1443 GIDPTGQQQMWQAIQAVvknTERGV--LLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1503
Cdd:PRK11124 171 ALDPEITAQIVSIIREL---AETGItqVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1501 |
5.38e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.42 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV---------ELKGCSSVLGHLGYCPQ--ENVLWpmlT 1371
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidySRKGLMKLRESVGMVFQdpDNQLF---S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREHLEV-YAAVK-GLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1449
Cdd:PRK13636 98 ASVYQDVsFGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1450 QQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1303-1492 |
5.63e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 69.74 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLG--------HLGYCPQENVLWPMLTA 1372
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdVSDLRGraipylrrKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHLEVYAAVKGlrkVDARLAITRLVSAFKL----HEQLNVPVQkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTg 1448
Cdd:cd03292 96 YENVAFALEVTG---VPPREIRKRVPAALELvglsHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622880985 1449 qqQMWQAIQAVVKNTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:cd03292 171 --TTWEIMNLLKKINKAGttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
463-692 |
5.87e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 463 DDYFEPVAPEfQGKEAIRIRNVKKEykgksgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIY 542
Cdd:COG1129 242 EDLFPKRAAA-PGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 543 NKNLS-----EMQD-----LEEIRKITGVCPqfnvqfdILTVKENLSL-----FAKIKGIHPQEVEQEVQRILLELD--M 605
Cdd:COG1129 313 GKPVRirsprDAIRagiayVPEDRKGEGLVL-------DLSIRENITLasldrLSRGGLLDRRRERALAEEYIKRLRikT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 606 QNIqDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREhRADH---VILFSTQsMDEADILAD 682
Cdd:COG1129 386 PSP-EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE-LAAEgkaVIVISSE-LPELLGLSD 462
|
250
....*....|
gi 1622880985 683 RKVIMSNGRL 692
Cdd:COG1129 463 RILVMREGRI 472
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1303-1504 |
7.55e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGIT---KPTAGEVELKG----CSSVLG--------HLGYCPQENVLW 1367
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrtvqREGRLArdirksraNTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTAREHLEVYAA------------VKGLRKVDARLAITRLVSAFKLHEQlnvpVQKLTTGTMRKLCFVLSLLGNSPVL 1435
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcfswFTREQKQRALQALTRVGMVHFAHQR----VSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 1436 LLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1504
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
496-692 |
8.62e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 496 EALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD----------LEEIRKITG----- 560
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvyLPEDRQSSGlylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 561 -----VC--PQFNVQFDILTVKEN--LSLFAKIKGIHPQEVEQEVQRilleldmqniqdnlakhLSEGQKRKLTFGIAIL 631
Cdd:PRK15439 357 plawnVCalTHNRRGFWIKPARENavLERYRRALNIKFNHAEQAART-----------------LSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 632 GDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
479-691 |
9.04e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 69.04 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVE-ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsemqdleeirk 557
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 iTGVCPQFN-VQFDilTVKENLsLFAKIkgIHPQEVEQEVQRILLELDMQNIQDNLAKH-------LSEGQKRKLTFGIA 629
Cdd:cd03250 68 -IAYVSQEPwIQNG--TIRENI-LFGKP--FDEERYEKVIKACALEPDLEILPDGDLTEigekginLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 630 ILGDPQILLLDEPTTGLDPFSRDQVW-SLLREHRADH--VILfSTQSMdeaDIL--ADRKVIMSNGR 691
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNktRIL-VTHQL---QLLphADQIVVLDNGR 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1298-1495 |
1.21e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--------CSSVLGHLGYCPQ---ENVL 1366
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprspLDAVKKGMAYITEsrrDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1367 WPMLTAREHLEVYAAVK--------GL--RKVDARLA-ITRLVSAFKLHeQLNVPVQKLTTGTMRKLCFVLSLLGNSPVL 1435
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKdggykgamGLfhEVDEQRTAeNQRELLALKCH-SVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1436 LLDEPSTGIDPTGQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRLRCI 1495
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
479-692 |
1.99e-12 |
|
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: 71.64 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNILNGLSVPTEGSVTIYNKNLSEM--QDL 552
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLseREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 553 EEIR--KI--------TGVCPQFNV--QfdiltVKENLSLfakIKGIHPQEVEQEVQRILLELDMQNIQDNLAK--H-LS 617
Cdd:COG4172 87 RRIRgnRIamifqepmTSLNPLHTIgkQ-----IAEVLRL---HRGLSGAAARARALELLERVGIPDPERRLDAypHqLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 618 EGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQsmdeaDI-----LADRKVIMSNG 690
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITH-----DLgvvrrFADRVAVMRQG 233
|
..
gi 1622880985 691 RL 692
Cdd:COG4172 234 EI 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1307-1472 |
2.06e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLG----HLGYCPQENVLWPMLTAREHLEVYAAV 1382
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdrsrFMAYLGHLPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1383 KGLRKVD---ARLAITRLVSafklHEQlnVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAV 1459
Cdd:PRK13543 110 HGRRAKQmpgSALAIVGLAG----YED--TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAH 183
|
170
....*....|...
gi 1622880985 1460 VKnTERGVLLTTH 1472
Cdd:PRK13543 184 LR-GGGAALVTTH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1307-1500 |
2.42e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLG--------YCP----QENVLwPMLTARE 1374
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagimLCPedrkAEGII-PVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HLEVYAAVKGLR-------KVDARLA---ITRLVSAFKLHEQlnvPVQKLTTGTMRKLcfVLS--LLGNSPVLLLDEPST 1442
Cdd:PRK11288 351 NINISARRHHLRagclinnRWEAENAdrfIRSLNIKTPSREQ---LIMNLSGGNQQKA--ILGrwLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1443 GIDPTGQQQMWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRLRciGSIQH 1500
Cdd:PRK11288 426 GIDVGAKHEIYNVIYEL---AAQGvaVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1305-1492 |
2.72e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLG----------HLGYCPQENVLWPMLTAR 1373
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmSKLSsaakaelrnqKLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1453
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622880985 1454 QAIQAVVKNTERGVLLTTHNLAEAEALcDRVAIMVSGRL 1492
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1492 |
2.90e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.95 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------------CSSVLGHLGYCPQENVLWPml 1370
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkslleVRKTVGIVFQNPDDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 TAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1450
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622880985 1451 QMWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK13639 175 QIMKLLYDL---NKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
494-647 |
3.09e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 72.19 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 494 KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVP--TEGSVTI--YNKNLsemqdlEEIRKITGVCPQFNVQF 569
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRIsgFPKKQ------ETFARISGYCEQNDIHS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 570 DILTVKENL--SLFAKIkgihPQEVEQE-----VQRILLELDMQNIQDNLA-----KHLSEGQKRKLTFGIAILGDPQIL 637
Cdd:PLN03140 966 PQVTVRESLiySAFLRL----PKEVSKEekmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSII 1041
|
170
....*....|
gi 1622880985 638 LLDEPTTGLD 647
Cdd:PLN03140 1042 FMDEPTSGLD 1051
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1295-1492 |
3.12e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.72 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGHL------------GYCP 1361
Cdd:COG1135 11 FPTKGGPVTAlDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG--VDLTALserelraarrkiGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1362 Q-----------ENVLWPMLTA-----------REHLEVyaaVkGLR-KVDA-----------RLAITRlvsAfklheql 1407
Cdd:COG1135 89 QhfnllssrtvaENVALPLEIAgvpkaeirkrvAELLEL---V-GLSdKADAypsqlsggqkqRVGIAR---A------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1408 nvpvqklttgtmrklcfvlslLGNSP-VLLLDEPSTGIDP-TGQQqmwqaIQAVVK--NTERG--VLLTTHNLAEAEALC 1481
Cdd:COG1135 155 ---------------------LANNPkVLLCDEATSALDPeTTRS-----ILDLLKdiNRELGltIVLITHEMDVVRRIC 208
|
250
....*....|.
gi 1622880985 1482 DRVAIMVSGRL 1492
Cdd:COG1135 209 DRVAVLENGRI 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1280-1492 |
3.33e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.56 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1280 ASCLHKEYAGQkkSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLGHL-- 1357
Cdd:PRK10419 6 VSGLSHHYAHG--GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP--LAKLnr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1358 -------------------GYCPQENVLW----PM-----LTAREHLEVYAAVkgLRKVDARLAItrlvsAFKLHEQlnv 1409
Cdd:PRK10419 82 aqrkafrrdiqmvfqdsisAVNPRKTVREiirePLrhllsLDKAERLARASEM--LRAVDLDDSV-----LDKRPPQ--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1410 pvqkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVS 1489
Cdd:PRK10419 152 ----LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
...
gi 1622880985 1490 GRL 1492
Cdd:PRK10419 228 GQI 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
510-692 |
3.34e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 510 ITAILGHSGAGKSSLLNILNGLSVPTEG-----SVTIYNKNLSEMQDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKI 584
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 585 KGIHPQEVEQEVQRILLELDMQN-IQDNLAK---HLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE 660
Cdd:PRK14271 129 KLVPRKEFRGVAQARLTEVGLWDaVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190
....*....|....*....|....*....|..
gi 1622880985 661 HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK14271 209 LADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1311-1488 |
3.70e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1311 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV--ELKgcssvlghLGYCPQEnvlwpmLTAREHLEVYAAvkgLRKV 1388
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpELK--------ISYKPQY------IKPDYDGTVEDL---LRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1389 DARLA----ITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTE 1464
Cdd:PRK13409 425 TDDLGssyyKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEERE 504
|
170 180
....*....|....*....|....
gi 1622880985 1465 RGVLLTTHNLAEAEALCDRvaIMV 1488
Cdd:PRK13409 505 ATALVVDHDIYMIDYISDR--LMV 526
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
496-711 |
4.24e-12 |
|
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: 70.92 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 496 EALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDiLTVK 575
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHTLRQFINYLPQEPYIFS-GSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 576 ENLSLFAKiKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSE-------GQKRKLTFGIAILGDPQILLLDEPTTGLDp 648
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEegssisgGQKQRIALARALLTDSKVLILDESTSNLD- 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 649 fsrdqvwsLLREHR--------ADHVILFSTQSMDEADiLADRKVIMSNGRLKCAGSSIFLKRRWGLGYHL 711
Cdd:TIGR01193 644 --------TITEKKivnnllnlQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
503-676 |
4.60e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.43 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDlEEIRKITGVCPQFNVQF-DilTVKENLSLF 581
Cdd:PRK10247 28 FSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFgD--TVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 582 AKIKGIHPQEveqevQRILLELDMQNIQDNLAKH----LSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSL 657
Cdd:PRK10247 105 WQIRNQQPDP-----AIFLDDLERFALPDTILTKniaeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
|
170 180
....*....|....*....|.
gi 1622880985 658 LREHRADHVI--LFSTQSMDE 676
Cdd:PRK10247 180 IHRYVREQNIavLWVTHDKDE 200
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1305-1499 |
5.06e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.83 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVL-GHLGYCPQENVL-WPmLTARE-- 1374
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawSPWELaRRRAVLPQHSSLaFP-FTVEEvv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 ------HLEVYAAVKGLrkVDARLAITRLVSafkLHEQLnvpVQKLTTGTM------RKLCFVLSLLGNSP-VLLLDEPS 1441
Cdd:COG4559 97 algrapHGSSAAQDRQI--VREALALVGLAH---LAGRS---YQTLSGGEQqrvqlaRVLAQLWEPVDGGPrWLFLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1442 TGIDPTGQQQMwqaIQAVVKNTERG--VLLTTH--NLAeaeAL-CDRVAIMVSGRLRCIGSIQ 1499
Cdd:COG4559 169 SALDLAHQHAV---LRLARQLARRGggVVAVLHdlNLA---AQyADRILLLHQGRLVAQGTPE 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1295-1475 |
5.44e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 67.25 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQ----- 1362
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrKSLRSMIGVVLQdtflf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1363 -----ENVLWPMLTAREHLEVYAAvkglRKVDARLAITRLVSAfkLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLL 1437
Cdd:cd03254 90 sgtimENIRLGRPNATDEEVIEAA----KEAGAHDFIMKLPNG--YDTVLGENGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622880985 1438 DEPSTGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLA 1475
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLS 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1303-1492 |
6.51e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLG------HLG----YcpQENVLWPMLTA 1372
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAsttaalAAGvaiiY--QELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHLEVYAAVKGLRKVDARLAITRLVSAFK-LHEQL--NVPVQKLTTGT--MRKLCFVLSLlgNSPVLLLDEPSTGIDPT 1447
Cdd:PRK11288 97 AENLYLGQLPHKGGIVNRRLLNYEAREQLEhLGVDIdpDTPLKYLSIGQrqMVEIAKALAR--NARVIAFDEPTSSLSAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1448 GQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK11288 175 EIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
468-697 |
8.17e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.99 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 468 PVAPEFQG-KEAIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL 546
Cdd:PRK13657 323 PGAIDLGRvKGAVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 547 SEMqDLEEIRKITGVCPQFNVQFDiLTVKENLSLfakikGiHPQEVEQEVQRIL-----LELDMQNIQ--DNLA----KH 615
Cdd:PRK13657 400 RTV-TRASLRRNIAVVFQDAGLFN-RSIEDNIRV-----G-RPDATDEEMRAAAeraqaHDFIERKPDgyDTVVgergRQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 616 LSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLL---REHRADHVILFSTQSMDEadilADRKVIMSNGRL 692
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdelMKGRTTFIIAHRLSTVRN----ADRILVFDNGRV 547
|
....*
gi 1622880985 693 KCAGS 697
Cdd:PRK13657 548 VESGS 552
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
498-693 |
8.62e-12 |
|
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: 67.57 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLsVPTEGSVTIYNKNLSEMQdLEEIRKITGVCPQFNVQFDiLTVKEN 577
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKAFGVIPQKVFIFS-GTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 578 LSLFAKIKgihpqevEQEVQRILLELDMQNIQDNLAKHL-----------SEGQKRKLTFGIAILGDPQILLLDEPTTGL 646
Cdd:cd03289 97 LDPYGKWS-------DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622880985 647 DPFSRDQVWSLLREHRADHVILFSTQSMdEADILADRKVIMSNGRLK 693
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1300-1504 |
8.89e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.55 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1300 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-----------KGCSSVLGHLGYCPQ--ENVL 1366
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetgnKNLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1367 WPMlTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQL-NVPVQKLTTGTMRKLCfVLSLLGNSP-VLLLDEPSTGI 1444
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVA-IAGVMAYEPeILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1445 DPTGQQQMWQaiqaVVKNTERG---VLLTTHNLAEAEALCDRVAIMVSGRLrcigsIQHLKNK 1504
Cdd:PRK13641 177 DPEGRKEMMQ----LFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1283-1477 |
9.69e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.03 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1283 LHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG---HLGY 1359
Cdd:PRK11248 7 LYADYGGKP-----------ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-KPVEGpgaERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1360 CPQENVLWPMLTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDE 1439
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622880985 1440 PSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEA 1477
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1287-1523 |
1.06e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1287 YAGQKKSCFSKRkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-----------KGCSSVLG 1355
Cdd:PRK13646 10 YTYQKGTPYEHQ----AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditithktkdKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1356 HLGYCPQ--ENVLWPMLTAREHLEVYAAVK-GLRKVDARlaitrlvsAFKLHEQL----NV----PVQkLTTGTMRKLCF 1424
Cdd:PRK13646 86 RIGMVFQfpESQLFEDTVEREIIFGPKNFKmNLDEVKNY--------AHRLLMDLgfsrDVmsqsPFQ-MSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1425 VLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1504
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
250
....*....|....*....
