|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
174-1593 |
1.56e-113 |
|
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: 399.77 E-value: 1.56e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 174 GFVALQTAINTAIieitTNHPVMEElmSVTAITMKTLP---FITKN--LLHNEMFILFFLLHFsplVYFISLNVT----K 244
Cdd:TIGR01257 607 GFAYLQDMVEQGI----TRSQMQAE--PPVGIYLQQMPypcFVDDSfmIILNRCFPIFMVLAW---IYSVSMTVKsivlE 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 245 ERKKSKNLMKMMGLQDSAFWLSWGLIYAGFIFIISIFVTIIITFTQIIVMTGFMVIFILFFLYGLSLVALVFLMSVLLKK 324
Cdd:TIGR01257 678 KELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 325 AVLTNLV--VFLLTLFWGCLGFTVFYEQLPSSLEWILNICSPFAFTTGMIQIIKLDYNLNGV----IFPDP-SGDSYTMI 397
Cdd:TIGR01257 758 ASLAAACsgVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLqwsnIGNSPlEGDEFSFL 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 398 ATFSMLLLDGLIYLLLALYFDKILPyGDERHYSPLFFLNSSSCF--------QHQRTNAK---VIEKEIDAEHP---SDD 463
Cdd:TIGR01257 838 LSMKMMLLDAALYGLLAWYLDQVFP-GDYGTPLPWYFLLQESYWlggegcstREERALEKtepLTEEMEDPEHPegiNDS 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 464 YFEPVAPEFQgkEAIRIRNVKKEYKgKSGKvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK 543
Cdd:TIGR01257 917 FFERELPGLV--PGVCVKNLVKIFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 544 NLSemQDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKL 623
Cdd:TIGR01257 993 DIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKL 1070
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 624 TFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSMFLKRR 703
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNC 1150
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 704 WGLGYHLSLHRN------------------------------EICNPEQI--------TSFITHHIPDAKLKTENKEKLV 745
Cdd:TIGR01257 1151 FGTGFYLTLVRKmkniqsqrggcegtcsctskgfstrcparvDEITPEQVldgdvnelMDLVYHHVPEAKLVECIGQELI 1230
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 746 YTLPLE--RTNTFPDLFSDLDKC-SDQGVTGYDISMSTLNEVFMKLEGQST--------IEQDFEQVEM----IRDSESL 810
Cdd:TIGR01257 1231 FLLPNKnfKQRAYASLFRELEETlADLGLSSFGISDTPLEEIFLKVTEDADsgslfaggAQQKRENANLrhpcSGPTEKA 1310
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 811 NEMELAHSSFSEMQTAVSDMG------------------LWRMQVFAMARLRFLKLKRQTK-----VLLTLLLVFGIAIF 867
Cdd:TIGR01257 1311 GQTPQASHTCSPGQPAAHPEGqpppepedpgvplntgarLILQHVQALLVKRFQHTIRSHKdflaqIVLPATFVFLALML 1390
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 868 PLIVENI-----------MYA----------------------MLNE--------KIDW--EFK--NELYFLSPG----- 897
Cdd:TIGR01257 1391 SIIIPPFgeypaltlhpwMYGqqytffsmdepnsehlevladvLLNKpgfgnrclKEEWlpEYPcgNSTPWKTPSvspni 1470
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 898 ---------------------------QLPQEP-------------RTSLLIINNTESNIEDFI---------KSLKHQn 928
Cdd:TIGR01257 1471 thlfqkqkwtaahpspscrcstrekltMLPECPegagglpppqrtqRSTEILQDLTDRNISDFLvktypalirSSLKSK- 1549
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 929 ilLEVDdfENRNGtdGLSYNG---AIIVSGK-----------------------------------QKDYRFSVVCNTKR 970
Cdd:TIGR01257 1550 --FWVN--EQRYG--GISIGGklpAIPITGEalvgflsdlgqmmnvsggpvtreaskempdflkhlETEDNIKVWFNNKG 1623
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 971 LHCFPILMNIISNGLLQMFNHTQH------IRIESSPF-----PLSHIGLWTGLPDGS------FFLFLVLCSISPYItm 1033
Cdd:TIGR01257 1624 WHALVSFLNVAHNAILRASLPKDRdpeeygITVISQPLnltkeQLSEITVLTTSVDAVvaicviFAMSFVPASFVLYL-- 1701
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1034 gsISDYKKNAKSQLWISGLYTSAYWCGQALVDVSFFILILLLMYLIFyIENMQYLLITSQIVFALVIVTPGYAASLVFFI 1113
Cdd:TIGR01257 1702 --IQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIF-IGFQKKAYTSPENLPALVALLMLYGWAVIPMM 1778
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1114 YMISFIFRKRRKNSGLWSFYFFF----ASTIMFSITLI-NHFDL----SILITTMVLVPSYT----LLGFKTFLEVRDQe 1180
Cdd:TIGR01257 1779 YPASFLFDVPSTAYVALSCANLFiginSSAITFVLELFeNNRTLlrfnAMLRKLLIVFPHFClgrgLIDLALSQAVTDV- 1857
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1181 hYREFPEA------NFELSATDFLVCFIP---YFQTLLFV----FVLRCMelkcgkkrmrkdpvfrispqsrdAKPNPEE 1247
Cdd:TIGR01257 1858 -YAQFGEEhsanpfQWDLIGKNLVAMAVEgvvYFLLTLLIqhhfFLSRWI-----------------------AEPAKEP 1913
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1248 PIDEDEDIQTERIRTATAlttsiLDEKPVIIASCLHKEYAGQKKScfskrkkkiAARNISFCVQEGEILGLLGPNGAGKS 1327
Cdd:TIGR01257 1914 IFDEDDDVAEERQRIISG-----GNKTDILRLNELTKVYSGTSSP---------AVDRLCVGVRPGECFGLLGVNGAGKT 1979
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1328 SSIRMISGITKPTAGEVELKG------CSSVLGHLGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFK 1401
Cdd:TIGR01257 1980 TTFKMLTGDTTVTSGDATVAGksiltnISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLG 2059
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1402 LHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCD 1481
Cdd:TIGR01257 2060 LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCT 2138
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1482 RVAIMVSGRLRCIGSIQHLKNKLGKDYILELKVKETSQVTL-----VHTEILKLFPQAAGQERYSSLLTYKLPVADvypL 1556
Cdd:TIGR01257 2139 RLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDLLpdlnpVEQFFQGNFPGSVQRERHYNMLQFQVSSSS---L 2215
|
1690 1700 1710
....*....|....*....|....*....|....*..