gi 1622880985 1505 lgKDYILELKVKEPSQVTL 1523
Cdd:PRK13646 237 --KKKLADWHIGLPEIVQL 253
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
479-698 |
1.07e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.96 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL----SVPtEGSVTIYNKNLSE----MQ 550
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSA-GSHIELLGRTVQRegrlAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 551 DLEEIRKITG-VCPQFNVqFDILTVKENLSLFAKikGIHP----------QEVEQEVQRILLELDMQNIQDNLAKHLSEG 619
Cdd:PRK09984 80 DIRKSRANTGyIFQQFNL-VNRLSVLENVLIGAL--GSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 620 QKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-HRADHVILFST-QSMDEADILADRKVIMSNGRLKCAGS 697
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGS 236
|
.
gi 1622880985 698 S 698
Cdd:PRK09984 237 S 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1302-1491 |
1.24e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1302 IAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGHLGYCPQ--------ENV-LWPMLTA 1372
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG-QHIEGLPGHQIArmgvvrtfQHVrLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 RE------HLEVYAAV-KGLRKVDA-----RLAITRLVSAFK---LHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLL 1437
Cdd:PRK11300 98 IEnllvaqHQQLKTGLfSGLLKTPAfrraeSEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1438 DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1301-1511 |
1.24e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1301 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLG-------------HLGYCPQENVLW 1367
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGkdifqidaiklrkEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTAREHLEVYAAVKGLRKVDARLAIT----RLVSAFK-LHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVeeclRKVGLWKeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1443 GIDPTGQQQMWQAIQAVVKntERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL----KNKLGKDYIL 1511
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
468-693 |
1.41e-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: 69.08 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 468 PVAPEFQGKEAIRIRNVKKeYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGlSVPT--EGSVTIYNKN 545
Cdd:TIGR02633 247 PHEPHEIGDVILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKP 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 546 LSEMQDLEEI----------RKITGVCPQFNVQFDI-LTVkenLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLA- 613
Cdd:TIGR02633 325 VDIRNPAQAIragiamvpedRKRHGIVPILGVGKNItLSV---LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPi 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 614 KHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQsMDEADILADRKVIMSNGR 691
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEGK 480
|
..
gi 1622880985 692 LK 693
Cdd:TIGR02633 481 LK 482
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1294-1506 |
1.46e-11 |
|
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: 66.10 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1294 CFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVL 1366
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtLDSLRRAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1367 W----------PMLTAREHlEVYAAVKglrkvdarlaitrlvsAFKLHEQ-LNVPVQ----------KLTTGTMRKLCFV 1425
Cdd:cd03253 87 FndtigyniryGRPDATDE-EVIEAAK----------------AAQIHDKiMRFPDGydtivgerglKLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1426 LSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQHLKNKL 1505
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKG 226
|
.
gi 1622880985 1506 G 1506
Cdd:cd03253 227 G 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
468-691 |
1.75e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 69.08 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 468 PVAPEFQGKEA-IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL 546
Cdd:COG5265 346 PDAPPLVVGGGeVRFENVSFGYDPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 547 SEMQdLEEIRKITGVCPQ----FNvqfDilTVKENLSlFAKIkGIHPQEVEQEVQrilleldMQNIQDNLAK-------- 614
Cdd:COG5265 423 RDVT-QASLRAAIGIVPQdtvlFN---D--TIAYNIA-YGRP-DASEEEVEAAAR-------AAQIHDFIESlpdgydtr 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 615 ------HLSEGQKRKLtfGIA--ILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVIL-----FSTqSMDeadilA 681
Cdd:COG5265 488 vgerglKLSGGEKQRV--AIArtLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLviahrLST-IVD-----A 559
|
250
....*....|
gi 1622880985 682 DRKVIMSNGR 691
Cdd:COG5265 560 DEILVLEAGR 569
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1283-1492 |
1.82e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.52 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1283 LHKEYAGqkkscfsKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLG------ 1355
Cdd:PRK11153 7 ISKVFPQ-------GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDlTALSekelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1356 ---HLGYCPQ-----------ENVLWPML---TAREHLEvyaavkglRKVDARLAitrLVSafkLHEQLNV-PV-----Q 1412
Cdd:PRK11153 80 arrQIGMIFQhfnllssrtvfDNVALPLElagTPKAEIK--------ARVTELLE---LVG---LSDKADRyPAqlsggQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1413 KLTTGTMRKlcfvlslLGNSP-VLLLDEPSTGIDPtgqqQMWQAIQAVVK--NTERG--VLLTTHNLAEAEALCDRVAIM 1487
Cdd:PRK11153 146 KQRVAIARA-------LASNPkVLLCDEATSALDP----ATTRSILELLKdiNRELGltIVLITHEMDVVKRICDRVAVI 214
|
....*
gi 1622880985 1488 VSGRL 1492
Cdd:PRK11153 215 DAGRL 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
482-691 |
2.15e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.98 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 482 RNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPT---EGSVTiYNkNLSEMQDLEEIRKI 558
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIH-YN-GIPYKEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGihpqeveqevqrilleldmqniqDNLAKHLSEGQKRKLTFGIAILGDPQILL 638
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 639 LDEPTTGLDPFSRDQVWSLLRE--HRADHVILFS-TQSMDEADILADRKVIMSNGR 691
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTmaDVLKTTTFVSlYQASDEIYDLFDKVLVLYEGR 197
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
493-660 |
2.23e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.16 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKItGVCPQFNVQFDIL 572
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI-GLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 TVKENLSlfakiKGIHP---------QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPT 643
Cdd:PRK10253 97 TVQELVA-----RGRYPhqplftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170
....*....|....*..
gi 1622880985 644 TGLDPFSRDQVWSLLRE 660
Cdd:PRK10253 172 TWLDISHQIDLLELLSE 188
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1296-1492 |
2.35e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.07 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1296 SKR--KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLGHL------------GYCP 1361
Cdd:COG2884 8 SKRypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD--LSRLkrreipylrrriGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1362 Q-----------ENVLWPMLtarehlevyaaVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLG 1430
Cdd:COG2884 86 QdfrllpdrtvyENVALPLR-----------VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1431 NSPVLLLDEPSTGIDPTGQQQMWQAIQAVvkNtERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEI--N-RRGttVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
479-692 |
2.35e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.25 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYK-----GKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLE 553
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL-NRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 554 EIR------------KITGVCPQFNVQfDILtvKENLSlfaKIKGIHPQEVEQEVQRILLELDMQ-NIQDNLAKHLSEGQ 620
Cdd:PRK10419 83 QRKafrrdiqmvfqdSISAVNPRKTVR-EII--REPLR---HLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 621 KRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1305-1511 |
2.46e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 65.59 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMlTAREHLE 1377
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladPAWLRRQVGVVLQENVLFNR-SIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 VYAAVKGLRKVdarLAITRLVSA----FKLHEQLNVPVQK----LTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1449
Cdd:cd03252 98 LADPGMSMERV---IEAAKLAGAhdfiSELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1450 QQMWQAIQAVVKNteRGVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLGKDYIL 1511
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1316-1501 |
2.89e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1316 ILGLLGPNGAGKSSSIRMISGITKPTAG-----EVELKGCS-----SVLG---HLGYCPQENVLWPMLTAREhleVYAAV 1382
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSifnyrDVLEfrrRVGMLFQRPNPFPMSIMDN---VLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1383 KGLRKV---------DARLAITRLVSAFKlhEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1453
Cdd:PRK14271 126 RAHKLVprkefrgvaQARLTEVGLWDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622880985 1454 QAIQAVVKNTErgVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK14271 204 EFIRSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
470-647 |
2.91e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.21 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 470 APEF-QGKeaIRIRNVKKEYKGKSgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSE 548
Cdd:TIGR00958 471 APLNlEGL--IEFQDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 549 MqDLEEIRKITGVCPQFNVQFDiLTVKENLSL---FAKIKGIHPQEVEQEVQRILLELDmQNIQDNLAKH---LSEGQKR 622
Cdd:TIGR00958 548 Y-DHHYLHRQVALVGQEPVLFS-GSVRENIAYgltDTPDEEIMAAAKAANAHDFIMEFP-NGYDTEVGEKgsqLSGGQKQ 624
|
170 180
....*....|....*....|....*
gi 1622880985 623 KLTFGIAILGDPQILLLDEPTTGLD 647
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALD 649
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1295-1501 |
2.92e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVElkgCSSVL------------------- 1354
Cdd:PRK10261 22 FMQEQQKIAAvRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ---CDKMLlrrrsrqvielseqsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1355 -----GHLGYCPQENV--LWPMLTAREHL-EVYAAVKGLRKVDArlaitrLVSAFKLHEQLNVPVQKLT--------TGT 1418
Cdd:PRK10261 99 rhvrgADMAMIFQEPMtsLNPVFTVGEQIaESIRLHQGASREEA------MVEAKRMLDQVRIPEAQTIlsryphqlSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1419 MRKLCFVLSLLGNSP-VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:PRK10261 173 MRQRVMIAMALSCRPaVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
....
gi 1622880985 1498 IQHL 1501
Cdd:PRK10261 253 VEQI 256
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1305-1484 |
3.37e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 62.85 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQenvlwpmLTAREHlevyaavkg 1384
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI----GYFEQ-------LSGGEK--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1385 lrkvdARLAITRLvsafklheqlnvpvqklttgtmrklcfvlsLLGNSPVLLLDEPSTGIDPTGQqqmwQAIQAVVKNTE 1464
Cdd:cd03221 77 -----MRLALAKL------------------------------LLENPNLLLLDEPTNHLDLESI----EALEEALKEYP 117
|
170 180
....*....|....*....|
gi 1622880985 1465 RGVLLTTHNLAEAEALCDRV 1484
Cdd:cd03221 118 GTVILVSHDRYFLDQVATKI 137
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
493-696 |
3.76e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.17 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVcPQ-----FNv 567
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV-PQdtslsFE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 568 qFDILTVKE-----NLSLFAKIKGIHPQEVEQEVQRIllelDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEP 642
Cdd:PRK09536 92 -FDVRQVVEmgrtpHRSRFDTWTETDRAAVERAMERT----GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 643 TTGLDPFSRDQVWSLLREHRAD-HVILFSTQSMDEADILADRKVIMSNGRLKCAG 696
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1316-1497 |
3.78e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1316 ILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLGYC------------PQENVLWPMLTArehlEVYAAVK 1383
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLalrqqvatvfqdPEQQIFYTDIDS----DIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1384 GL--------RKVDARLAitrLVSAFKLHEQlnvPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1455
Cdd:PRK13638 105 NLgvpeaeitRRVDEALT---LVDAQHFRHQ---PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 1456 IQAVVKNTERgVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:PRK13638 179 IRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1306-1526 |
3.83e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.52 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcsSVLGHLgyCPQENVlWPMltaREHLE-------- 1377
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI------IIDGDL--LTEENV-WDI---RHKIGmvfqnpdn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 --VYAAV----------KGL------RKVDARLAITRLvSAFKLHEQlnvpvQKLTTGTMRKLCFVLSLLGNSPVLLLDE 1439
Cdd:PRK13650 93 qfVGATVeddvafglenKGIpheemkERVNEALELVGM-QDFKEREP-----ARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1440 PSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQHLKNKlGKDyILELKVKEPS 1519
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR-GND-LLQLGLDIPF 243
|
....*..
gi 1622880985 1520 QVTLVHT 1526
Cdd:PRK13650 244 TTSLVQS 250
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1303-1492 |
3.91e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcssvlghlgycpQENVLWPmlTAREHLEVYAAV 1382
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG------------KDITDWQ--TAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1383 KGLRKVDARLA--------------------ITRLVSAF-KLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPS 1441
Cdd:PRK11614 86 PEGRRVFSRMTveenlamggffaerdqfqerIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQL---REQGmtIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
481-660 |
4.08e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKSGK---------VEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD 551
Cdd:PRK15079 11 VADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 552 LE--EIRK---------ITGVCPQFNVQfDIltVKENLSLFakikgiHP----QEVEQEVQRILLELDM-QNIQDNLAKH 615
Cdd:PRK15079 91 DEwrAVRSdiqmifqdpLASLNPRMTIG-EI--IAEPLRTY------HPklsrQEVKDRVKAMMLKVGLlPNLINRYPHE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622880985 616 LSEGQKRKLtfGIA---ILgDPQILLLDEPTTGLDPFSRDQVWSLLRE 660
Cdd:PRK15079 162 FSGGQCQRI--GIAralIL-EPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1311-1486 |
4.61e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 63.36 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1311 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlgYCPQenvlwpmltarehlevyaavkglrKVDa 1390
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-----YKPQ------------------------YID- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1391 rlaitrlvsafklheqlnvpvqkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLT 1470
Cdd:cd03222 72 -----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVV 128
|
170
....*....|....*.
gi 1622880985 1471 THNLAEAEALCDRVAI 1486
Cdd:cd03222 129 EHDLAVLDYLSDRIHV 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
497-687 |
4.74e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 497 ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemQDLEEirKITGVCPQFN-VQFDILTVK 575
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQK--NLVAYVPQSEeVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 576 ENLSLFAKIKGI----HPQEVEQE-VQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFS 650
Cdd:PRK15056 98 EDVVMMGRYGHMgwlrRAKKRDRQiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622880985 651 RDQVWSLLREHRAD-HVILFSTQSMDEADILADRKVIM 687
Cdd:PRK15056 178 EARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1305-1492 |
5.91e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGH----------------------LGYCPQ 1362
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglangivyisedrkrdglvLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1363 ENVlwpMLTAREHLEvYAAVKgLRKVDARLAITRLVSAFKLH----EQlnvPVQKLTTGTMRKLCFVLSLLGNSPVLLLD 1438
Cdd:PRK10762 349 ENM---SLTALRYFS-RAGGS-LKHADEQQAVSDFIRLFNIKtpsmEQ---AIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1439 EPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQ-FKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1303-1543 |
5.96e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.01 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV-----------ELKGCSSVLGHLGYCPQENVLWPmlT 1371
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsKLQGIRKLVGIVFQNPETQFVGR--T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRklCFVLS-LLGNSP-VLLLDEPSTGIDPTGQ 1449
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQ--CVALAgILTMEPeCLIFDEVTSMLDPDSG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1450 QQMWQAIQavvKNTERG--VLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLGKDYileLKVKEPSQVTLvhTE 1527
Cdd:PRK13644 173 IAVLERIK---KLHEKGktIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQT---LGLTPPSLIEL--AE 243
|
250
....*....|....*.