gi 27436953 1557 SQTFHKLEAVKHNFNLEEYSLSQCTLEKVFLELSKEQ 1593
Cdd:TIGR01257 2216 ARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1296-1501 |
1.88e-81 |
|
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: 267.06 E-value: 1.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1296 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWPML 1369
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdrkAARQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1449
Cdd:cd03263 91 TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1450 QMWQAIQAVVKNteRGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLK 1501
Cdd:cd03263 171 AIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
478-701 |
1.10e-78 |
|
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: 258.97 E-value: 1.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLseMQDLEEIRKI 557
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSMFLK 701
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1295-1512 |
3.42e-70 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 235.34 E-value: 3.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWP 1367
Cdd:COG1131 7 TKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1447
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 1448 QQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYILEL 1512
Cdd:COG1131 167 RRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLEL 230
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
478-696 |
1.49e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 227.64 E-value: 1.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqDLEEIRKI 557
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1276-1507 |
9.86e-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: 194.31 E-value: 9.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1276 VIIASCLHKEYagqkkscfskrKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSS---- 1351
Cdd:COG4555 1 MIEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkep 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1352 --VLGHLGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLG 1429
Cdd:COG4555 70 reARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1430 NSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKD 1507
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
478-696 |
3.36e-55 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 192.77 E-value: 3.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqDLEEIRKI 557
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK--EPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1302-1589 |
2.86e-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: 189.14 E-value: 2.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcsSVLGH------------LGYCPQENVLWPML 1369
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTA------RVAGYdvvreprkvrrsIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1449
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1450 QMWQAIQAVVKnTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYILELKVKETSQVTLVHTEILK 1529
Cdd:TIGR01188 162 AIWDYIRALKE-EGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1530 LFPQAAGQERYSSLL-TYKLPVADvypLSQTFHKL--EAVKHNFNLEEYSLSQCTLEKVFLEL 1589
Cdd:TIGR01188 241 LGETGLGLLAVTVDSdRIKILVPD---GDETVPEIveAAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1295-1491 |
5.93e-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: 183.37 E-value: 5.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWP 1367
Cdd:cd03230 7 SKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDikkepeEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLevyaavkglrkadarlaiarlvsafklheqlnvpvqKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1447
Cdd:cd03230 87 NLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 1448 QQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03230 131 RREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
478-691 |
2.82e-52 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 181.44 E-value: 2.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqDLEEIRKI 557
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLslfakikgihlkeveqevqrilleldmqniqdnlakHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKtILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1295-1595 |
1.40e-50 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 181.46 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---CSSVLGHLGYCPQENVLWPMLT 1370
Cdd:COG4152 8 TKRfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGeplDPEDRRRIGYLPEERGLYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1450
Cdd:COG4152 88 VGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1451 MWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKdYILELKVKETsqvtlvhTEIL 1528
Cdd:COG4152 168 LKDVIREL---AAKGttVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR-NTLRLEADGD-------AGWL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1529 KLFPQAAGQERYSSLLTYKLPvADVYPlsQTFhkLEAVKHNFNLEEYSLSQCTLEKVFLELSKEQEV 1595
Cdd:COG4152 237 RALPGVTVVEEDGDGAELKLE-DGADA--QEL--LRALLARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1302-1501 |
1.51e-50 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 178.33 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWPMLTLREHL 1375
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvreprEVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 EVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1455
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27436953 1456 QAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLK 1501
Cdd:cd03265 175 EKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
492-790 |
1.70e-50 |
|
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: 181.43 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLseMQDLEEIRKITGVCPQFNVQFDIL 571
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRKVRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 TVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRD 651
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 652 QVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSMFLKRRWGlGYHLSLHRNEICNPEQITSFITHH 730
Cdd:TIGR01188 162 AIWDYIRAlKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 731 IPDAKLKTENKEKL--VYTLPLER-TNTFPDLFSDLDKcsdQGVTGYDISM--STLNEVFMKLEG 790
Cdd:TIGR01188 241 LGETGLGLLAVTVDsdRIKILVPDgDETVPEIVEAAIR---NGIRIRSISTerPSLDDVFLKLTG 302
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1276-1517 |
4.43e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 174.89 E-value: 4.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1276 VIIASCLHKEY---------AGQKKSCFSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVE 1345
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRREYREVEAvDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1346 LkgcssvlghLGYCPQEN----------V------LWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVP 1409
Cdd:COG4586 81 V---------LGYVPFKRrkefarrigvVfgqrsqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1410 VQKLTAGiTRKLC-FVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVvkNTERG--VLLTTHNLAEAEALCDRVAIM 1486
Cdd:COG4586 152 VRQLSLG-QRMRCeLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRERGttILLTSHDMDDIEALCDRVIVI 228
|
250 260 270
....*....|....*....|....*....|.
gi 27436953 1487 VSGRLRCIGSIQHLKNKLGKDYILELKVKET 1517
Cdd:COG4586 229 DHGRIIYDGSLEELKERFGPYKTIVLELAEP 259
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
479-690 |
1.62e-47 |
|
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: 169.18 E-value: 1.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 479 RIRNVKKEYKGksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKIT 558
Cdd:cd03225 1 ELKNLSFSYPD--GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 559 GVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03225 78 GLVFQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGR 690
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
478-696 |
8.05e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 167.89 E-value: 8.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 557
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQF-NVQFDILTVKENLSlFA-KIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF-GITILgDPQ 634
Cdd:COG1122 77 VGLVFQNpDDQLFAPTVEEDVA-FGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIaGVLAM-EPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 635 ILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
478-701 |
1.21e-46 |
|
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: 167.16 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNknLSEMQDLEEIRKI 557
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAGSSMFLK 701
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1294-1495 |
2.56e-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: 165.92 E-value: 2.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---SVLGHLGYCPQENVLWPML 1369
Cdd:cd03269 6 VTKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiAARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1449
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27436953 1450 QMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:cd03269 166 LLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
478-691 |
1.89e-45 |
|
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: 163.81 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIR 555
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLseKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 --KITGVCPQFNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDP 633
Cdd:cd03255 81 rrHIGFVFQSFNL-LPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 634 QILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADiLADRKVIMSNGRL 691
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
478-692 |
1.66e-42 |
|
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: 155.04 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGqITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDleEIRKI 557
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ--KLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQ-FNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQIL 636
Cdd:cd03264 74 IGYLPQeFGV-YPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 637 LLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRLK 692
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 ... |
1294-1495 |
2.18e-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: 154.83 E-value: 2.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLW 1366
Cdd:cd03266 11 FRDVKKTVQAvDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDvvkepaEARRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1367 PMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1446
Cdd:cd03266 91 DRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27436953 1447 GQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:cd03266 171 ATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1304-1478 |
2.55e-42 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 154.17 E-value: 2.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHLGYCPQENVLWPMLTLREHLEV 1377
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 YAAVKGLRKADARlaIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1457
Cdd:COG4133 99 WAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170 180
....*....|....*....|...
gi 27436953 1458 VVkntERG--VLLTTHNLAEAEA 1478
Cdd:COG4133 177 HL---ARGgaVLLTTHQPLELAA 196
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
475-691 |
5.49e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 5.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 475 KEAIRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLE 552
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLseRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 553 EIR--KItGVCPQ-FNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQK------RKL 623
Cdd:COG1136 82 RLRrrHI-GFVFQfFNL-LPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQqrvaiaRAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 624 tfgitiLGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADIlADRKVIMSNGRL 691
Cdd:COG1136 160 ------VNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
478-691 |
1.15e-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: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEIR 555
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITG-VCPQFNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRiLLEL-DMQNIQDNLAKHLSEGQKRKLTFGITILGDP 633
Cdd:cd03258 82 RRIGmIFQHFNL-LSSRTVFENVALPLEIAGVPKAEIEERVLE-LLELvGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 634 QILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
478-692 |
1.44e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 149.54 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNknlsemQDLEEIRKI 557
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG------EPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSN--GRLK 692
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
478-691 |
1.61e-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: 149.29 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNlseMQDLEEIRKI 557
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS---YQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGV---CPQFnvqFDILTVKENLSLFAKIKGIHlkevEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQ 634
Cdd:cd03268 74 IGAlieAPGF---YPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 635 ILLLDEPTTGLDPFSRDQVWSLLR-ERRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILsLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
478-695 |
2.96e-40 |
|
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: 148.67 E-value: 2.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIynKNLSEMQDLEEIRKI 557
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAG 695
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1295-1492 |
4.19e-40 |
|
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: 148.11 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGeILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWP 1367
Cdd:cd03264 7 TKRyGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqKLRRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPtg 1447
Cdd:cd03264 86 NFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27436953 1448 QQQMwqaiqaVVKN------TERGVLLTTHNLAEAEALCDRVAIMVSGRLR 1492
Cdd:cd03264 164 EERI------RFRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1290-1492 |
5.65e-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: 147.75 E-value: 5.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1290 KKSCFSKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-----CSSVLGHLGYCPQEN 1363
Cdd:cd03268 2 KTNDLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkNIEALRRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1364 VLWPMLTLREHLEVYAAVKGLRKADarlaIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGI 1443
Cdd:cd03268 82 GFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27436953 1444 DPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLR 1492
Cdd:cd03268 158 DPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
478-691 |
1.43e-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: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL-----SVPTEGSVTIYNKNLSEMQ-DL 551
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDvDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 552 EEIRKITGVCPQFNVQFDiLTVKENLSLFAKIKGIHLKEVEQEVQRILLE---LDmQNIQDNL-AKHLSEGQKRKLTFGI 627
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRkaaLW-DEVKDRLhALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 628 TILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1277-1491 |
2.82e-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: 146.71 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1277 IIASCLHKEYA---------GQKKSCFSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL 1346
Cdd:cd03267 1 IEVSNLSKSYRvyskepgliGSLKSLFKRKYREVEAlKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1347 KG-------------CSSVLGhlgycpQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKL 1413
Cdd:cd03267 81 AGlvpwkrrkkflrrIGVVFG------QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1414 TAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1300-1490 |
2.63e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 146.10 E-value: 2.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGH-------LGYCPQENVLWPMLTLR 1372
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRarharqrVGVVPQFDNLDPDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1452
Cdd:PRK13537 99 ENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27436953 1453 QAIQAVVKnteRG--VLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:PRK13537 179 ERLRSLLA---RGktILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
478-695 |
2.72e-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: 142.80 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqdleEIRKI 557
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAG 695
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
457-798 |
4.27e-38 |
|
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: 157.10 E-value: 4.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 457 AEHPSDDYFEPVAPEFQ-------GKEAIRIRNVKKEYKGKSGKveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG 529
Cdd:TIGR01257 1910 AKEPIFDEDDDVAEERQriisggnKTDILRLNELTKVYSGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 530 LSVPTEGSVTIYNKNLseMQDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQD 609
Cdd:TIGR01257 1988 DTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYAD 2065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 610 NLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVW----SLLRERRAdhvILFSTQSMDEADILADRKVI 685
Cdd:TIGR01257 2066 RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWntivSIIREGRA---VVLTSHSMEECEALCTRLAI 2142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 686 MSNGRLKCAGSSMFLKRRWGLGYHLSLhrnEICNPEQ--------ITSFITHHIPDAKLKTENKEKLVYTLPlerTNTFP 757
Cdd:TIGR01257 2143 MVKGAFQCLGTIQHLKSKFGDGYIVTM---KIKSPKDdllpdlnpVEQFFQGNFPGSVQRERHYNMLQFQVS---SSSLA 2216
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 27436953 758 DLFSDLDKCSDQ-GVTGYDISMSTLNEVFMKLEGQSTIEQDF 798
Cdd:TIGR01257 2217 RIFQLLISHKDSlLIEEYSVTQTTLDQVFVNFAKQQTETYDL 2258
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
497-643 |
5.99e-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: 139.71 E-value: 5.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSeMQDLEEIRKITGVCPQFNVQFDILTVKEN 576
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 577 LSLFAKIKGIHLKEVEQEVQRILLELDMQNI----QDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTT 643
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
478-690 |
2.28e-37 |
|
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: 139.92 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemQDLEEIRKI 557
Cdd:COG4133 3 LEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--DAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEveQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADH-VILFSTQsmDEADILADRKVIMSNGR 690
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGgAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
477-692 |
2.50e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.77 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsemqDLEEIRK 556
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK------PVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLtfGI--TILGDPQ 634
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV--AIarALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 635 ILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSN--GRLK 692
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
478-691 |
4.10e-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: 140.33 E-value: 4.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEIR 555
Cdd:cd03261 1 IELRGLTKSFGGR--TV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQFNVQFDILTVKENLSLFAKikgIHLKEVEQEVQRILLE-LDMQNI---QDNLAKHLSEGQKRKLTFGITILG 631
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLR---EHTRLSEEEIREIVLEkLEAVGLrgaEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 632 DPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-785 |
5.47e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 142.17 E-value: 5.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLsemqDLEEIRK 556
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 I------TGVCPQfnvqfdiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITIL 630
Cdd:COG4152 73 IgylpeeRGLYPK-------MKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGSSMFLKRRWGlgyh 709
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTtVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG---- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 710 lslHRNEICNPEQITSFItHHIPDAKLKTENKEKLVYTLPLERTNtfPDLFSDLdkcSDQG-VTGYDISMSTLNEVF 785
Cdd:COG4152 222 ---RNTLRLEADGDAGWL-RALPGVTVVEEDGDGAELKLEDGADA--QELLRAL---LARGpVREFEEVRPSLNEIF 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1305-1598 |
6.81e-37 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 153.25 E-value: 6.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFcvQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHLGYCPQENVLWPMLTLREHLEVY 1378
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1379 AAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIqaV 1458
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--L 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1459 VKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYILEL-------------------------- 1512
Cdd:TIGR01257 1106 KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrkmkniqsqrggcegtcsctskgfs 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1513 ------------------KVKETSQVTLVHTEILKLFpQAAGQErysslLTYKLPVADV--YPLSQTFHKLEAVKHNFNL 1572
Cdd:TIGR01257 1186 trcparvdeitpeqvldgDVNELMDLVYHHVPEAKLV-ECIGQE-----LIFLLPNKNFkqRAYASLFRELEETLADLGL 1259
|
330 340
....*....|....*....|....*.