gi 1622880985 1528 ILKLFPQAAGQERYSS 1543
Cdd:PRK13644 244 NLKMHGVVIPWENTSS 259
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1305-1533 |
6.32e-11 |
|
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: 64.88 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSS----SIRMISgitkpTAGEVELKGCSSVLGHL-------GYCPQENVLWPMlTAR 1373
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGDIQIDGVSWNSVPLqkwrkafGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHLEVYAAVKG--LRKVDARLAITRLVSAF--KLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTgq 1449
Cdd:cd03289 95 KNLDPYGKWSDeeIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1450 qqMWQAIQAVVKNTERG--VLLTTHNLaEAEALCDRVAIMVSGRLRCIGSIQHLKNKlgkdyilelkvKEPSQVTLVHTE 1527
Cdd:cd03289 173 --TYQVIRKTLKQAFADctVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFKQAISPSD 238
|
....*.
gi 1622880985 1528 ILKLFP 1533
Cdd:cd03289 239 RLKLFP 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1305-1492 |
8.40e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV-----ELKGCSSV----LGhLGYCPQE------------ 1363
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRImlngkEINALSTAqrlaRG-LVYLPEDrqssglyldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1364 --NV---------LWpMLTAREH--LEVYAAVKGLRKVDArlaitrlvsafklhEQlnvPVQKLTTGTMRKLCFVLSLLG 1430
Cdd:PRK15439 359 awNVcalthnrrgFW-IKPARENavLERYRRALNIKFNHA--------------EQ---AARTLSGGNQQKVLIAKCLEA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1431 NSPVLLLDEPSTGIDPTGQQQMWQAIQAVVK-NTerGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1307-1492 |
8.83e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITkPTAGEVELKGCS------SVLGHL-GY-CPQENVL-----WPMLTar 1373
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPleawsaAELARHrAYlSQQQTPPfampvFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 ehLEVYAavkGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSP-------VLLLDEPSTGIDP 1446
Cdd:PRK03695 92 --LHQPD---KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622880985 1447 TGQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK03695 167 AQQAALDRLLSELCQQG-IAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1307-1492 |
9.77e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.09 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITkPTAGEVELKG-----CS-SVLGHL-GYCPQENVLWPMLTAREHLEVY 1379
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGrplsdWSaAELARHrAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1380 AAvKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPV-------LLLDEPSTGIDPTGQQQM 1452
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTinpegqlLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 1453 WQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG4138 173 DRLLREL---CQQGitVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1311-1487 |
9.81e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1311 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-SSVLGH-----LG--------------YCPQENVLWPMl 1370
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwDEVLKRfrgteLQnyfkklyngeikvvHKPQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 tarehlevyaAVKG-----LRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGID 1445
Cdd:PRK13409 175 ----------VFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 1446 PTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAEALCDRVAIM 1487
Cdd:PRK13409 245 IRQRLNVARLIRELAEG--KYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
468-697 |
1.22e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 468 PVAPEFQGKEAIRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNILNGLSVPTE-GSVTIY 542
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQcDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 543 NKN-----LSEMQD--LEEIR----------KITGVCPQFNVQFDIltvKENLSLFakiKGIHPQEVEQEVQRILLELDM 605
Cdd:PRK10261 82 RRSrqvieLSEQSAaqMRHVRgadmamifqePMTSLNPVFTVGEQI---AESIRLH---QGASREEAMVEAKRMLDQVRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 606 QNIQDNLAKH---LSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLR--EHRADHVILFSTQSMDEADIL 680
Cdd:PRK10261 156 PEAQTILSRYphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEI 235
|
250
....*....|....*..
gi 1622880985 681 ADRKVIMSNGRLKCAGS 697
Cdd:PRK10261 236 ADRVLVMYQGEAVETGS 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1306-1475 |
1.51e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKgcSSVlgHLGYCPQEnvlwpmltaREHLE----VYAA 1381
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETV--KLAYVDQS---------RDALDpnktVWEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1382 VK--------GLRKVDARLAITRLvsAFKLHEQlNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1453
Cdd:TIGR03719 407 ISggldiiklGKREIPSRAYVGRF--NFKGSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALE 483
|
170 180
....*....|....*....|....*....
gi 1622880985 1454 QAIQ-----AVVKNTERGVL--LTTHNLA 1475
Cdd:TIGR03719 484 EALLnfagcAVVISHDRWFLdrIATHILA 512
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1298-1490 |
1.80e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcsSVLGH----------LGYCPQ-ENVL 1366
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI------SILGQptrqalqknlVAYVPQsEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1367 WPMLTAREHLEV---YAAVKGLRKVDA--RLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPS 1441
Cdd:PRK15056 91 WSFPVLVEDVVMmgrYGHMGWLRRAKKrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622880985 1442 TGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDrVAIMVSG 1490
Cdd:PRK15056 171 TGVDVKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1303-1491 |
1.87e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.84 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGE---------VELKGCSS--VL----GHLGYCPQ-ENVL 1366
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwVDLAQASPreILalrrRTIGYVSQfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1367 wPMLTArehLEVYAAVKGLRKVDARLAITRlvsAFKLHEQLNVPvQKL-----TT---GTMRKLCFVLSLLGNSPVLLLD 1438
Cdd:COG4778 106 -PRVSA---LDVVAEPLLERGVDREEARAR---ARELLARLNLP-ERLwdlppATfsgGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1439 EPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:COG4778 178 EPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1301-1539 |
2.31e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.18 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1301 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLGH------LGYCPQen 1364
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeykRAKYIGRvfqdpmMGTAPS-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1365 vlwpmLTAREHLEVyAAVKGLRKvDARLAITR--------LVSAFK--LHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPV 1434
Cdd:COG1101 97 -----MTIEENLAL-AYRRGKRR-GLRRGLTKkrrelfreLLATLGlgLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1435 LLLDEPSTGIDP-TGQQQMwQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLrcigsiqhlknklgkdyILEL 1513
Cdd:COG1101 170 LLLDEHTAALDPkTAALVL-ELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI-----------------ILDV 231
|
250 260
....*....|....*....|....*.
gi 1622880985 1514 KVKEPSQVTLvhTEILKLFPQAAGQE 1539
Cdd:COG1101 232 SGEEKKKLTV--EDLLELFEEIRGEE 255
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1305-1492 |
3.43e-10 |
|
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: 61.72 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLGHLGYCP-------QENVLW 1367
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkyLHSKVSLVGQEPvlfarslQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTAREHLEVYAAVKGlrkvDARLAITRLVSAFklHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1447
Cdd:cd03248 111 GLQSCSFECVKEAAQKA----HAHSFISELASGY--DTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1448 GQQQMWQAIQAvvKNTERGVLLTTHNLAEAEAlCDRVAIMVSGRL 1492
Cdd:cd03248 185 SEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1307-1492 |
3.80e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.07 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTA-----GEVELKGCSSVLG----------HLGYCPQENVLWPMLT 1371
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTARSLSQqkglirqlrqHVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREH-LEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1450
Cdd:PRK11264 102 VLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 1451 QMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK11264 182 EVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
478-692 |
4.33e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 557
Cdd:PLN03232 1234 SIKFEDVHLRYR--PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF-GLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNVQFDiLTVKENLSLFAK------IKGIHPQEVEQEVQRILLELDMQNIQDnlAKHLSEGQKRKLTFGIAIL 631
Cdd:PLN03232 1311 VLSIIPQSPVLFS-GTVRFNIDPFSEhndadlWEALERAHIKDVIDRNPFGLDAEVSEG--GENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 632 GDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEAdILADRKVIMSNGRL 692
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQV 1447
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
479-641 |
5.59e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSGKVEALKGLL----------------FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiy 542
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDLFfrskdgeyhyalnnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 543 nknlsemqDLEEIRKITGVCPQFNVQfdiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKR 622
Cdd:PRK13545 82 --------DIKGSAALIAISSGLNGQ---LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKS 150
|
170
....*....|....*....
gi 1622880985 623 KLTFGIAILGDPQILLLDE 641
Cdd:PRK13545 151 RLGFAISVHINPDILVIDE 169
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
481-696 |
5.63e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.62 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSV--PTEGSVTIYNKNLSEM--------- 549
Cdd:COG0396 3 IKNLHVSVEGK----EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELspderarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 550 -----QDLEEIRKITgvcpqfNVQFdILTVKENLSLfakiKGIHPQEVEQEVQRILLELDMQN--IQDNLAKHLSEGQKR 622
Cdd:COG0396 79 iflafQYPVEIPGVS------VSNF-LRTALNARRG----EELSAREFLKLLKEKMKELGLDEdfLDRYVNEGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 623 KL-TFGIAILgDPQILLLDEPTTGLDpfsrdqVWSL---------LR-EHRAdhVILFSTQS--MDEadILADRKVIMSN 689
Cdd:COG0396 148 RNeILQMLLL-EPKLAILDETDSGLD------IDALrivaegvnkLRsPDRG--ILIITHYQriLDY--IKPDFVHVLVD 216
|
....*..
gi 1622880985 690 GRLKCAG 696
Cdd:COG0396 217 GRIVKSG 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
456-691 |
5.85e-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: 63.94 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 456 IDAEhPSddyFEPVAPEFQGKEAIRIRNVKKEYKGKSG-------KVEALKGLLFDIYEGQITAILGHSGAGKSSL-LNI 527
Cdd:COG4172 257 LAAE-PR---GDPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 528 LnGLsVPTEGSVTIYNKNLSEM--QDLEEIRKitgvcpQFNVQF--------------DILTvkENLSLFAkiKGIHPQE 591
Cdd:COG4172 333 L-RL-IPSEGEIRFDGQDLDGLsrRALRPLRR------RMQVVFqdpfgslsprmtvgQIIA--EGLRVHG--PGLSAAE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 592 VEQEVQRILLELDMqniqDNLAKH-----LSEGQKRKLtfGIA---ILgDPQILLLDEPTTGLDPFSRDQVWSLLREHRA 663
Cdd:COG4172 401 RRARVAEALEEVGL----DPAARHrypheFSGGQRQRI--AIAralIL-EPKLLVLDEPTSALDVSVQAQILDLLRDLQR 473
|
250 260 270
....*....|....*....|....*....|
gi 1622880985 664 DHVI--LFSTQSMDEADILADRKVIMSNGR 691
Cdd:COG4172 474 EHGLayLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
498-647 |
5.87e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL--SVPTEGSVTIYNKNLSEmqdleEIRKITGVCPQFNVQFDILTVK 575
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 576 ENL---SLFAKIKGIHPQEVEQEVQRILLELDMQN-----IQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLD 647
Cdd:PLN03211 159 ETLvfcSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1305-1497 |
6.58e-10 |
|
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: 60.97 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSI----RMISgitkPTAGEVELKGCS-SVLG------HLGYCPQENVLWPMlTAR 1373
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILIDGVDiSKIGlhdlrsRISIIPQDPVLFSG-TIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHL---------EVYAAvkgLRKVDARLAITrlvsafKLHEQLNVPVQK----LTTGTMRKLCFVLSLLGNSPVLLLDEP 1440
Cdd:cd03244 96 SNLdpfgeysdeELWQA---LERVGLKEFVE------SLPGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLaEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:cd03244 167 TASVDPETDALIQKTIREAFKD--CTVLTIAHRL-DTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1295-1493 |
7.04e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKpTAGEVELKGCSSVLGHLGYCPQENV--------- 1365
Cdd:PRK14258 15 FYYDTQKIL-EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1366 ------LWPMlTAREHLEVYAAVKGLR-KVDARLAITRLVSAFKLHEQLNVPVQK----LTTGTMRKLCFVLSLLGNSPV 1434
Cdd:PRK14258 93 vhpkpnLFPM-SVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 1435 LLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLR 1493
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1311-1487 |
7.38e-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: 61.61 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1311 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLGHLGYCPQENVLWPMLTAREHL--------EVYAA 1381
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdWDEILDEFRGSELQNYFTKLLEGDVKVivkpqyvdLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1382 VKG-----LRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1456
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170 180 190
....*....|....*....|....*....|.