gi 27436953 1573 EEYSLSQCTLEKVFLELSKEQEVGNF 1598
Cdd:TIGR01257 1260 SSFGISDTPLEEIFLKVTEDADSGSL 1285
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
478-690 |
3.59e-36 |
|
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: 135.20 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 557
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDiLTVKENLslfakikgihlkeveqevqrilleldmqniqdnlakhLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03228 78 IAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADiLADRKVIMSNGR 690
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
478-712 |
4.45e-36 |
|
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: 138.74 E-value: 4.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEY-KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL--SEMQDLEEI 554
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 RKITGVCPQF--------NVQFDILTVKENLslfakikGIHLKEVEQEVQRILlelDMQNIQDNLAKH----LSEGQKRK 622
Cdd:TIGR04521 81 RKKVGLVFQFpehqlfeeTVYKDIAFGPKNL-------GLSEEEAEERVKEAL---ELVGLDEEYLERspfeLSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 623 ltfgITILG----DPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:TIGR04521 151 ----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
250
....*....|....*...
gi 27436953 697 SM--FLKRRWGLGYHLSL 712
Cdd:TIGR04521 227 PRevFSDVDELEKIGLDV 244
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
479-690 |
5.44e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.29 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 479 RIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKIT 558
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-PLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 559 GVCPQfnvqfdiltvkenlslfakikgihlkeveqevqrilleldmqniqdnlakhLSEGQKRKLTFGITILGDPQILLL 638
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 639 DEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGR 690
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
478-696 |
8.68e-36 |
|
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: 137.56 E-value: 8.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVC---P--QF---NVQFDILTVKENLslfakikGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKltfgITI 629
Cdd:TIGR04520 79 VGMVfqnPdnQFvgaTVEDDVAFGLENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR----VAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 630 LG----DPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEAdILADRKVIMSNGRLKCAGS 696
Cdd:TIGR04520 148 AGvlamRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMNKGKIVAEGT 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1285-1490 |
1.08e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 139.58 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1285 EYAGQKKScfskRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcsSVLG---------- 1354
Cdd:PRK13536 43 DLAGVSKS----YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI------TVLGvpvpararla 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1355 --HLGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSP 1432
Cdd:PRK13536 113 raRIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1433 VLLLDEPSTGIDPTGQQQMWQAIQAVVKnteRG--VLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLA---RGktILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
478-691 |
2.12e-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: 134.57 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemqDLEEIRKI 557
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03259 154 LDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
478-691 |
3.05e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.17 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGkveaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 557
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDiLTVKENLSLFAKIKgiHLKEVEQEVQRILLELDMQniQDNLAK---HLSEGQKRKLTFGITILGDPQ 634
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLR--ERKFDRERALELLERLGLP--PDILDKpveRLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 635 ILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1304-1502 |
4.36e-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: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLGH------LGYCPQENVLWPMLTLREHL 1375
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrdITGLPPHeraragIGYVPEGRRIFPELTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 EVYAAVKGLRKADARlaIARLVSAF-KLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1454
Cdd:cd03224 97 LLGAYARRRAKRKAR--LERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27436953 1455 IQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1502
Cdd:cd03224 175 IRE-LRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
444-690 |
1.79e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 136.11 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 444 QRTNAKVIEKEID---AEHPSDDYFEPVAPEFQGKE--AIRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGA 518
Cdd:PRK13536 3 TRAVAEEAPRRLElspIERKHQGISEAKASIPGSMStvAIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 519 GKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRI 598
Cdd:PRK13536 79 GKSTIARMILGMTSPDAGKITVLGVPVPARARLA--RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 599 LLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRA-DHVILFSTQSMDEAD 677
Cdd:PRK13536 157 LEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAE 236
|
250
....*....|...
gi 27436953 678 ILADRKVIMSNGR 690
Cdd:PRK13536 237 RLCDRLCVLEAGR 249
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
478-690 |
2.46e-34 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 130.38 E-value: 2.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIR 555
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQFNVqFDILTVKENLSLfakikgihlkeveqevqrilleldmqniqdnlakHLSEGQKRKLTFGITILGDPQI 635
Cdd:cd03229 77 RIGMVFQDFAL-FPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGR 690
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
478-691 |
3.55e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.21 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIR 555
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALseRELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQfnvQFDIL---TVKENLSLFAKIKGIHLKEVEQEVQRiLLEL-DMQNIQDNLAKHLSEGQKRKLtfGI--TI 629
Cdd:COG1135 82 RKIGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRKRVAE-LLELvGLSDKADAYPSQLSGGQKQRV--GIarAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 630 LGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
481-691 |
1.45e-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: 128.82 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 481 RNVKKEYKGKSGKVEA--LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL--SVPTEGSVTIYNKNLsemqDLEEIRK 556
Cdd:cd03213 7 RNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL----DKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFNVQFDILTVKENLSLFAKIKGIhlkeveqevqrilleldmqniqdnlakhlSEGQKRKLTFGITILGDPQIL 636
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 637 LLDEPTTGLDPFSRDQVWSLLReRRAD--HVILFST-QSMDEADILADRKVIMSNGRL 691
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1294-1495 |
4.90e-33 |
|
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: 127.64 E-value: 4.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSV---LGHLGYCPQENVLWP 1367
Cdd:cd03259 6 LSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdVTGVppeRRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLeVYA-AVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1446
Cdd:cd03259 86 HLTVAENI-AFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27436953 1447 GQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1295-1496 |
5.40e-33 |
|
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: 128.43 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---------SVLGhLGYCPQENV 1364
Cdd:cd03218 7 SKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrARLG-IGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1365 LWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 1445 PTGQQQmwqaIQAVVKN-TER--GVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:cd03218 166 PIAVQD----IQKIIKIlKDRgiGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
477-696 |
7.69e-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: 128.17 E-value: 7.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEI 554
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 RKITGVCPQFNVQFDILTVKENLSLFakikgihLKEV----EQEVQRILLE-LDMQNIQDnlAKH-----LSEGQKRKLt 624
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFP-------LREHtdlsEAEIRELVLEkLELVGLPG--AADkmpseLSGGMRKRV- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 625 fGI--TILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH-----VIlfsTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:COG1127 151 -ALarALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsvVV---THDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
478-691 |
9.41e-33 |
|
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: 128.19 E-value: 9.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 557
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRI--LLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELlaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLR--ERRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-690 |
2.03e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 129.15 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRk 556
Cdd:PRK13537 7 PIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 iTGVCPQF-NVQFDiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:PRK13537 82 -VGVVPQFdNLDPD-FTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRERRA-DHVILFSTQSMDEADILADRKVIMSNGR 690
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1304-1441 |
2.22e-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: 123.53 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMLTLREHLE 1376
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltddeRKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1377 VYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGIT----RKLCFVLSLLGNSPVLLLDEPST 1441
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSggqrQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
478-691 |
3.21e-32 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 126.08 E-value: 3.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD--LEEIR 555
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQ-----FNvqfDILTVKENLSLFAKIKGIHLKEVEQEvqRILLELDMQ-----NIQDNLAKHLSEGQKRKLTF 625
Cdd:cd03257 82 KEIQMVFQdpmssLN---PRMTIGEQIAEPLRIHGKLSKKEARK--EAVLLLLVGvglpeEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 626 GITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
477-696 |
3.88e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.10 E-value: 3.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPT---EGSVTIYNKNLSEMQDLEE 553
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 554 IRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDP 633
Cdd:COG1123 82 GRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 634 QILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
478-690 |
6.23e-32 |
|
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: 124.85 E-value: 6.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIhlKEVEQEVQRIlLEL--DMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRR--AKRKARLERV-YELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGR 690
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVtILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
475-691 |
1.92e-31 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 123.98 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 475 KEAIRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIyNKNLSEMQDLEEI 554
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-AGLVPWKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 RKITGVCPQFN-VQFDiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDP 633
Cdd:cd03267 94 RRIGVVFGQKTqLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 634 QILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
466-697 |
1.97e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.79 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 466 EPVAPEFQGKEAIRIRNVKKEYKGKS-GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKN 544
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 545 LSEM--QDLEEIRKITGVCPQF-NVQFD-ILTVKENLSLFAKIKGIH-LKEVEQEVQRIL----LELDMqniqdnLAKH- 614
Cdd:COG1123 329 LTKLsrRSLRELRRRVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLLsRAERRERVAELLervgLPPDL------ADRYp 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 615 --LSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHV--ILFSTQSMDEADILADRKVIMSNGR 690
Cdd:COG1123 403 heLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGltYLFISHDLAVVRYIADRVAVMYDGR 482
|
....*..
gi 27436953 691 LKCAGSS 697
Cdd:COG1123 483 IVEDGPT 489
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1304-1502 |
2.71e-31 |
|
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: 123.55 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGH---------LGYCPQENVLWPMLTLREH 1374
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG-EDITGLpphriarlgIGYVPEGRRIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 LEVyAAVKGLRKADARLAIARLVSAF-KLHEQLNVPVQKLTAG------ITRklcfvlSLLGNSPVLLLDEPSTGIDPTG 1447
Cdd:COG0410 99 LLL-GAYARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGeqqmlaIGR------ALMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1448 QQQMWQAIQAVVkntERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1502
Cdd:COG0410 172 VEEIFEIIRRLN---REGvtILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
444-710 |
4.11e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 130.66 E-value: 4.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 444 QRTNAkVIEKEIDAEHPSDDYFEPVAPefqgkeAIRIRNVKKEYKGksGKVEALKGLLFDIYEGQITAILGHSGAGKSSL 523
Cdd:COG4987 307 RRLNE-LLDAPPAVTEPAEPAPAPGGP------SLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 524 LNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDIlTVKENLsLFAKIKGIH--LKEVEQEVQriLLE 601
Cdd:COG4987 378 LALLLRFLDPQSGSITLGGVDLRDL-DEDDLRRRIAVVPQRPHLFDT-TLRENL-RLARPDATDeeLWAALERVG--LGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 602 LdMQNIQDNL-------AKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMD 674
Cdd:COG4987 453 W-LAALPDGLdtwlgegGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
250 260 270
....*....|....*....|....*....|....*.
gi 27436953 675 EADiLADRKVIMSNGRLKCAGSSMFLKRRWGLGYHL 710
Cdd:COG4987 532 GLE-RMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
477-696 |
5.64e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 123.23 E-value: 5.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 556
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL-SRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFN-VQFDiLTVKE--------NLSLFAKIKgihlKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGI 627
Cdd:COG1120 76 RIAYVPQEPpAPFG-LTVRElvalgrypHLGLFGRPS----AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 628 TILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1304-1499 |
9.51e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 9.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS--SVLGHLGYCPQ-ENVLW--PMlTLRE----- 1373
Cdd:COG1121 23 EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprRARRRIGYVPQrAEVDWdfPI-TVRDvvlmg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 ---HLevyAAVKGLRKADaRLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1450
Cdd:COG1121 102 rygRR---GLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27436953 1451 MWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVaIMVSGRLRCIGSIQH 1499
Cdd:COG1121 178 LYELLRELRRE-GKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1296-1495 |
1.65e-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: 120.72 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1296 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLGhLGYCPQenvlwPMLTLREH 1374
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrVSSLLG-LGGGFN-----PELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 LEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEP-STGiDPTGQQQMWQ 1453
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 1454 AIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:cd03220 184 RLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1295-1502 |
1.78e-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: 121.23 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---------SVLGhLGYCPQENV 1364
Cdd:TIGR04406 8 IKSyKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDithlpmherARLG-IGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1365 LWPMLTLREHLE-VYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGI 1443
Cdd:TIGR04406 87 IFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1444 DPTGQQQmwqaIQAVVKN-TER--GVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1502
Cdd:TIGR04406 167 DPIAVGD----IKKIIKHlKERgiGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
478-659 |
2.34e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.54 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDlEEI--- 554
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR-REIpyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 -RKItGVCPQ-FNVQFDiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLtfGIT--IL 630
Cdd:COG2884 78 rRRI-GVVFQdFRLLPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV--AIAraLV 153
|
170 180
....*....|....*....|....*....
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRE 659
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEE 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
478-691 |
2.61e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.76 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIR 555
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQfnvQFDIL---TVKENLSLFAKIKGIHLKEVEQEVQRiLLEL-DMQNIQDNLAKHLSEGQKRKLtfGI--TI 629
Cdd:PRK11153 82 RQIGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKARVTE-LLELvGLSDKADRYPAQLSGGQKQRV--AIarAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 630 LGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
478-691 |
2.94e-30 |
|
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: 119.94 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS-EMQDLEEIRK 556
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITG-VCPQFNVqFDILTVKENLSL-FAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQ 634
Cdd:cd03262 77 KVGmVFQQFNL-FPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 635 ILLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
478-696 |
4.31e-30 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 120.23 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKi 557
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 tGVCPQF-NVQ-FDILTVKENL----------SLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF 625
Cdd:cd03219 76 -GIGRTFqIPRlFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 626 GITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1296-1490 |
4.78e-30 |
|
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: 117.35 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1296 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQenvlwpm 1368
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdiaklplEELRRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1369 ltlrehlevyaAVKGLRKadaRLAIARLvsafklheqlnvpvqkltagitrklcfvlsLLGNSPVLLLDEPSTGIDPTGQ 1448
Cdd:cd00267 81 -----------LSGGQRQ---RVALARA------------------------------LLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 1449 QQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:cd00267 117 ERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1275-1496 |
5.33e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 119.75 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1275 PVIIASCLHKEYagqkkscfskrKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSV-- 1352
Cdd:COG1137 2 MTLEAENLVKSY-----------GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG-EDIth 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1353 --------LGhLGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAG------IT 1418
Cdd:COG1137 70 lpmhkrarLG-IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGerrrveIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1419 RklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQmwqaIQAVVKN-TER--GVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:COG1137 149 R------ALATNPKFILLDEPFAGVDPIAVAD----IQKIIRHlKERgiGVLITDHNVRETLGICDRAYIISEGKVLAEG 218
|
.