gi 1622880985 1457 QAVVKNtERGVLLTTHNLAEAEALCDRVAIM 1487
Cdd:cd03236 183 RELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
503-692 |
7.66e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEI----------RKITGVCPQFNVQFDIL 572
Cdd:PRK10982 269 FDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalvteeRRSTGIYAYLDIGFNSL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 tVKENLSLFAKIKGIHPQEVEQEVQRILlelDMQNI----QDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDP 648
Cdd:PRK10982 349 -ISNIRNYKNKVGLLDNSRMKSDTQWVI---DSMRVktpgHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 649 FSRDQVWSLLRE-HRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK10982 425 GAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1305-1491 |
8.15e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.35 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTA---GEVELKG------CSSVLGHLGYCPQENVLWPMLTAREH 1375
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGipykefAEKYPGEIIYVSEEDVHFPTLTVRET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1376 LEVYAAVKGlrkvdarlaitrlvsafklheqlNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1455
Cdd:cd03233 104 LDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622880985 1456 IQAVVKNTERGVLLTTHNLA-EAEALCDRVAIMVSGR 1491
Cdd:cd03233 161 IRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGR 197
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
481-683 |
9.40e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.88 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKSGKVEALKGllfDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemqdleeiRKITG 560
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 561 VCPQFNVqfdilTVKENLSLFAKIKGIHPQ-EVEqevqrILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLL 639
Cdd:cd03237 70 IKADYEG-----TVRDLLSSITKDFYTHPYfKTE-----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 640 DEPTTGLDPFSRDQVWSLLR---EHR------ADHVILFstqsmdeADILADR 683
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRrfaENNektafvVEHDIIM-------IDYLADR 185
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
501-648 |
1.04e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 501 LLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqdlEEIRKIT--GVCPQFNVQFDILtvkENL 578
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAylGHLPGLKADLSTL---ENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 579 SLFAKIKGIHPQEVEQEVQRILlelDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDP 648
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
508-686 |
1.04e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 508 GQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIK 585
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 586 GIHPQEVEQEVQRILLE-LDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE---- 660
Cdd:PRK11831 113 TQLPAPLLHSTVMMKLEaVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnsa 192
|
170 180 190
....*....|....*....|....*....|....*
gi 1622880985 661 ---------HRADHVILFStqsmDEADILADRKVI 686
Cdd:PRK11831 193 lgvtcvvvsHDVPEVLSIA----DHAYIVADKKIV 223
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
498-678 |
1.10e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSE-----MQDLEEIRKITGVCPQfnvqfdiL 572
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctyQKQLCFVGHRSGINPY-------L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 TVKENlSLFakikGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRD 652
Cdd:PRK13540 90 TLREN-CLY----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180 190
....*....|....*....|....*....|
gi 1622880985 653 QVWSLLREHRAD--HVILFSTQ--SMDEAD 678
Cdd:PRK13540 165 TIITKIQEHRAKggAVLLTSHQdlPLNKAD 194
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
468-692 |
1.24e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 468 PVAPEFQGKEAIRIRNVKKEYKGKSGkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS 547
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAYQDNGF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 548 eMQDLEEIRKItgvcpqfnvqfdILTVKENLSLFAKIKGIHPQEVEQE-VQRILLELDMQN---IQDN--LAKHLSEGQK 621
Cdd:PRK10522 389 -AEQPEDYRKL------------FSAVFTDFHLFDQLLGPEGKPANPAlVEKWLERLKMAHkleLEDGriSNLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 622 RKLTFGIAILGDPQILLLDEPTTGLDP-FSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPhFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1504 |
1.36e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.90 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYC---PQENVLwpMLTA 1372
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevnaenEKWVRSKVGLVfqdPDDQVF--SSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHLEVYAAVKGLRK--VDARL-AITRLVSAFKLHEQlnvPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1449
Cdd:PRK13647 98 WDDVAFGPVNMGLDKdeVERRVeEALKAVRMWDFRDK---PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1450 QQMwQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1504
Cdd:PRK13647 175 ETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1311-1493 |
1.36e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1311 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---------SVL--GHLGYCPQENVLWPMLTAREHLEVY 1379
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmdeearAKLraKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1380 AAVKGLRKVDARLAITRLVSAFKLHEQLN-VPVQkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1458
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDhLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 1622880985 1459 VVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRLR 1493
Cdd:PRK10584 192 LNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1306-1491 |
1.51e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKS----SSIRMISgiTKP---TAGEVELKGcSSVL------------GHLGYCPQENV- 1365
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPvvyPSGDIRFHG-ESLLhaseqtlrgvrgNKIAMIFQEPMv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1366 -LWPMLTAREHL-EVYAAVKGLRKVDARLAITRLVSAFKLHE---QLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEP 1440
Cdd:PRK15134 104 sLNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1300-1501 |
1.57e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.80 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1300 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGhlgycpQENVlWPMltaREHLE-- 1377
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG--MVLS------EETV-WDV---RRQVGmv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 --------VYAAVK-----GL-----------RKVDARLAITRLvSAFKLHEqlnvPvQKLTTGTMRKLCfVLSLLGNSP 1433
Cdd:PRK13635 87 fqnpdnqfVGATVQddvafGLenigvpreemvERVDQALRQVGM-EDFLNRE----P-HRLSGGQKQRVA-IAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 1434 -VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK13635 160 dIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1291-1504 |
1.59e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.77 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1291 KKSCFSKRK-KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlghlgyCPQENVLWpm 1369
Cdd:PRK13632 11 ENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT--------ISKENLKE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1370 ltAREHLE----------VYAAVK-----GL--RKVDA---RLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCF--VLS 1427
Cdd:PRK13632 81 --IRKKIGiifqnpdnqfIGATVEddiafGLenKKVPPkkmKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIasVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1428 LlgNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQH-LKNK 1504
Cdd:PRK13632 159 L--NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1301-1498 |
1.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.83 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1301 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---------CSSVLGHLGYCPQ--ENVLW-- 1367
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvkLSDIRKKVGLVFQypEYQLFee 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 ---------PMLTAREHLEVYAAVK-GLRKVDARLAITRLVSAFKLheqlnvpvqklTTGTMRKLCFVLSLLGNSPVLLL 1437
Cdd:PRK13637 100 tiekdiafgPINLGLSEEEIENRVKrAMNIVGLDYEDYKDKSPFEL-----------SGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1438 DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSI 1498
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1300-1510 |
1.73e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1300 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMIS--GITKPtagEVELKGCSSVLGHLGYCPQENVL----------- 1366
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNP---EVTITGSIVYNGHNIYSPRTDTVdlrkeigmvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1367 ----WPMlTAREHLeVY----AAVKGLRKVDARLAiTRLVSAF---KLHEQLNVPVQKLTTGTMRKLCfVLSLLGNSP-V 1434
Cdd:PRK14239 94 qpnpFPM-SIYENV-VYglrlKGIKDKQVLDEAVE-KSLKGASiwdEVKDRLHDSALGLSGGQQQRVC-IARVLATSPkI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1435 LLLDEPSTGIDPTGQQQMWQAIQAVVKNTErgVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL----KNKLGKDYI 1510
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMfmnpKHKETEDYI 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1305-1492 |
1.82e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS----SV-----LGhLGYCPQE---NVLWPMLTA 1372
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitglSPrerrrLG-VAYIPEDrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHL-----EVYAAVKG--LRKVDARLAITRLVSAFKL-HEQLNVPVQKLTTGTMRKlcFVLS--LLGNSPVLLLDEPST 1442
Cdd:COG3845 354 AENLilgryRRPPFSRGgfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQK--VILAreLSRDPKLLIAAQPTR 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1443 GIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG3845 432 GLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
508-647 |
2.20e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.19 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 508 GQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVcPQFNVQFDILTVKENLSLfakikGI 587
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL-PQQLPAAEGMTVRELVAI-----GR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 588 HP---------QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLD 647
Cdd:PRK10575 111 YPwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
498-670 |
2.33e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLsVPTEGSVTIYNKNLSEMQdLEEIRKITGVCPQFNVQFDiLTVKEN 577
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFGVIPQKVFIFS-GTFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 578 LSlfakikgIHPQEVEQEVQRILLELDMQNIQDNLAKHL-----------SEGQKRKLTFGIAILGDPQILLLDEPTTGL 646
Cdd:TIGR01271 1312 LD-------PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180
....*....|....*....|....
gi 1622880985 647 DPFSRDQVWSLLREHRADHVILFS 670
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILS 1408
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1305-1506 |
2.36e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.15 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLGHLGycpqENVLWPMLTA---REHLevYAA 1381
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP--IADYS----EAALRQAISVvsqRVHL--FSA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1382 VkgLRKvDARLAITRLVSAfKLHEQLN-VPVQKLTT------------------GTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:PRK11160 429 T--LRD-NLLLAAPNASDE-ALIEVLQqVGLEKLLEddkglnawlgeggrqlsgGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1443 GIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAEALcDRVAIMVSGRLRCIGSIQHLKNKLG 1506
Cdd:PRK11160 505 GLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
479-647 |
2.48e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK-NLSEMqDLEEIRK 557
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDI-NLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQ----------FNVQFDILTVKE---------------------NLSLFAKIKG-------------------- 586
Cdd:PTZ00265 461 KIGVVSQdpllfsnsikNNIKYSLYSLKDlealsnyynedgndsqenknkRNSCRAKCAGdlndmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 587 ---IHPQEVEQEVQRILLELDMQNIQDNL-------AKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLD 647
Cdd:PTZ00265 541 yqtIKDSEVVDVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1305-1506 |
2.57e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.05 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPM-------- 1369
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydHHYLHRQVALVGQEPVLFSGsvreniay 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1370 -LTAREHLEVYAAVKglrKVDARLAITRLVSAFklHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDptg 1448
Cdd:TIGR00958 578 gLTDTPDEEIMAAAK---AANAHDFIMEFPNGY--DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD--- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1449 qQQMWQAIQAVVKNTERGVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLG 1506
Cdd:TIGR00958 650 -AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
478-647 |
2.92e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 557
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF-GLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNVQFDiLTVKENLSLFAK---------IKGIHPQEVeqeVQRILLELDMQNIQDnlAKHLSEGQKRKLTFGI 628
Cdd:PLN03130 1314 VLGIIPQAPVLFS-GTVRFNLDPFNEhndadlwesLERAHLKDV---IRRNSLGLDAEVSEA--GENFSVGQRQLLSLAR 1387
|
170
....*....|....*....
gi 1622880985 629 AILGDPQILLLDEPTTGLD 647
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVD 1406
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1286-1501 |
2.94e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.03 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1286 EYAGQKKSCFSKRkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-----------KGCSSVL 1354
Cdd:PRK13634 9 EHRYQYKTPFERR----ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1355 GHLGYCPQenvlWPmltarEHLEVYAAVK----------GLRKVDARLAITRLVSAFKLHEQL--NVPVQkLTTGTMRKL 1422
Cdd:PRK13634 85 KKVGIVFQ----FP-----EHQLFEETVEkdicfgpmnfGVSEEDAKQKAREMIELVGLPEELlaRSPFE-LSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 1423 CFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1300-1477 |
2.99e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1300 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQeNVLWP---- 1368
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaSKEVARRIGLLAQ-NATTPgdit 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 --MLTAREHLEVYAAVKGLRKVDARlAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDP 1446
Cdd:PRK10253 98 vqELVARGRYPHQPLFTRWRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190
....*....|....*....|....*....|...
gi 1622880985 1447 TGQQQMWQAIQAVvkNTERGVLLTT--HNLAEA 1477
Cdd:PRK10253 177 SHQIDLLELLSEL--NREKGYTLAAvlHDLNQA 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1299-1445 |
4.28e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1299 KKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQENVLWPMLTAREHLE- 1377
Cdd:TIGR03719 17 KKEIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKV----GYLPQEPQLDPTKTVRENVEe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 ----VYAAVKGLRKVDARLA---------------ITRLVSAFKLHE---QLNV------------PVQKLTTGTMRKLC 1423
Cdd:TIGR03719 92 gvaeIKDALDRFNEISAKYAepdadfdklaaeqaeLQEIIDAADAWDldsQLEIamdalrcppwdaDVTKLSGGERRRVA 171
|
170 180
....*....|....*....|..
gi 1622880985 1424 FVLSLLGNSPVLLLDEPSTGID 1445
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
479-697 |
4.47e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.92 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS--VPTEGSVTIYNKNLSEMQDLEEIR 556
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVCPQFNVQFDILTVKENLslfakikgihpqeveqevqRilleldmqniqdNLAKHLSEGQKRKLTFGIAILGDPQI 636
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFL-------------------R------------YVNEGFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 637 LLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEAD-ILADRKVIMSNGRLKCAGS 697
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKsVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1306-1493 |
4.67e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGiTKPTAGE---------VELKGCSSVLGH-----------LGYCPQ--- 1362
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEgnvfingkpVDIRNPAQAIRAgiamvpedrkrHGIVPIlgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1363 -ENVLWPMLTAREHLEVYAAVKGLRKVDArlAITRL-VSAFklheQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEP 1440
Cdd:TIGR02633 357 gKNITLSVLKSFCFKMRIDAAAELQIIGS--AIQRLkVKTA----SPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVVKnteRGV--LLTTHNLAEAEALCDRVAIMVSGRLR 1493
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1305-1478 |
4.97e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.89 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLG----------HLGYCPQENVLWPMLTAR 1373
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqDVATLDadalaqlrreHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHLEVYAAVKGL----RKVDARLAITRLvsafKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDP-TG 1448
Cdd:PRK10535 105 QNVEVPAVYAGLerkqRLLRAQELLQRL----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDShSG 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622880985 1449 QQQMwqaiqAVVKN-TERG--VLLTTHN---LAEAE 1478
Cdd:PRK10535 181 EEVM-----AILHQlRDRGhtVIIVTHDpqvAAQAE 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1306-1501 |
4.98e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.12 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---CSSVLGHLGYCP--QENVLWPMLTAREHLEVYA 1380
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQRDICMvfQSYALFPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1381 AVKGLRKVDARlaiTRLVSAFKLHEQLNVP---VQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQ 1457
Cdd:PRK11432 104 KMLGVPKEERK---QRVKEALELVDLAGFEdryVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622880985 1458 AVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK11432 181 ELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1305-1533 |
5.45e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSsirMISGITK--PTAGEVELKGCS--SVL-----GHLGYCPQENVLWPMlTAREH 1375
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRllSTEGEIQIDGVSwnSVTlqtwrKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1376 LEVYA--AVKGLRKVDARLAITRLVSAF--KLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1451
Cdd:TIGR01271 1312 LDPYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQI 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1452 MWQAIQAVVKNTErgVLLTTHNLaEAEALCDRVAIMVSGRLRCIGSIQHLKNklgkdyilelkvkEPSQVTLV--HTEIL 1529
Cdd:TIGR01271 1392 IRKTLKQSFSNCT--VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLN-------------ETSLFKQAmsAADRL 1455
|
....
gi 1622880985 1530 KLFP 1533
Cdd:TIGR01271 1456 KLFP 1459
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
479-647 |
6.15e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiynknlsEMQDLEEIrki 558
Cdd:PRK09544 5 VSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLRI--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 tGVCPQfNVQFDI---LTVKEnlslFAKIK-GIHPQEVEQEVQRI----LLELDMQNiqdnlakhLSEGQKRKLTFGIAI 630
Cdd:PRK09544 70 -GYVPQ-KLYLDTtlpLTVNR----FLRLRpGTKKEDILPALKRVqaghLIDAPMQK--------LSGGETQRVLLARAL 135
|
170
....*....|....*..