gi 27436953 1496 S 1496
Cdd:COG1137 219 T 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
454-710 |
6.30e-30 |
|
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: 128.41 E-value: 6.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 454 EIDAEHPSDDYFEPVaPEFQGkeAIRIRNVKKEYKGKSgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVP 533
Cdd:COG2274 453 DLPPEREEGRSKLSL-PRLKG--DIELENVSFRYPGDS--PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 534 TEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDIlTVKENLSLF------------AKIKGIHlkeveQEVQRILLE 601
Cdd:COG2274 528 TSGRILIDGIDLRQI-DPASLRRQIGVVLQDVFLFSG-TIRENITLGdpdatdeeiieaARLAGLH-----DFIEALPMG 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 602 LDMQnIQDNlAKHLSEGQKRKLtfGI--TILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADiL 679
Cdd:COG2274 601 YDTV-VGEG-GSNLSGGQRQRL--AIarALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIR-L 675
|
250 260 270
....*....|....*....|....*....|.
gi 27436953 680 ADRKVIMSNGRLKCAGSSMFLKRRWGLGYHL 710
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1294-1490 |
7.68e-30 |
|
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: 117.29 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---------CSSVLGHLGYCPQEN 1363
Cdd:cd03229 6 VSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledeLPPLRRRIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1364 VLWPMLTLREHLeVYAAVKGLRKadaRLAIARlvsafklheqlnvpvqkltagitrklcfvlSLLGNSPVLLLDEPSTGI 1443
Cdd:cd03229 86 ALFPHLTVLENI-ALGLSGGQQQ---RVALAR------------------------------ALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27436953 1444 DPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1295-1497 |
9.00e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 9.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLGH-LGYCPQenvlwpmLTLR 1372
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrVSALLELgAGFHPE-------LTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKGLRKADARLAIARLVsAF-KLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEP-STGiDPTGQQQ 1450
Cdd:COG1134 107 ENIYLNGRLLGLSRKEIDEKFDEIV-EFaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DAAFQKK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27436953 1451 MWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSI 1497
Cdd:COG1134 185 CLARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
477-703 |
1.06e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.23 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRK 556
Cdd:PRK13647 4 IIEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:PRK13647 80 KVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLL-RERRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSMFLKRR 703
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
477-691 |
1.18e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.39 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEI 554
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 RKITGVCPQfnvQFDI---LTVKEN--------LSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKL 623
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 624 tfGI--TILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHV-ILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:COG3638 156 --AIarALVQEPKLILADEPVASLDPKTARQVMDLLRRiAREDGItVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
492-695 |
1.45e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.63 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqdleeiRKITGVCPQ---FNVQF 568
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVPQrrsIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 569 DIlTVKE--NLSLFAKIKGIHL--KEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTG 644
Cdd:cd03235 84 PI-SVRDvvLMGLYGHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27436953 645 LDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRkVIMSNGRLKCAG 695
Cdd:cd03235 163 VDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1277-1490 |
1.55e-29 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 117.96 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1277 IIASCLHKEYAGqkkscfsKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLG 1354
Cdd:cd03293 1 LEVRNVSKTYGG-------GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1355 HLGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLN-VPVQkLTAGITRKLCFVLSLLGNSPV 1433
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENaYPHQ-LSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1434 LLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMvSGR 1490
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-714 |
1.85e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdleeiRK 556
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVcPQ---FNVQFDIlTVKE--------NLSLFAKIKgihlKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF 625
Cdd:COG1121 77 IGYV-PQraeVDWDFPI-TVRDvvlmgrygRRGLFRRPS----RADREAVDEALERVGLEDLADRPIGELSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 626 GITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRkVIMSNGRLKCAG------SSM 698
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGppeevlTPE 229
|
250
....*....|....*.
gi 27436953 699 FLKRRWGLGYHLSLHR 714
Cdd:COG1121 230 NLSRAYGGPVALLAHG 245
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
507-695 |
4.75e-29 |
|
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: 116.44 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 507 GQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRKITGVCPQFNVqFDILTVKENLSLfAKIKGI 586
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNL-FAHLTVEQNVGL-GLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 587 HLKEVEQE-VQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH- 664
Cdd:cd03298 100 KLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETk 179
|
170 180 190
....*....|....*....|....*....|..
gi 27436953 665 -VILFSTQSMDEADILADRKVIMSNGRLKCAG 695
Cdd:cd03298 180 mTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1297-1496 |
6.50e-29 |
|
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: 117.07 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLG---------HLGYCPQENVLWP 1367
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD--LAslsrrelarRIAYVPQEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLRE--------HLevyAAVKGLRKADaRLAIARLVSAFKLHEQLNVPVQKLTAG------ITRklcfvlSLLGNSPV 1433
Cdd:COG1120 89 GLTVRElvalgrypHL---GLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGerqrvlIAR------ALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1434 LLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1293-1498 |
6.52e-29 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 116.28 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1293 CFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQEnvl 1365
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlRELRRKVGLVFQN--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1366 wP-----MLTLREhlEV-YAAV-KGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCF--VLSLlgNSPVLLL 1436
Cdd:COG1122 84 -PddqlfAPTVEE--DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1437 DEPSTGIDPTGQQQMWQAIQAVvKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1498
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
477-696 |
7.17e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.78 E-value: 7.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRK 556
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRERR--ADHVILFSTQSMDEAdILADRKVIMSNGRLKCAGS 696
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1302-1502 |
8.43e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 116.38 E-value: 8.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGH---------LGYCPQENVLWPMLTLR 1372
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG-EDITGLppheiarlgIGRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVyAAVKGLR-----------KADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPST 1441
Cdd:cd03219 94 ENVMV-AAQARTGsglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 1442 GIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1502
Cdd:cd03219 173 GLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1305-1495 |
9.02e-29 |
|
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: 115.47 E-value: 9.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVqEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC---SSVLG--------HLGYCPQENVLWPMLTLRE 1373
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKinlppqqrKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HLEVyaAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQ 1453
Cdd:cd03297 95 NLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 1454 AIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1302-1491 |
9.09e-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: 117.06 E-value: 9.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG-------HLG----YcpQENVLWPMLT 1370
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG-RDITGlpphriaRLGiartF--QNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHLEV----------YAAVKGLRKADARLAIAR-----LVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLL 1435
Cdd:COG0411 96 VLENVLVaaharlgrglLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1436 LDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
430-696 |
9.88e-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: 123.33 E-value: 9.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 430 SPLFFL---NSSSCFqHQRTN----AKVIEKEIDAEHPSDDYFEPVAPeFQGKEAIRIRNVKKEYkgkSGKVEALKGLLF 502
Cdd:COG4988 284 APEFFLplrDLGSFY-HARANgiaaAEKIFALLDAPEPAAPAGTAPLP-AAGPPSIELEDVSFSY---PGGRPALDGLSL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 503 DIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDiLTVKENLSLFAK 582
Cdd:COG4988 359 TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL-DPASWRRQIAWVPQNPYLFA-GTIRENLRLGRP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 583 -------IKGIHLKEVEQEVQRILLELDMQnIQDNlAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWS 655
Cdd:COG4988 437 dasdeelEAALEAAGLDEFVAALPDGLDTP-LGEG-GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ 514
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 27436953 656 LLRERRADHVILFSTQSMDEADiLADRKVIMSNGRLKCAGS 696