gi 1622880985 631 LGDPQILLLDEPTTGLD 647
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVD 152
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
503-647 |
6.17e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtIYNKNL--SEMQDlEEIRKITGvcpqfNVqFDIltVKENLSL 580
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLivARLQQ-DPPRNVEG-----TV-YDF--VAEGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 581 FA-KIKGIH--PQEVEQE--------VQRILLELDMQN-------IQDNLAK----------HLSEGQKRKLTFGIAILG 632
Cdd:PRK11147 94 QAeYLKRYHdiSHLVETDpseknlneLAKLQEQLDHHNlwqlenrINEVLAQlgldpdaalsSLSGGWLRKAALGRALVS 173
|
170
....*....|....*
gi 1622880985 633 DPQILLLDEPTTGLD 647
Cdd:PRK11147 174 NPDVLLLDEPTNHLD 188
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
418-673 |
6.26e-09 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 59.33 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 418 FDKILPYGDERRYSPLFFLNSSSCFQ--HQGTDNKVIEKEIDAEHPSDDYFEPVAPEFQGKEAIRIRNVKKEYKGKSGKV 495
Cdd:pfam13304 36 RSRNGGIGGIPSLLNGIDPKEPIEFEisEFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 496 EALKGLLFDIYEGQITAIL---GHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVCPQFNVQFDIL 572
Cdd:pfam13304 116 EELRLGLDVEERIELSLSElsdLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 TVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDnlAKHLSEGQKRKLTFGIAILGDPQ---ILLLDEPTTGLDPF 649
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELP--AFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPK 273
|
250 260
....*....|....*....|....*
gi 1622880985 650 SRDQVWSLLREHRADHV-ILFSTQS 673
Cdd:pfam13304 274 LLRRLLELLKELSRNGAqLILTTHS 298
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1307-1492 |
6.62e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.95 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLG---------HLGYCPQENVLW 1367
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnLRRKIGmvfqnpdnqFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTA---REHLevyaavkgLRKVD-ARLAITRLvsAFKLHEQlnvpvQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTG 1443
Cdd:PRK13642 106 GMENQgipREEM--------IKRVDeALLAVNML--DFKTREP-----ARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622880985 1444 IDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRL 1492
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1287-1497 |
7.94e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1287 YAGQKKSCFSKRkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV---------------ELKGCS 1351
Cdd:PRK13645 14 YTYAKKTPFEFK----ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipanlkkikEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1352 SVLGHLGYCPQENVLWPmlTAREHLEVYAAVKGLRKVDARLAITRLVSAFKLHEQL--NVPVQkLTTGTMRKLCF--VLS 1427
Cdd:PRK13645 90 KEIGLVFQFPEYQLFQE--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYvkRSPFE-LSGGQKRRVALagIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1428 LLGNSpvLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:PRK13645 167 MDGNT--LVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1287-1497 |
7.98e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1287 YAGQKKSCFSKRkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV--------------ELKGCSS 1352
Cdd:PRK13643 9 YTYQPNSPFASR----ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstskqkEIKPVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1353 VLGHLGYCPQENVLWPmlTAREHLEVYAAVKGLRKVDA-RLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGN 1431
Cdd:PRK13643 85 KVGVVFQFPESQLFEE--TVLKDVAFGPQNFGIPKEKAeKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1432 SPVLLLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
480-691 |
9.67e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 480 RIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtIYNKNLSEMQDLEEI---- 555
Cdd:PRK11701 8 SVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-HYRMRDGQLRDLYALseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 -----RKITGVCPQF-------------NVQFDILTVKENlslfakikgiHPQEVEQEVQRIL--LELDMQNIqDNLAKH 615
Cdd:PRK11701 83 rrrllRTEWGFVHQHprdglrmqvsaggNIGERLMAVGAR----------HYGDIRATAGDWLerVEIDAARI-DDLPTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 616 LSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRAD---HVILFsTQSMDEADILADRKVIMSNGR 691
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElglAVVIV-THDLAVARLLAHRLLVMKQGR 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
477-693 |
1.12e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 477 EAIRIRNVKKEY----------------KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT 540
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 541 IYNknlsemqDLEEIRKITGVCPQfnvqfdiLTVKENLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQ 620
Cdd:PRK13546 83 RNG-------EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 621 KRKLTFGIAILGDPQILLLDEP-TTGLDPFSRDQVWSLLREHRADHVILFSTQSMDEADILADRKVIMSNGRLK 693
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
500-691 |
1.23e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 500 GLLFDIYEGQITAILGHSGAGKS-SLLNILNGLSVP----TEGSVTIYNKNL--SEMQDLEEIR--KITGVCPQFNVQFD 570
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhASEQTLRGVRgnKIAMIFQEPMVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 571 IL-TVK----ENLSLFakiKGIHPQEVEQEVQRILLELDMQNIQDNLAKH---LSEGQKRKLTFGIAILGDPQILLLDEP 642
Cdd:PRK15134 107 PLhTLEkqlyEVLSLH---RGMRREAARGEILNCLDRVGIRQAAKRLTDYphqLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 643 TTGLDPFSRDQVWSLLREHRA--DHVILFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
476-668 |
1.28e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.65 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 476 KEAIRIRNVKKEYKGKsgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdLEEI 555
Cdd:PRK11176 339 KGDIEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT-LASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 RKITGVCPQfNVQFDILTVKENLSlFAKiKGIHPQEVEQEVQRILLELD----MQN-----IQDNLAKhLSEGQKRKLTF 626
Cdd:PRK11176 416 RNQVALVSQ-NVHLFNDTIANNIA-YAR-TEQYSREQIEEAARMAYAMDfinkMDNgldtvIGENGVL-LSGGQRQRIAI 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 627 GIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVIL 668
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1297-1472 |
1.50e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.48 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1297 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSS-----SIRMISGITKptaGEVELKG---CSSVLGHLGYCPQENVLWP 1368
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlAGRKTAGVIT---GEILINGrplDKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLEVYAAVKGL----RKvdaRLAI-TRLVSafklheqlnvpvqklttgtmrklcfvlsllgnSPVLL-LDEPST 1442
Cdd:cd03232 93 NLTVREALRFSALLRGLsveqRK---RLTIgVELAA--------------------------------KPSILfLDEPTS 137
|
170 180 190
....*....|....*....|....*....|..
gi 1622880985 1443 GIDptgQQQMWQAIQAVVK--NTERGVLLTTH 1472
Cdd:cd03232 138 GLD---SQAAYNIVRFLKKlaDSGQAILCTIH 166
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
867-1168 |
1.52e-08 |
|
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: 58.56 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 867 MFPLIVENIMYAMLNEKIDWEFKTELYFLSPgqlpQEPRTSLLIINNTESNieDFIKSLKHQNILLEVDDFENRNGTDGL 946
Cdd:pfam12698 9 LLPILLILLLGLIFSNAVNDPEELPVAVVDE----DNSSLSRQLVRALEAS--PTVNLVQYVDSEEEAKEALKNGKIDGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 947 SY--NGAIIVSGKQKDYRFSVVCNTKRLHCFPILMNIIsNGLLRMLNHTQ---HIRIESSPFPLSHIGLWTGLPDGSF-- 1019
Cdd:pfam12698 83 LVipKGFSKDLLKGESATVTVYINSSNLLVSKLILNAL-QSLLQQLNASAlvlLLEALSTSAPIPVESTPLFNPQSGYay 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1020 ----FLFLVLCSISPYITMGSISDYKKN-AKSQLWISGLYTSAYWCGQALVDVSFFILILLAMYLIFYIENMQYllitSQ 1094
Cdd:pfam12698 162 ylvgLILMIIILIGAAIIAVSIVEEKESrIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPF----GN 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1095 IVFALVIVTPGYAASlVFLIYMISFIFRKRRKNSALWSFYFFFASIIMFVTALISNFDlSILITTMVLVPSYTL 1168
Cdd:pfam12698 238 LGLLLLLFLLYGLAY-IALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPP-SFLQWIFSIIPFFSP 309
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1306-1492 |
2.02e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.02 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCsSVLG----------HLGYCPQENVLWPMLTAreh 1375
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL-KVNDpkvderlirqEAGMVFQQFYLFPHLTA--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1376 LEVYA----AVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1451
Cdd:PRK09493 95 LENVMfgplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622880985 1452 MWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK09493 175 VLKVMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
478-647 |
2.12e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 478 AIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiynkNLSEMQDLeeirk 557
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSENANI----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 itGVCPQFNV-QFDI-LTVKENLSLFAKikgihPQEVEQEVQRILLELDMQniQDNL---AKHLSEGQKRKLTFGIAILG 632
Cdd:PRK15064 385 --GYYAQDHAyDFENdLTLFDWMSQWRQ-----EGDDEQAVRGTLGRLLFS--QDDIkksVKVLSGGEKGRMLFGKLMMQ 455
|
170
....*....|....*
gi 1622880985 633 DPQILLLDEPTTGLD 647
Cdd:PRK15064 456 KPNVLVMDEPTNHMD 470
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1303-1501 |
2.23e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.81 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP---TAGEVELKGcSSVLG----HLGYCPQENV---------- 1365
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNG-REILNlpekELNKLRAEQIsmifqdpmts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1366 LWPMLTAREHL-EVYAAVKGLRKVDARLAITRLVSAFKLHE---QLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPS 1441
Cdd:PRK09473 110 LNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1305-1510 |
2.38e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.77 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK--PTA---GEVELKGCS---------SVLGHLGYCPQENVLWPML 1370
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNiyspdvdpiEVRREVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 TAREH----LEVYAAVKGLRKVDARL--AITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGI 1444
Cdd:PRK14267 101 TIYDNvaigVKLNGLVKSKKELDERVewALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANI 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1445 DPTGQQQMWQAIQAVvkNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL----KNKLGKDYI 1510
Cdd:PRK14267 181 DPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVfenpEHELTEKYV 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1312-1487 |
2.44e-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: 58.64 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1312 QEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcssvlghlgycPQENVLwpmltAR-------EHLE-VYA--- 1380
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEP-----------SWDEVL-----KRfrgtelqDYFKkLANgei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1381 --------------AVKG-----LRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPS 1441
Cdd:COG1245 161 kvahkpqyvdlipkVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIM 1487
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1305-1497 |
2.65e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 56.63 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC------SSVLG-HLGYCPQENVLWPMLTAREhLe 1377
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAkRLAILRQENHINSRLTVRE-L- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 V----YAAVKG-LRKVDaRLAITRLVSAFKLHE-------QLnvpvqkltTGTMRKLCFV-LSLLGNSPVLLLDEPSTGI 1444
Cdd:COG4604 96 VafgrFPYSKGrLTAED-REIIDEAIAYLDLEDladryldEL--------SGGQRQRAFIaMVLAQDTDYVLLDEPLNNL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1445 DPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1497
Cdd:COG4604 167 DMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
477-660 |
2.70e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 477 EAIRIRNVKKEYK-------GKSGkvealkgllFDIY------EGQITAILGHSGAGKSSLLNILNGLSVPTEGSvtiYN 543
Cdd:PRK13409 64 DAISIVNLPEELEeepvhryGVNG---------FKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 544 KNLS-----------EMQD-LEEIRKitgvcpqfnvqfdiltvkenlslfAKIKGIH-PQEVEQ-------EVQRILL-- 601
Cdd:PRK13409 132 EEPSwdevlkrfrgtELQNyFKKLYN------------------------GEIKVVHkPQYVDLipkvfkgKVRELLKkv 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 602 -----------ELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE 660
Cdd:PRK13409 188 dergkldevveRLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRE 257
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1306-1499 |
2.80e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.79 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLG---HLGYCPQENVLWPMLTAREHLEVYA 1380
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdVSRLHArdrKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1381 AVKGLRKVDARLAI----TRLVSAFKL-HEQLNVPVQkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1455
Cdd:PRK10851 100 TVLPRRERPNAAAIkakvTQLLEMVQLaHLADRYPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622880985 1456 IQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1499
Cdd:PRK10851 179 LRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1299-1531 |
3.44e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.28 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1299 KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGIT--KPTAGEvelkgcssVLGHLGYCP-------QENVLWPM 1369
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGR--------IIYHVALCEkcgyverPSKVGEPC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1370 LTAREHLEVY------AAVKGLRKVDARLAI------------TRLVSAFKLHEQLNVPVQK------------------ 1413
Cdd:TIGR03269 83 PVCGGTLEPEevdfwnLSDKLRRRIRKRIAImlqrtfalygddTVLDNVLEALEEIGYEGKEavgravdliemvqlshri 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1414 ------LTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIM 1487
Cdd:TIGR03269 163 thiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622880985 1488 VSGRLRCIGSIQHLKNKlgkdYILELKVKEPSQVTLVHTEILKL 1531
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV----FMEGVSEVEKECEVEVGEPIIKV 282
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
481-691 |
3.51e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNIL--NGLsvpTEGSVTIYNK---NLSEMQ- 550
Cdd:PRK09473 15 VKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGR---IGGSATFNGReilNLPEKEl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 551 ---DLEEIRKI-----TGVCPQFNVQFDILTVkenLSLFakiKGIHPQEVEQEVQRILLELDMQNIQD--NLAKH-LSEG 619
Cdd:PRK09473 92 nklRAEQISMIfqdpmTSLNPYMRVGEQLMEV---LMLH---KGMSKAEAFEESVRMLDAVKMPEARKrmKMYPHeFSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 620 QKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH--VILFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1306-1445 |
3.62e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELkGcSSVlgHLGYCPQenvlwpmltAREHLE----VYAA 1381
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETV--KLAYVDQ---------SRDALDpnktVWEE 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1382 VK--------GLRKVDARLAITRLvsAFKLHEQlNVPVQKLTTGTMRKLCFVLSLL--GNspVLLLDEPSTGID 1445
Cdd:PRK11819 409 ISggldiikvGNREIPSRAYVGRF--NFKGGDQ-QKKVGVLSGGERNRLHLAKTLKqgGN--VLLLDEPTNDLD 477
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1305-1479 |
4.39e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 55.18 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP---TAGEVELKGCSSVLG-----HLGYCPQENVLWPmltareHL 1376
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALpaeqrRIGILFQDDLLFP------HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1377 EV-----YAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGT------MRklcfvlSLLGNSPVLLLDEPSTGID 1445
Cdd:COG4136 92 SVgenlaFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQrarvalLR------ALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622880985 1446 PTGQQQM----WQAIQavvkntERG--VLLTTHNLAEAEA 1479
Cdd:COG4136 166 AALRAQFrefvFEQIR------QRGipALLVTHDEEDAPA 199
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1273-1491 |
4.40e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.09 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1273 DEKPVIIASCLHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSS 1352
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRK-----------GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1353 VLGHLGYCPQENVLWPMLTAREHLEVYAAvKGLR-KVDARLAI-TRLVSAFKLH------------EQLNVPVQKL---- 1414
Cdd:PRK11701 71 QLRDLYALSEAERRRLLRTEWGFVHQHPR-DGLRmQVSAGGNIgERLMAVGARHygdiratagdwlERVEIDAARIddlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1415 TT--GTMRKLCFVLSLLGNSPVL-LLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:PRK11701 150 TTfsGGMQQRLQIARNLVTHPRLvFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1305-1510 |
4.97e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.69 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK--PTA---GEVELKG-------CSSVLGHLGYCPQENVLWPMLTA 1372
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGqdifkmdVIELRRRVQMVFQIPNPIPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REH----LEVYAAVKGLRKVDARL--AITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDP 1446
Cdd:PRK14247 100 FENvalgLKLNRLVKSKKELQERVrwALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1447 TGQQQMWQAIQAVVKntERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL----KNKLGKDYI 1510
Cdd:PRK14247 180 ENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVftnpRHELTEKYV 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1306-1484 |
5.17e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.49 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLG------HLGYCPQ----------ENVLWP 1368
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKpeiyrqQVSYCAQtptlfgdtvyDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLEVYAAVKGLRKvdarlaitrlvsaFKLHEQ-LNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1447
Cdd:PRK10247 105 WQIRNQQPDPAIFLDDLER-------------FALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622880985 1448 GQQQMWQAIQAVVKNTERGVLLTTHNLAEAEAlCDRV 1484
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1295-1472 |
5.34e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAARNISFCvqEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSS---VLGHLGYCPQENVLWPMLT 1371
Cdd:PRK13541 9 FNIEQKNLFDLSITFL--PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniAKPYCTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREHLEVYAAVkglrkVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1451
Cdd:PRK13541 87 VFENLKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|..
gi 1622880985 1452 MWQAIqaVVKNTERG-VLLTTH 1472
Cdd:PRK13541 162 LNNLI--VMKANSGGiVLLSSH 181
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1305-1497 |
5.41e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 55.11 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSV-LGHL----GYCPQENVLWpMLTAREHLE 1377
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidISTIpLEDLrsslTIIPQDPTLF-SGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 VYAavkglRKVDARLaitrlVSAFKLHEQ-LNvpvqkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDptgqQQMWQAI 1456
Cdd:cd03369 104 PFD-----EYSDEEI-----YGALRVSEGgLN-----LSQGQRQLLCLARALLKRPRVLVLDEATASID----YATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622880985 1457 QAVVKNTERG--VLLTTHNLAEAeALCDRVAIMVSGRLRCIGS 1497
Cdd:cd03369 165 QKTIREEFTNstILTIAHRLRTI-IDYDKILVMDAGEVKEYDH 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1305-1496 |
5.92e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.96 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGE----------VELKGCSsvlghLGYCPQENVLWPMLTARE 1374
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDlfigekrmndVPPAERG-----VGMVFQSYALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HLEVYAAVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQ 1454
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622880985 1455 AIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1496
Cdd:PRK11000 175 EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1314-1447 |
5.97e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1314 GEILGLLGPNGAGKSSSIRMISGITKPT--AGEV---ELKGCSSVLGHLGYCPQENVLWPMLTAREHLeVYAAV----KG 1384
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTIlanNRKPTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLlrlpKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1385 LRKVDARLAITRLVSAFKLHEQLNVPV-----QKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1447
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1298-1506 |
6.40e-08 |
|
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: 55.24 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMl 1370
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnLRWLRSQIGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1371 TAREHL----------EVYAAvkglrkvdARLA-ITRLVSafKLHEQLNVPV----QKLTTGTMRKLCFVLSLLGNSPVL 1435
Cdd:cd03249 92 TIAENIrygkpdatdeEVEEA--------AKKAnIHDFIM--SLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1436 LLDEPSTGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLG 1506
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKG--RTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
491-692 |
6.90e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.55 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 491 KSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL---SVPTEGSVTiYNKnlsemQDLEEI--RKITGVCPQF 565
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKldpSLKVSGEIT-YNG-----YRLNEFvpRKTSAYISQN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 566 NVQFDILTVKENLSLFAKIKG-------------------IHPqevEQEVQRILLELDMQNIQDNL-------------- 612
Cdd:PLN03140 248 DVHVGVMTVKETLDFSARCQGvgtrydllselarrekdagIFP---EAEVDLFMKATAMEGVKSSLitdytlkilgldic 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 613 ---------AKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFS-TQSMDEADIL 680
Cdd:PLN03140 325 kdtivgdemIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQivHLTEATVLMSlLQPAPETFDL 404
|
250
....*....|..
gi 1622880985 681 ADRKVIMSNGRL 692
Cdd:PLN03140 405 FDDIILLSEGQI 416
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
461-678 |
7.06e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 461 PSDDYFEPVAPEFQGKeaIRIRNVKKEYKgkSGKVeALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT 540
Cdd:PRK10790 325 PRQQYGNDDRPLQSGR--IDIDNVSFAYR--DDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 541 IYNKNLSEMQDlEEIRKitGVCpqfNVQFDILTVKEnlSLFAKI---KGIHPQEVEQEVQRILLELDMQNIQDNLAKHLS 617
Cdd:PRK10790 400 LDGRPLSSLSH-SVLRQ--GVA---MVQQDPVVLAD--TFLANVtlgRDISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 618 E-------GQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRD---QVWSLLREHRADHVILFSTQSMDEAD 678
Cdd:PRK10790 472 EqgnnlsvGQKQLLALARVLVQTPQILILDEATANIDSGTEQaiqQALAAVREHTTLVVIAHRLSTIVEAD 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
494-692 |
8.38e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 494 KVEALKG------LLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVCPQfNV 567
Cdd:PRK11288 259 RLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPE-DR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 568 QFD----ILTVKENLSLFAKIKGIH-------PQEVEQEVQRIllelDMQNIQ----DNLAKHLSEGQKRKltfgiAILG 632
Cdd:PRK11288 338 KAEgiipVHSVADNINISARRHHLRagclinnRWEAENADRFI----RSLNIKtpsrEQLIMNLSGGNQQK-----AILG 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 633 -----DPQILLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRL 692
Cdd:PRK11288 409 rwlseDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVaVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1299-1492 |
1.57e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.71 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1299 KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSvlghlgycPQENVLWP------MLTA 1372
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT--------SDEENLWDirnkagMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHLEVYAAVK-----------GLRKVDARLAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPS 1441
Cdd:PRK13633 93 NPDNQIVATIVeedvafgpenlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1442 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRL 1492
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1305-1504 |
1.84e-07 |
|
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: 53.30 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGI--TKPTAGEVELKGCS---------SVLGhLGYCPQENVLWPMLTAR 1373
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlppeerARLG-IFLAFQYPPEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1374 EHlevyaavkgLRKVDARLaitrlvsafklheqlnvpvqkltTGTMRKLCFVLSLLGNSPVL-LLDEPSTGIDPTGQQQM 1452
Cdd:cd03217 96 DF---------LRYVNEGF-----------------------SGGEKKRNEILQLLLLEPDLaILDEPDSGLDIDALRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1453 WQAIQAvVKNTERGVLLTTHNLAEAEAL-CDRVAIMVSGRLRCIGS---IQHLKNK 1504
Cdd:cd03217 144 AEVINK-LREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDkelALEIEKK 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1299-1440 |
1.84e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1299 KKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQENVLWPMLTAREHLE- 1377
Cdd:PRK11819 19 KKQIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKV----GYLPQEPQLDPEKTVRENVEe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1378 ----VYAAVKGLRKVDARLA------------ITRL------VSAFKLHEQLNV------------PVQKLTTGTMRK-- 1421
Cdd:PRK11819 94 gvaeVKAALDRFNEIYAAYAepdadfdalaaeQGELqeiidaADAWDLDSQLEIamdalrcppwdaKVTKLSGGERRRva 173
|
170 180
....*....|....*....|
gi 1622880985 1422 LCfvlSLLGNSP-VLLLDEP 1440
Cdd:PRK11819 174 LC---RLLLEKPdMLLLDEP 190
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1305-1491 |
2.15e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 53.24 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSsirMISGITkptaGEVE-LKGCSSVLGHLGYCPQ----------ENVLW--PMLT 1371
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSS---LLSALL----GELEkLSGSVSVPGSIAYVSQepwiqngtirENILFgkPFDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AR--EHLEVYAAVKGLRKVD-------------------ARLAITRlvsafklheqlnvpvqklttgtmrklcfvlSLLG 1430
Cdd:cd03250 95 ERyeKVIKACALEPDLEILPdgdlteigekginlsggqkQRISLAR------------------------------AVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1431 NSPVLLLDEPSTGIDP-TGQQQMWQAIQAVVKNtERGVLLTTHNLAEAEAlCDRVAIMVSGR 1491
Cdd:cd03250 145 DADIYLLDDPLSAVDAhVGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
501-647 |
2.48e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 501 LLFDIYEGQITAILGHSGAGKSSLLNILNGLSvPTEGSVTIYNKNLSEMQDLEEIRKITGVCPQFNVQFdILTVKENLSL 580
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF-AMPVFQYLTL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 581 FakikgIHPQEVEQEVQRILLEL-DMQNIQDNLAKH---LSEGQKRKLTFGIAIL-----GDP--QILLLDEPTTGLD 647
Cdd:PRK03695 93 H-----QPDKTRTEAVASALNEVaEALGLDDKLGRSvnqLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD 165
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1303-1490 |
2.51e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC--------SSVLGHLGYCPQENVLWPMLTARE 1374
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngpkSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HL----------------EVYA-AVKGLRKVDARLAITRLVSAFKLHEQLNVPVQKlttgtmrklcfVLSLlgNSPVLLL 1437
Cdd:PRK10762 99 NIflgrefvnrfgridwkKMYAeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK-----------VLSF--ESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1438 DEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSG 1490
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRE-LKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1303-1491 |
2.81e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP----TA-----GEVELKGCSS-----VLGH-LGYCPQE--NV 1365
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTAdrmrfDDIDLLRLSPrerrkLVGHnVSMIFQEpqSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1366 LWPmlTAREHLEVYAAVKG------------LRKvdaRLAITRLVS-AFKLHEQL--NVPVQkLTTGTMRKLCFVLSLlG 1430
Cdd:PRK15093 102 LDP--SERVGRQLMQNIPGwtykgrwwqrfgWRK---RRAIELLHRvGIKDHKDAmrSFPYE-LTEGECQKVMIAIAL-A 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622880985 1431 NSPVLLL-DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:PRK15093 175 NQPRLLIaDEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
498-648 |
2.86e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNG--LSVPTEGSVtiynknlsEMQDLEEIRKITGVcPQFNVQFDILTVK 575
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCV--------DVPDNQFGREASLI-DAIGRKGDFKDAV 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 576 ENLSlfakikgihpqeveqevqrilleldMQNIQDNLA-----KHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDP 648
Cdd:COG2401 117 ELLN-------------------------AVGLSDAVLwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1298-1493 |
3.60e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIaaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK-PTAGEVELKG-------CSSVLGH-LGYCP------- 1361
Cdd:PRK13549 274 HIKRV--DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpvkirnPQQAIAQgIAMVPedrkrdg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1362 -------QENVLWPML---TAREHLEVYAAVKGLRKVDARLAItRLVSAFklheqlnVPVQKLTTGTMRKLCFVLSLLGN 1431
Cdd:PRK13549 352 ivpvmgvGKNITLAALdrfTGGSRIDDAAELKTILESIQRLKV-KTASPE-------LAIARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1432 SPVLLLDEPSTGIDPTGQQQMWQAIQAVVKnteRGV--LLTTHNLAEAEALCDRVAIMVSGRLR 1493
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQ---QGVaiIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
477-660 |
3.77e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 477 EAIRIRNVKKEYK-------GKSGkvealkgllFDIY------EGQITAILGHSGAGKSSLLNILNGLSVPTEGsvtIYN 543
Cdd:COG1245 64 DAISIVNLPEELEedpvhryGENG---------FRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 544 KNLS-----------EMQD-LEEIRKitgvcpqfnvqfdiltvkenlslfAKIKGIH-PQEVEQ-------EVqRILLE- 602
Cdd:COG1245 132 EEPSwdevlkrfrgtELQDyFKKLAN------------------------GEIKVAHkPQYVDLipkvfkgTV-RELLEk 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 603 -------------LDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE 660
Cdd:COG1245 187 vdergkldelaekLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
510-658 |
4.00e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 510 ITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLeeirKITGVCPQFNVQFDiLTVKENLSLFAKIkgihp 589
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP----YCTYIGHNLGLKLE-MTVFENLKFWSEI----- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 590 QEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLL 658
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1314-1501 |
4.04e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1314 GEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMLTAREHLEV-----YAA 1381
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1382 VKGLRKVDARL---AITrLVSAFKLHEQLnvpVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1458
Cdd:PRK10575 117 LGRFGAADREKveeAIS-LVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 1459 VVKntERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1501
Cdd:PRK10575 193 LSQ--ERGltVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
503-693 |
4.13e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGlSVP--TEGSVTIYNKNLSEMQDLEEI----------RKITGVCPQFNVQFD 570
Cdd:PRK13549 283 FSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKIRNPQQAIaqgiamvpedRKRDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 571 ILTVkeNLSLFAKIKGIHPQEVEQEVQRILLELDMQNIQDNLA-KHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPF 649
Cdd:PRK13549 362 ITLA--ALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 650 SRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGRLK 693
Cdd:PRK13549 440 AKYEIYKLINQLVQQGVaIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1295-1507 |
4.40e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.58 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQEnvlw 1367
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtrASLRRNIAVVFQD---- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTAR---EHL----------EVYAAVKGLRKVDarlAITRLVSAFKLH--EQLNvpvqKLTTGTMRKLCFVLSLLGNS 1432
Cdd:PRK13657 418 AGLFNRsieDNIrvgrpdatdeEMRAAAERAQAHD---FIERKPDGYDTVvgERGR----QLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1433 PVLLLDEPSTGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAE-AEAlcDRVAIMVSGRLRCIGSIQHLKNKLGK 1507
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKG--RTTFIIAHRLSTvRNA--DRILVFDNGRVVESGSFDELVARGGR 562
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
493-647 |
4.48e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 493 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG---LSVpTEGSVTIYNKNLSEMQdlEEIRKITGVCPQFNVQF 569
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKI-LEGDILFKGESILDLE--PEERAHLGIFLAFQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 570 DILTVKE----NLSLFAKIKGIHPQEVEQ-EVQRILLE-LDMQNIQDN-LAKHLSEG-----QKRKLTFGIAILgDPQIL 637
Cdd:CHL00131 95 EIPGVSNadflRLAYNSKRKFQGLPELDPlEFLEIINEkLKLVGMDPSfLSRNVNEGfsggeKKRNEILQMALL-DSELA 173
|
170
....*....|
gi 1622880985 638 LLDEPTTGLD 647
Cdd:CHL00131 174 ILDETDSGLD 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
456-665 |
4.81e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 456 IDAEhPSDDyfePVAPEFQGKEAIRIRNVKKEYKGKSGKV-------EALKGLLFDIYEGQITAILGHSGAGKSS----L 524
Cdd:PRK15134 257 LNSE-PSGD---PVPLPEPASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 525 LNILNglsvpTEGSVTIYNK---NLSEMQDLEEIRKITGVC--------PQFNVQfdiLTVKENLSLFAKIkgIHPQEVE 593
Cdd:PRK15134 333 LRLIN-----SQGEIWFDGQplhNLNRRQLLPVRHRIQVVFqdpnsslnPRLNVL---QIIEEGLRVHQPT--LSAAQRE 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 594 QEVQRILLELDMqniqDNLAKH-----LSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADH 665
Cdd:PRK15134 403 QQVIAVMEEVGL----DPETRHrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKH 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
479-663 |
8.15e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGlsvptegsvtIYNKNLSEMQDLEEIRKI 558
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG----------IYTRDAGSILYLGKEVTF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGvcPQFNVQFDI------------LTVKENLSL----FAKIKGIHPQEVEQEVQRILLELDMQNIQDNLAKHLSEGQKR 622
Cdd:PRK10762 71 NG--PKSSQEAGIgiihqelnlipqLTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622880985 623 KLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRA 663
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS 189
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
498-690 |
8.29e-07 |
|
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: 52.55 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTiYNKNLSemqdleeirkitgVCPQFNVqfdIL--TVK 575
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGRIS-------------FSSQFSW---IMpgTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 576 ENLslfakIKGIHPQEVEQE--VQRILLELDMQNI--QDN--LAK---HLSEGQKRKLTFGIAILGDPQILLLDEPTTGL 646
Cdd:cd03291 116 ENI-----IFGVSYDEYRYKsvVKACQLEEDITKFpeKDNtvLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 647 DPFSRDQVW-SLLREHRADHVILFSTQSMDEADIlADRKVIMSNG 690
Cdd:cd03291 191 DVFTEKEIFeSCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1299-1491 |
8.38e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 51.88 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1299 KKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISG--ITKPTAGEVELKGcSSVL-------GHLG--YCPQENVLW 1367
Cdd:TIGR01978 12 DKEIL-KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKG-QDLLelepderARAGlfLAFQYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1368 PMLTAREHL-EVYAAVKGLR------------KVDARLAITRLVSAFkLHEQLNVPVqkltTGTMRKLCFVLSLLGNSPV 1434
Cdd:TIGR01978 90 PGVSNLEFLrSALNARRSARgeepldlldfekLLKEKLALLDMDEEF-LNRSVNEGF----SGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 1435 L-LLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALC-DRVAIMVSGR 1491
Cdd:TIGR01978 165 LaILDEIDSGLDIDALKIVAEGINR-LREPDRSFLIITHYQRLLNYIKpDYVHVLLDGR 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
466-683 |
9.22e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 466 FE--PVAPEFQGKEAIRIRNVKKEYKGKSGKVEAlkGllfDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIyn 543
Cdd:PRK13409 326 FEerPPRDESERETLVEYPDLTKKLGDFSLEVEG--G---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 544 knlsemqdleEIR---KitgvcPQF-NVQFDIlTVKENLSLFAKIKGIHPQEVEqevqrILLELDMQNIQDNLAKHLSEG 619
Cdd:PRK13409 399 ----------ELKisyK-----PQYiKPDYDG-TVEDLLRSITDDLGSSYYKSE-----IIKPLQLERLLDKNVKDLSGG 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 620 QKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLR----EHRA-----DHVILFstqsmdeADILADR 683
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRriaeEREAtalvvDHDIYM-------IDYISDR 523
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
507-660 |
9.98e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 507 EGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT--------IYNKNLSEMQDLEEIRKITGVCPQFNVQF-DIL--TVK 575
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPQYvDLIpkAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 576 ENLSLFAKIKGihpqevEQEVQRILLE-LDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQV 654
Cdd:cd03236 105 GKVGELLKKKD------ERGKLDELVDqLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
....*.