Cdd:COG4988 515 ALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGT 554
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
482-691 |
1.19e-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: 115.45 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 482 NVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLsVP----TEGSVTIYNKNLSEmqdlEEIRKI 557
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEgggtTSGQILFNGQPRKP----DQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKI-------KGIHLKEVEQEVqriLLELDMQNIQDNLAKHLSEGQKRKLTFGITIL 630
Cdd:cd03234 83 VAYVRQDDILLPGLTVRETLTYTAILrlprkssDAIRKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQlaRRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
478-691 |
1.23e-28 |
|
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: 115.04 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsEMQDLE-EIRK 556
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPpKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQIL 636
Cdd:cd03301 74 IAMVFQNYAL-YPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 637 LLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1300-1495 |
1.30e-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: 114.94 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLGHLGYCPQ-ENVLW--P------- 1367
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkpLEKERKRIGYVPQrRSIDRdfPisvrdvv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLEVYAAVKGLRKADARLAIARlVSAFKLHEQlnvPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1447
Cdd:cd03235 92 LMGLYGHKGLFRRLSKADKAKVDEALER-VGLSELADR---QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27436953 1448 QQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVaIMVSGRLRCIG 1495
Cdd:cd03235 168 QEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
478-691 |
1.78e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 116.72 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS-EMQDLEEIRK 556
Cdd:PRK13639 2 LETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:PRK13639 79 TVGIVFQNpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
477-696 |
1.82e-28 |
|
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: 115.51 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEiRK 556
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-PVQE-RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ItGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRI---LLEL-DMQNIQDNLAKHLSEGQKRKLTFGITILGD 632
Cdd:cd03296 76 V-GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKvheLLKLvQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 633 PQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1296-1490 |
1.85e-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: 114.49 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1296 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------SVLGHLGYCPQEnvlwP- 1367
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkELRRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 ----MLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGI 1443
Cdd:cd03225 86 dqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27436953 1444 DPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:cd03225 166 DPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
477-691 |
2.52e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNlsemqdleeirk 556
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQ-------FnvQ----FDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQK----- 620
Cdd:COG3842 69 VTGLPPEkrnvgmvF--QdyalFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrval 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 621 -RKLTFgitilgDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:COG3842 147 aRALAP------EPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
473-691 |
2.55e-28 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 116.20 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 473 QGKEAIRIR---NVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM- 548
Cdd:cd03294 13 NPQKAFKLLakgKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMs 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 549 -QDLEEIR--KITGVCPQFNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF 625
Cdd:cd03294 93 rKELRELRrkKISMVFQSFAL-LPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 626 GITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1294-1491 |
3.15e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 114.53 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG-----------HLGYCPQ 1361
Cdd:cd03257 11 FPTGGGSVKAlDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDG-KDLLKlsrrlrkirrkEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1362 E--NVLWPMLTLREHL-EVYAAVKGLRKADARLAIARLV-SAFKLHEQL--NVPVQkLTAGITRKLCFVLSLLGNSPVLL 1435
Cdd:cd03257 90 DpmSSLNPRMTIGEQIaEPLRIHGKLSKKEARKEAVLLLlVGVGLPEEVlnRYPHE-LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1436 LDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
479-692 |
6.51e-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: 112.74 E-value: 6.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 479 RIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmqdlEEIRKIT 558
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 559 GVCPQfNVQFDIL--TVKENLSLFAKIKGihlkEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQIL 636
Cdd:cd03226 74 GYVMQ-DVDYQLFtdSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 637 LLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLK 692
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
479-695 |
7.81e-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: 111.76 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 479 RIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKIT 558
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-SPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 559 GVCPQFNVQFDILtvkenlslfakikgiHLKEveqevqRILLEldmqniqdnlakhLSEGQKRKLTFGITILGDPQILLL 638
Cdd:cd03214 76 AYVPQALELLGLA---------------HLAD------RPFNE-------------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 639 DEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAG 695
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
478-696 |
7.82e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.14 E-value: 7.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEY-KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ-DLEEIR 555
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRI--LLELDMQNIQDNLAKHLSEGQKRKLTFGITILGD 632
Cdd:PRK13637 83 KKVGLVFQYpEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 633 PQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1282-1491 |
8.87e-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: 112.97 E-value: 8.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1282 LHKEYAGQKKscfskrkKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLG------ 1354
Cdd:cd03255 6 LSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiSKLSekelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1355 ----HLGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAG------ITRklcfv 1424
Cdd:cd03255 79 frrrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGqqqrvaIAR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1425 lSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLaEAEALCDRVAIMVSGRL 1491
Cdd:cd03255 154 -ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1274-1490 |
1.76e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 113.26 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1274 KPVIIASCLHKEYAgqkkscfSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVL 1353
Cdd:COG1116 5 APALELRGVSKRFP-------TGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1354 G---HLGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNV-PVQ-----KLTAGITRklcfv 1424
Cdd:COG1116 77 GpgpDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAyPHQlsggmRQRVAIAR----- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1425 lSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMvSGR 1490
Cdd:COG1116 152 -ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL-SAR 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
475-695 |
1.93e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 475 KEAIRIRNVKKEYKGKSGKveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEI 554
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE-ETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 RKITGVCPQfNV--QFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGD 632
Cdd:PRK13635 80 RRQVGMVFQ-NPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 633 PQILLLDEPTTGLDPFSRDQVWSLLRERRADHVI--LFSTQSMDEAdILADRKVIMSNGRLKCAG 695
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGItvLSITHDLDEA-AQADRVIVMNKGEILEEG 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
477-691 |
2.71e-27 |
|
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: 111.53 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKsgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 556
Cdd:cd03245 2 RIEFRNVSFSYPNQ--EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQfNVQFDILTVKENLSLFAkikgihlkeVEQEVQRILLELDMQNIQDNLAKH--------------LSEGQKRK 622
Cdd:cd03245 79 NIGYVPQ-DVTLFYGTLRDNITLGA---------PLADDERILRAAELAGVTDFVNKHpngldlqigergrgLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 623 LTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFST--QSMDEadiLADRKVIMSNGRL 691
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIThrPSLLD---LVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
478-712 |
4.81e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.95 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEY-KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSV-----TIYNKnlSEMQDL 551
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvddiTITHK--TKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 552 EEIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDM-QNIQDNLAKHLSEGQKRKLTFgITI 629
Cdd:PRK13646 81 RPVRKRIGMVFQFpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAI-VSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 630 LG-DPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRL--KCAGSSMFLKRRW 704
Cdd:PRK13646 160 LAmNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKK 239
|
....*...