gi 1622880985 655 WSLLRE 660
Cdd:cd03236 179 ARLIRE 184
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
479-654 |
1.01e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGlSVPTEGS--VTIYNKNLSEMQDLEEI- 555
Cdd:PRK10938 261 IVLNNGVVSYNDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSndLTLFGRRRGSGETIWDIk 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 RKITGVCPQFNVQFDILTVKEN--LSLFAKIKGIHpQEVeQEVQRILLE--LDMQNIQDNLAKH----LSEGQKRKLTFG 627
Cdd:PRK10938 336 KHIGYVSSSLHLDYRVSTSVRNviLSGFFDSIGIY-QAV-SDRQQKLAQqwLDILGIDKRTADApfhsLSWGQQRLALIV 413
|
170 180
....*....|....*....|....*..
gi 1622880985 628 IAILGDPQILLLDEPTTGLDPFSRDQV 654
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLV 440
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
466-683 |
1.10e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 466 FE--PVAPEFQGKEAIRIRNVKKEYKGKSGKVEAlkGllfDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTiyn 543
Cdd:COG1245 327 FEvhAPRREKEEETLVEYPDLTKSYGGFSLEVEG--G---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 544 knlsemqdlEEIR---KitgvcPQFnVQFDI-LTVKENLSlfAKIKGIHPQEVEQEvqRILLELDMQNIQDNLAKHLSEG 619
Cdd:COG1245 399 ---------EDLKisyK-----PQY-ISPDYdGTVEEFLR--SANTDDFGSSYYKT--EIIKPLGLEKLLDKNVKDLSGG 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 620 QKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLR----EHRA-----DHVILFstqsmdeADILADR 683
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfaeNRGKtamvvDHDIYL-------IDYISDR 525
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1297-1362 |
1.15e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 1.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1297 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLGYCPQ 1362
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQ 87
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1303-1492 |
1.23e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.15 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKS----SSIRMISGITKPTAGEVELKGcSSVLG------------HLGYCPQEnvl 1366
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG-QDLLGlserelrrirgnRIAMIFQE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1367 wPMlTA--------REHLEVYAAVKGLRKVDARLAITRLVSAFKLHEqlnvPVQKLT------TGTMRKLCFVLSLLGNS 1432
Cdd:COG4172 101 -PM-TSlnplhtigKQIAEVLRLHRGLSGAAARARALELLERVGIPD----PERRLDayphqlSGGQRQRVMIAMALANE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 1433 PVLLL-DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:COG4172 175 PDLLIaDEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
508-752 |
1.63e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 508 GQITAILGHSGAGKSSLLNIL----NGLSVPTEGSVTiYNKnlsemQDLEEIRK-ITG---VCPQFNVQFDILTVKENLS 579
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVIT-YDG-----ITPEEIKKhYRGdvvYNAETDVHFPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 580 LFAKIKGihPQE-----VEQEVQRILLELDMQ----------NIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTT 644
Cdd:TIGR00956 161 FAARCKT--PQNrpdgvSREEYAKHIADVYMAtyglshtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 645 GLDPFSRDQVWSLLRE--HRADHVILFST-QSMDEADILADRKVIMSNGRLKCAGSS-----IFLKrrwgLGYhlslhrn 716
Cdd:TIGR00956 239 GLDSATALEFIRALKTsaNILDTTPLVAIyQCSQDAYELFDKVIVLYEGYQIYFGPAdkakqYFEK----MGF------- 307
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622880985 717 eICNPEQITS-FITHHI-PDAKLKTKNKEKLVYTLPLE 752
Cdd:TIGR00956 308 -KCPDRQTTAdFLTSLTsPAERQIKPGYEKKVPRTPQE 344
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1305-1492 |
1.70e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.22 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVeLKGcSSVLGH------LGYcpQENVLWPMLTAREHleV 1378
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-TAPLAEaredtrLMF--QDARLLPWKKVIDN--V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 YAAVKGLRKVDARLAItrlvSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1458
Cdd:PRK11247 103 GLGLKGQWRDAALQAL----AAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIES 178
|
170 180 190
....*....|....*....|....*....|....
gi 1622880985 1459 VVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK11247 179 LWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1305-1473 |
1.76e-06 |
|
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: 49.84 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLghlgYCPQEnvlwPMLTArehlevyaavkG 1384
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLL----FLPQR----PYLPL-----------G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1385 -LRkvdarlaitrlvsafklhEQLNVPVQK-LTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQ----A 1458
Cdd:cd03223 79 tLR------------------EQLIYPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKelgiT 140
|
170
....*....|....*
gi 1622880985 1459 VVKNTERGVLLTTHN 1473
Cdd:cd03223 141 VISVGHRPSLWKFHD 155
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
475-667 |
2.02e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 475 GKEAIRIRNVKkeYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILnglsvptegsvtiynknLSEMQDLEE 554
Cdd:TIGR00957 633 EGNSITVHNAT--FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----------------LAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 555 IRKITG----VCPQFNVQFDilTVKENLsLFAkiKGIHPQEVEQEVQRILLELDMQNI----QDNLAK---HLSEGQKRK 623
Cdd:TIGR00957 694 HVHMKGsvayVPQQAWIQND--SLRENI-LFG--KALNEKYYQQVLEACALLPDLEILpsgdRTEIGEkgvNLSGGQKQR 768
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622880985 624 LTFGIAILGDPQILLLDEPTTGLDpfsrdqvwSLLREHRADHVI 667
Cdd:TIGR00957 769 VSLARAVYSNADIYLFDDPLSAVD--------AHVGKHIFEHVI 804
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1305-1504 |
2.21e-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: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKgcssvlGHLGYCPQenVLWPML-TAREHLevyaaVK 1383
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS------GRISFSPQ--TSWIMPgTIKDNI-----IF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1384 GLRKVDARLaiTRLVSAFKLHEQLNVPVQK-----------LTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQM 1452
Cdd:TIGR01271 510 GLSYDEYRY--TSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 1453 WQAIQAVVKNTERGVLLTT--HNLAEAealcDRVAIMVSGRLRCIGSIQHLKNK 1504
Cdd:TIGR01271 588 FESCLCKLMSNKTRILVTSklEHLKKA----DKILLLHEGVCYFYGTFSELQAK 637
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
481-658 |
2.38e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.44 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNILNGLSVPTEGSVTIYNKNLSEMQdLEEIR 556
Cdd:COG4170 6 IRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLS-PRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITGVcpqfnvqfDILTV-KENLSLFAKIKGIHPQEVE---------------QEVQRILLEL-------DMQNIQDNLA 613
Cdd:COG4170 85 KIIGR--------EIAMIfQEPSSCLDPSAKIGDQLIEaipswtfkgkwwqrfKWRKKRAIELlhrvgikDHKDIMNSYP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622880985 614 KHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLL 658
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLL 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
458-670 |
3.13e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.02 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 458 AEHPS-DDYFEPVaPEFQGKEAIRIRNVKkeYKGKSgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTE 536
Cdd:PRK10789 295 AEAPVvKDGSEPV-PEGRGELDVNIRQFT--YPQTD--HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 537 GSVTIYNKNLSEMQdLEEIRKITGVCPQFNVQFDIlTVKENLSL------------FAKIKGIH------PQEVEQEV-Q 597
Cdd:PRK10789 370 GDIRFHDIPLTKLQ-LDSWRSRLAVVSQTPFLFSD-TVANNIALgrpdatqqeiehVARLASVHddilrlPQGYDTEVgE 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 598 RILLeldmqniqdnlakhLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHVILFS 670
Cdd:PRK10789 448 RGVM--------------LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIIS 506
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
479-718 |
4.73e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEykgksGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNILNGLSVPTEGSVTIYNKNLSemqdLEE 554
Cdd:PRK10418 5 IELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA----PCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 555 IRKITgvcpqfnvqfdILTVKEN-LSLFAKIKGIHPQEVE-------QEVQRILLEL-------DMQNIQDNLAKHLSEG 619
Cdd:PRK10418 76 LRGRK-----------IATIMQNpRSAFNPLHTMHTHAREtclalgkPADDATLTAAleavgleNAARVLKLYPFEMSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 620 QKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLLREHRADHV--ILFSTQSMDEADILADRKVIMSNGRL--KCA 695
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIveQGD 224
|
250 260
....*....|....*....|....*...
gi 1622880985 696 GSSIFLK-----RRWGLGYHLSLHRNEI 718
Cdd:PRK10418 225 VETLFNApkhavTRSLVSAHLALYGMEL 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1303-1492 |
4.75e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.49 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLGHLGYCPQENVLWPMLTA 1372
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknreVPFLRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1373 REHLEVYAAVKGLRKVDARlaitRLVSAF-----KLHEQLNVPVQkLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDpt 1447
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIR----RRVSAAldkvgLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD-- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622880985 1448 gqQQMWQAIQAVVKNTER---GVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK10908 170 --DALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
495-530 |
5.78e-06 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 48.93 E-value: 5.78e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1622880985 495 VEALKGLLfdiyEGQITAILGHSGAGKSSLLNILNG 530
Cdd:cd01854 76 LDELRELL----KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
482-658 |
6.53e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 482 RNVKKEYKGKSG------KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEI 555
Cdd:PRK11308 9 IDLKKHYPVKRGlfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 556 ----RKITGVC--------PQFNVQfDILT--VKENLSLFAkikgihpQEVEQEVQRILLELDMQNIQDNLAKHL-SEGQ 620
Cdd:PRK11308 88 kllrQKIQIVFqnpygslnPRKKVG-QILEepLLINTSLSA-------AERREKALAMMAKVGLRPEHYDRYPHMfSGGQ 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622880985 621 KRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLL 658
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
481-647 |
8.72e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS--VPTEGSVTIYNKNLSEMQdlEEIRKI 558
Cdd:PRK09580 4 IKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELS--PEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 559 TGVCPQFNVQFDILTVKENLSLFAKIKGIHPQEVEQEVQRI----LLE-----LDMQniQDNLAKHLSEG-----QKRKL 624
Cdd:PRK09580 78 EGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFdfqdLMEekialLKMP--EDLLTRSVNVGfsggeKKRND 155
|
170 180
....*....|....*....|...
gi 1622880985 625 TFGIAILgDPQILLLDEPTTGLD 647
Cdd:PRK09580 156 ILQMAVL-EPELCILDESDSGLD 177
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
495-530 |
8.74e-06 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 49.34 E-value: 8.74e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1622880985 495 VEALKGLLfdiyEGQITAILGHSGAGKSSLLNILNG 530
Cdd:COG1162 157 LDELRELL----KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
453-697 |
1.07e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 453 EKEIDAEHPsddyfePVAPefqGKEAIRIRNVKKEYKGKSGKvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS 532
Cdd:PLN03232 598 EERILAQNP------PLQP---GAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 533 VPTEGSVTIynknlsemqdleeIRKITGVCPQFNVQFDIlTVKENLsLFAKikgihpqevEQEVQRILLELDMQNIQDNL 612
Cdd:PLN03232 668 SHAETSSVV-------------IRGSVAYVPQVSWIFNA-TVRENI-LFGS---------DFESERYWRAIDVTALQHDL 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 613 --------------AKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVW-SLLREHRADHVILFSTQSMDEA 677
Cdd:PLN03232 724 dllpgrdlteigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTNQLHFL 803
|
250 260
....*....|....*....|
gi 1622880985 678 DiLADRKVIMSNGRLKCAGS 697
Cdd:PLN03232 804 P-LMDRIILVSEGMIKEEGT 822
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1298-1492 |
1.09e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISG-ITKPTA-------GEVELKG-------------CSSVLGH 1356
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGeplaaidaprlarLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1357 LG-----YCPQENVL---WPMLT---AREHLEVYAAVKGLRKVDARLAITRLVSAfklheqlnvpvqkLTTGTMRKLCF- 1424
Cdd:PRK13547 91 AAqpafaFSAREIVLlgrYPHARragALTHRDGEIAWQALALAGATALVGRDVTT-------------LSGGELARVQFa 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1425 -VLSLLGNSP-------VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTH--NLAEAEAlcDRVAIMVSGRL 1492
Cdd:PRK13547 158 rVLAQLWPPHdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHdpNLAARHA--DRIAMLADGAI 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1307-1492 |
1.10e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQENVLWPMlTAREHLEVY 1379
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvakfglTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1380 AA------VKGLRKVDARLAITRlvSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1453
Cdd:PLN03232 1334 SEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622880985 1454 QAIQAVVKNTErgVLLTTHNLaEAEALCDRVAIMVSGRL 1492
Cdd:PLN03232 1412 RTIREEFKSCT--MLVIAHRL-NTIIDCDKILVLSSGQV 1447
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1305-1491 |
1.25e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 48.52 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK--PTAGEVELKGcSSVLG-------HLG------YcPQE------ 1363
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDG-EDILElspderaRAGiflafqY-PVEipgvsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1364 -NVLWPMLTAReHLEVYAAVKGLRKVDARLAITRLVSAFkLHEQLNVpvqKLTTGTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:COG0396 95 sNFLRTALNAR-RGEELSAREFLKLLKEKMKELGLDEDF-LDRYVNE---GFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 1443 GIDptgqqqMWqAIQAV------VKNTERGVLLTTHN---LAEAEAlcDRVAIMVSGR 1491
Cdd:COG0396 170 GLD------ID-ALRIVaegvnkLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGR 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1273-1349 |
1.28e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 1.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1273 DEKPVIIASCLHKEYAgQKKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG 1349
Cdd:PRK11308 1 SQQPLLQAIDLKKHYP-VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1303-1491 |
1.37e-05 |
|
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: 49.82 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGItKPTA---GEVELKGCSSVLGH--------LGYCPQENVLWPMLT 1371
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNirdteragIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREHL----EVyaAVKGLRKVDARLaitrLVSAFKLHEQLNV-------PVQKLTTGTMRKLCFVLSLLGNSPVLLLDEP 1440
Cdd:TIGR02633 95 VAENIflgnEI--TLPGGRMAYNAM----YLRAKNLLRELQLdadnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1441 STGIDPTGQQQMWQAIQAVvknTERGV--LLTTHNLAEAEALCDRVAIMVSGR 1491
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDL---KAHGVacVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
476-650 |
1.43e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 476 KEAIRIRNVKKEYKGKSgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNIL--------------------------- 528
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRP-NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 529 --------------NGLSVPTEGS----VTIYNKNLSEMQD--------LEEIRKITGVCPQFNVQFdiltvkeNLSLFA 582
Cdd:PTZ00265 1242 yqgdeeqnvgmknvNEFSLTKEGGsgedSTVFKNSGKILLDgvdicdynLKDLRNLFSIVSQEPMLF-------NMSIYE 1314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 583 KIKGIHPQEVEQEVQRI--LLELD-----MQNIQDN----LAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFS 650
Cdd:PTZ00265 1315 NIKFGKEDATREDVKRAckFAAIDefiesLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
498-664 |
1.60e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.42 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTiynknlsemqdleeirkitgvCPQfnvQFDIL----- 572
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------------------RPA---GARVLflpqr 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 ------TVKENLSLFAKIKGIHPQEVEQEVQRILLE--LDMQNIQDNLAKHLSEGQKRKLTFGIAILGDPQILLLDEPTT 644
Cdd:COG4178 435 pylplgTLREALLYPATAEAFSDAELREALEAVGLGhlAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180
....*....|....*....|
gi 1622880985 645 GLDPFSRDQVWSLLREHRAD 664
Cdd:COG4178 515 ALDEENEAALYQLLREELPG 534
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1298-1472 |
1.85e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1298 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK--PTAGEVELKGCSsvlghlgyCPQENVL----WPMLT 1371
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ--------FGREASLidaiGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1372 AREHLEVYAAVkGLrkVDARLAITrlvsafklheqlnvPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1451
Cdd:COG2401 112 FKDAVELLNAV-GL--SDAVLWLR--------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|.
gi 1622880985 1452 MWQAIQAVVKNTERGVLLTTH 1472
Cdd:COG2401 175 VARNLQKLARRAGITLVVATH 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
481-691 |
2.29e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL---SEMQDLEEirK 557
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALEN--G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQFNvQFDILTVKENLSLFA-KIKG--IHPQEVEQEVQRILLELDMQ-NIQDNLAKhLSEGQKRKLTFGIAILGD 633
Cdd:PRK10982 75 ISMVHQELN-LVLQRSVMDNMWLGRyPTKGmfVDQDKMYRDTKAIFDELDIDiDPRAKVAT-LSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880985 634 PQILLLDEPTTGLDPFSRDQVWSLLREHRADHV-ILFSTQSMDEADILADRKVIMSNGR 691
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1305-1495 |
2.35e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGHLGYCPQENVLWPMLTAREHLEVYAAV-- 1382
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG-KKINNHNANEAINHGFALVTEERRSTGIYAYLdi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1383 ---KGLRKVDARLAITRLVSAFKLH-------EQLNV--PVQK-----LTTGTMRKLCFVLSLLGNSPVLLLDEPSTGID 1445
Cdd:PRK10982 344 gfnSLISNIRNYKNKVGLLDNSRMKsdtqwviDSMRVktPGHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1446 PTGQQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGRLRCI 1495
Cdd:PRK10982 424 VGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
481-658 |
2.44e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 481 IRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSvPTEGSVTIYNKNLSEMQDLE----EIR 556
Cdd:PRK15093 6 IRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVT-KDNWRVTADRMRFDDIDLLRlsprERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 557 KITG--VCPQFNVQFDILTVKENL--SLFAKI-----KGIHPQEVEQEVQRILlEL-------DMQNIQDNLAKHLSEGQ 620
Cdd:PRK15093 85 KLVGhnVSMIFQEPQSCLDPSERVgrQLMQNIpgwtyKGRWWQRFGWRKRRAI-ELlhrvgikDHKDAMRSFPYELTEGE 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622880985 621 KRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQVWSLL 658
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLL 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
503-659 |
3.36e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 503 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSvtiYNKNLSEMQDL--EEIRKITGVCPQFNvQFDILTVKENLSl 580
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---RQSQFSHITRLsfEQLQKLVSDEWQRN-NTDMLSPGEDDT- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 581 fakikGIHPQEVEQEVQR---ILLELDMQ-NIQDNLA---KHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFSRDQ 653
Cdd:PRK10938 99 -----GRTTAEIIQDEVKdpaRCEQLAQQfGITALLDrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
....*.
gi 1622880985 654 VWSLLR 659
Cdd:PRK10938 174 LAELLA 179
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1297-1472 |
3.89e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1297 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSS-----SIRMISGITkpTAGEVELKGC---SSVLGHLGYCPQENVLWP 1368
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTllnvlAERVTTGVI--TGGDRLVNGRpldSSFQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHLEVYAAVKGLRKV------DARLAITRLVSAFKLHEQL-NVPVQKLTTGTMRKLCFVLSLLGNSPVLL-LDEP 1440
Cdd:TIGR00956 850 TSTVRESLRFSAYLRQPKSVsksekmEYVEEVIKLLEMESYADAVvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190
....*....|....*....|....*....|....
gi 1622880985 1441 STGIDptgQQQMWQAIQAVVK--NTERGVLLTTH 1472
Cdd:TIGR00956 930 TSGLD---SQTAWSICKLMRKlaDHGQAILCTIH 960
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
468-541 |
3.97e-05 |
|
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: 48.39 E-value: 3.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 468 PVAPEFqGKEAIRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI 541
Cdd:TIGR03719 313 PPGPRL-GDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1295-1503 |
5.60e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.68 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1295 FSKRKKKIAArNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS----------------SVLGHLG 1358
Cdd:PRK11831 15 FTRGNRCIFD-NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsrsrlytvrkrmSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1359 YCPQ-----ENVLWPMltaREHLEVYAAVkgLRK-VDARLAITRLVSAFKLheqlnVPVQkLTTGTMRKLCFVLSLLGNS 1432
Cdd:PRK11831 94 ALFTdmnvfDNVAYPL---REHTQLPAPL--LHStVMMKLEAVGLRGAAKL-----MPSE-LSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1433 PVLLLDEPSTGIDPTGQQQMWQAIQAVvkNTERGV--LLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1503
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISEL--NSALGVtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
498-668 |
6.35e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.02 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDiLTVKEN 577
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-GLHDLRFKITIIPQDPVLFS-GSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 578 LSLFAKIKgihPQEVEQEVQRILLELDMQNIQDNL-------AKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLDPFS 650
Cdd:TIGR00957 1380 LDPFSQYS---DEEVWWALELAHLKTFVSALPDKLdhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
170
....*....|....*...
gi 1622880985 651 RDQVWSLLREHRADHVIL 668
Cdd:TIGR00957 1457 DNLIQSTIRTQFEDCTVL 1474
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
495-530 |
7.82e-05 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 44.84 E-value: 7.82e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1622880985 495 VEALKGLLfdiyEGQITAILGHSGAGKSSLLNILNG 530
Cdd:pfam03193 97 IEALKELL----KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1273-1491 |
8.23e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 47.37 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1273 DEKPVIIASCLHKEYAGQKKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITkPTAGEVELKGCSs 1352
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQD- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1353 vLGHLGycPQEnvlwpMLTAREHLEV-----YAAvkglrkVDARLAITRLVS-AFKLHEqlnvpvQKLTTGTMRKLcfVL 1426
Cdd:COG4172 349 -LDGLS--RRA-----LRPLRRRMQVvfqdpFGS------LSPRMTVGQIIAeGLRVHG------PGLSAAERRAR--VA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1427 SLL---GNSP-----------------------------VLLLDEPSTGIDPTGQQQM---WQAIQAvvkntERGV--LL 1469
Cdd:COG4172 407 EALeevGLDPaarhryphefsggqrqriaiaralilepkLLVLDEPTSALDVSVQAQIldlLRDLQR-----EHGLayLF 481
|
250 260
....*....|....*....|..
gi 1622880985 1470 TTHNLAEAEALCDRVAIMVSGR 1491
Cdd:COG4172 482 ISHDLAVVRALAHRVMVMKDGK 503
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
498-647 |
1.12e-04 |
|
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: 47.21 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 498 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTiYNKNLSemqdleeirkitgVCPQFNVqfdIL--TVK 575
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRIS-------------FSPQTSW---IMpgTIK 504
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622880985 576 ENLSL------FAKIKGIHPQEVEQEVQrILLELDMQNIQDNlAKHLSEGQKRKLTFGIAILGDPQILLLDEPTTGLD 647
Cdd:TIGR01271 505 DNIIFglsydeYRYTSVIKACQLEEDIA-LFPEKDKTVLGEG-GITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1314-1456 |
2.02e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1314 GEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-KGCSsvlghLGYCPQENVlwPMLTARE----HLevyaavkglrkv 1388
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIK-----LGYFAQHQL--EFLRADEsplqHL------------ 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1389 dARLAITRL-------VSAFKLH-EQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1456
Cdd:PRK10636 399 -ARLAPQELeqklrdyLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1492 |
2.03e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELK----GCSSVLGHLGYCPQENVLWPMLTAREHLEV 1378
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYSKKIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1379 ------YAAVK--------------GLRKVDAR-LAITRLVSAFKLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLL 1437
Cdd:PRK13631 121 vfqfpeYQLFKdtiekdimfgpvalGVKKSEAKkLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1438 DEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1305-1364 |
2.33e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 2.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQEN 1364
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANI----GYYAQDH 391
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
495-535 |
2.56e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 44.81 E-value: 2.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1622880985 495 VEALKGLLfdiyEGQITAILGHSGAGKSSLLN-ILNGLSVPT 535
Cdd:PRK00098 155 LDELKPLL----AGKVTVLAGQSGVGKSTLLNaLAPDLELKT 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1305-1472 |
2.68e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGitKPTAGEVElkGCSSVLGH----------LGYCPQENVLWPMLTARE 1374
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE--GDIRISGFpkkqetfariSGYCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1375 HLeVYAAVKGLRK----------VDARLAITRLVSafkLHEQL-NVP-VQKLTTGTMRKLCFVLSLLGNSPVLLLDEPST 1442
Cdd:PLN03140 973 SL-IYSAFLRLPKevskeekmmfVDEVMELVELDN---LKDAIvGLPgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190
....*....|....*....|....*....|
gi 1622880985 1443 GIDPTGQQQMWQAIQAVVkNTERGVLLTTH 1472
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
499-698 |
3.61e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 499 KGLLFD----IYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiynknLSEmqdleeiRKITGVcPQfnvQFDIL-- 572
Cdd:PTZ00243 673 KVLLRDvsvsVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAE-------RSIAYV-PQ---QAWIMna 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 573 TVKENLSLFAKIKGIHPQEVEQEVQrilLELDMQNIQDNLAK-------HLSEGQKRKLTFGIAILGDPQILLLDEPTTG 645
Cdd:PTZ00243 736 TVRGNILFFDEEDAARLADAVRVSQ---LEADLAQLGGGLETeigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 646 LDPFSRDQ-VWSLLREHRADHVILFSTQSMDEADiLADRKVIMSNGRLKCAGSS 698
Cdd:PTZ00243 813 LDAHVGERvVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSS 865
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1305-1369 |
4.15e-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: 44.08 E-value: 4.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKgcssvlGHLGYCPQenVLWPM 1369
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS------GRISFSSQ--FSWIM 110
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1303-1337 |
4.92e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 4.92e-04
10 20 30
....*....|....*....|....*....|....*
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGI 1337
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV 54
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1306-1504 |
5.43e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 44.13 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1306 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP----TA-----GEVELKGCSS-----VLGH-LGYCPQE--NVLWP 1368
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTAdrfrwNGIDLLKLSPrerrkIIGReIAMIFQEpsSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1369 MLTAREHL-EVYAA--VKGL---RKVDARLAITRLVS--AFKLHEQL--NVPVQkLTTGTMRKLCFVLSLlGNSPVLLL- 1437
Cdd:COG4170 105 SAKIGDQLiEAIPSwtFKGKwwqRFKWRKKRAIELLHrvGIKDHKDImnSYPHE-LTEGECQKVMIAMAI-ANQPRLLIa 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1438 DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1504
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1307-1349 |
7.31e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.68 E-value: 7.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622880985 1307 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG 1349
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG 65
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1492 |
1.21e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.77 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1303 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLGYcPQENVLWPMLTAREHLEVYAAV 1382
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTK-EKEKVLEKLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1383 KGLRKvdaRLAITRLVSAFKLHEQ------------LNVPVQK-------------LTTGTMRKLCFVLS---------- 1427
Cdd:PRK13651 101 KEIRR---RVGVVFQFAEYQLFEQtiekdiifgpvsMGVSKEEakkraakyielvgLDESYLQRSPFELSggqkrrvala 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1428 -LLGNSP-VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRL 1492
Cdd:PRK13651 178 gILAMEPdFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1305-1445 |
1.21e-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: 43.78 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1305 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------SVLGHLGYCPQENVLWPMlTAREHLE 1377
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglhDLRFKITIIPQDPVLFSG-SLRMNLD 1381
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622880985 1378 VYAAVKGlRKVDARLAITRL---VSAF--KLHEQLNVPVQKLTTGTMRKLCFVLSLLGNSPVLLLDEPSTGID 1445
Cdd:TIGR00957 1382 PFSQYSD-EEVWWALELAHLktfVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
480-530 |
1.29e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 480 RIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG 530
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1290-1345 |
1.30e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.77 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880985 1290 QKKSCFSKRKKKIAARN-ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV 1345
Cdd:PRK15079 22 DGKQWFWQPPKTLKAVDgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV 78
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1301-1345 |
1.35e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622880985 1301 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV 1345
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
479-666 |
1.45e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 479 IRIRNVKKEYKgkSGKVEALKGllfdiyegqITAILGHSGAGKSSllnILNGLSVPTEGSVTIYNKNLSEMQDL-EEIRK 557
Cdd:cd03240 4 LSIRNIRSFHE--RSEIEFFSP---------LTLIVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKLiREGEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 558 ITGVCPQF-NVQFDILTVKENLSLFAKIKGIHpQEveqEVQRILLELdmqniqdnlAKHLSEGQKRKLTFGIAI-----L 631
Cdd:cd03240 70 RAQVKLAFeNANGKKYTITRSLAILENVIFCH-QG---ESNWPLLDM---------RGRCSGGEKVLASLIIRLalaetF 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622880985 632 GDP-QILLLDEPTTGLDPFSRDQVWS-LLREHRADHV 666
Cdd:cd03240 137 GSNcGILALDEPTTNLDEENIEESLAeIIEERKSQKN 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
468-541 |
2.21e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 2.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622880985 468 PVAPEFqGKEAIRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI 541
Cdd:PRK11819 315 PPGPRL-GDKVIEAENLSKSFGDRL----LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
610-670 |
4.54e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 41.65 E-value: 4.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622880985 610 DNLAKHLSEGQKRKLTF--------GIAILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--HRADHVILFS 670
Cdd:COG4694 486 AKPAKTLSEGEKTAIALayflaeleGDENDLKKKIVVIDDPVSSLDSNHRFAVASLLKElsKKAKQVIVLT 556
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1017-1171 |
6.12e-03 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 39.95 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880985 1017 GSFFLFLVLCSISPYITMGSISDYKKNAKSQLWISGLYT-SAYWCGQALVDVSFFILILLAMYLIFYienmqyllitsqi 1095
Cdd:pfam01061 48 GLLFFSILFNAFSALSGISPVFEKERGVLYRELASPLYSpSAYVLAKILSELPLSLLQSLIFLLIVY------------- 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622880985 1096 vfalviVTPGYAASLVFLIYMISFIFrkrrknsalwSFYFFFASIIMFVTALISNFDLSILITTMVLVPSYTLLGF 1171
Cdd:pfam01061 115 ------FMVGLPPSAGRFFLFLLVLL----------LTALAASSLGLFISALAPSFEDASQLGPLVLLPLLLLSGF 174
|
|
| |