gi 27436953 705 GLGYHLSL 712
Cdd:PRK13646 240 LADWHIGL 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1297-1479 |
5.36e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 110.35 E-value: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLG----YCPQENVLWPMLTLR 1372
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKGlrkaDARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1452
Cdd:PRK13539 92 ENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170 180 190
....*....|....*....|....*....|..
gi 27436953 1453 QAIQAvvkNTERG--VLLTTHN---LAEAEAL 1479
Cdd:PRK13539 168 ELIRA---HLAQGgiVIAATHIplgLPGAREL 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
478-696 |
1.04e-26 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 110.02 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNlsemqdleeirkI 557
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD------------I 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCP---QFNVQFDI------LTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIT 628
Cdd:cd03300 65 TNLPPhkrPVNTVFQNyalfphLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
479-691 |
1.33e-26 |
|
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: 110.51 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 479 RIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDleeiRKIT 558
Cdd:COG0411 6 EVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP----HRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 559 --GVCPQF-NVQ-FDILTVKENL----------SLFAKIKGI-----HLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQ 619
Cdd:COG0411 78 rlGIARTFqNPRlFPELTVLENVlvaaharlgrGLLAALLRLprarrEEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 620 KRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH---VILFstqsmdEADI-----LADRKVIMSNGRL 691
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgitILLI------EHDMdlvmgLADRIVVLDFGRV 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
477-691 |
1.34e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 110.10 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI------YNKNLSEMQD 550
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 551 LEEIRKITGVCPQFNVqFDILTVKENLsLFAKIK--GIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIT 628
Cdd:COG4161 78 RLLRQKVGMVFQQYNL-WPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRA---DHVILfsTQSMDEADILADRKVIMSNGRL 691
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIV--THEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
492-676 |
1.73e-26 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 108.28 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS-EMQDLEEIRKITGVCPQfNVQFDI 570
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDySRKGLLERRQRVGLVFQ-DPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 571 L--TVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPF 648
Cdd:TIGR01166 82 FaaDVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180 190
....*....|....*....|....*....|
gi 27436953 649 SRDQVWSLLRERRAD--HVIlFSTQSMDEA 676
Cdd:TIGR01166 162 GREQMLAILRRLRAEgmTVV-ISTHDVDLA 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
492-697 |
2.14e-26 |
|
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: 109.30 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEI-RKitGV--CPQF-NVq 567
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIaRL--GIgyVPEGrRI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 568 FDILTVKENLSLFAKIKGIHlKEVEQEVQRILlEL-----DMQNiqdNLAKHLSEGQKRKLTFGITILGDPQILLLDEPT 642
Cdd:COG0410 90 FPSLTVEENLLLGAYARRDR-AEVRADLERVY-ELfprlkERRR---QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 643 TGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGSS 697
Cdd:COG0410 165 LGLAPLIVEEIFEIIRRLNREGVtILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
495-714 |
2.20e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.71 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 495 EALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS-EMQDLEEIRKITGVCPQF-NVQFDILT 572
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLRESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 573 VKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQ 652
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 653 VWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAG--SSMFLKRRWGLGYHLSLHR 714
Cdd:PRK13636 180 IMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLRLPR 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
478-691 |
2.63e-26 |
|
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: 108.77 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEY------------------KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT 539
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 540 IYNKnlsemqdleeirkitgVCP--QFNVQFD-ILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLS 616
Cdd:cd03220 81 VRGR----------------VSSllGLGGGFNpELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 617 EGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVIL-FSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTViLVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
478-691 |
3.20e-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: 106.36 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsemqdleeirki 557
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 tgvcpqfnvQFDILTVKEnlslfAKIKGIHLkeVEQevqrilleldmqniqdnlakhLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03216 63 ---------EVSFASPRD-----ARRAGIAM--VYQ---------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
492-700 |
4.25e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.09 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS-----VPTEGSVTIYNKNL-SEMQDLEEIRKITGVCPQFN 565
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSIVYNGHNIySPRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 566 VQFDiLTVKENLSLFAKIKGIHLKEV-EQEVQRILLELDMQN-IQDNL---AKHLSEGQKRKLTFGITILGDPQILLLDE 640
Cdd:PRK14239 96 NPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDeVKDRLhdsALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 641 PTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS--SMFL 700
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDtkQMFM 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
478-697 |
6.26e-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: 108.01 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGSS 697
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
478-690 |
6.41e-26 |
|
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: 108.04 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEIR 555
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQfnvQFDI---LTVKEN-----LSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNL---AKHLSEGQKRKLt 624
Cdd:cd03256 78 RQIGMIFQ---QFNLierLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAyqrADQLSGGQQQRV- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 625 fGI--TILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGR 690
Cdd:cd03256 154 -AIarALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
478-647 |
6.54e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 108.16 E-value: 6.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM-QDLEEIRK 556
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITG-VCPQFNVqFDILTVKENLSLfA--KIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQK------RKLTFgi 627
Cdd:COG1126 78 KVGmVFQQFNL-FPHLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQqrvaiaRALAM-- 153
|
170 180
....*....|....*....|
gi 27436953 628 tilgDPQILLLDEPTTGLDP 647
Cdd:COG1126 154 ----EPKVMLFDEPTSALDP 169
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
476-695 |
7.95e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 108.25 E-value: 7.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 476 EAIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEG-SVTIYNKNLSEMqDLEEI 554
Cdd:COG1119 2 PLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGE-DVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 RKITG-VCPQFNVQFDI-LTVKEN-LS-LFAKIkGIHLK---EVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGI 627
Cdd:COG1119 77 RKRIGlVSPALQLRFPRdETVLDVvLSgFFDSI-GLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 628 TILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEadILA--DRKVIMSNGRLKCAG 695
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
469-691 |
1.04e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.20 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 469 APEFQGKEAIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS--VP---TEGSVTIYNK 543
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 544 NLSEMQ-DLEEIRKITGVCPQ----FNvqfdiLTVKENLSLFAKIKGIHLK-EVEQEVQRILLELDMQN-IQDNL---AK 613
Cdd:COG1117 79 DIYDPDvDVVELRRRVGMVFQkpnpFP-----KSIYDNVAYGLRLHGIKSKsELDEIVEESLRKAALWDeVKDRLkksAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 614 HLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
477-691 |
2.75e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK--NLSEMQDLEEI 554
Cdd:PRK11124 2 SIQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 R----KITGVCPQFNVqFDILTVKENLsLFA--KIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIT 628
Cdd:PRK11124 78 RelrrNVGMVFQQYNL-WPHLTVQQNL-IEApcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH---VILfsTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGitqVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
478-712 |
3.20e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.41 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSG-KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS---EMQDLEE 553
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 554 IRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQniQDNLAK---HLSEGQKRKLTFGITI 629
Cdd:PRK13634 83 LRKKVGIVFQFpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP--EELLARspfELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 630 LGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS--SMFLKRRWG 705
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPDEL 240
|
....*..
gi 27436953 706 LGYHLSL 712
Cdd:PRK13634 241 EAIGLDL 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1274-1500 |
3.38e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.92 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1274 KPVIIASCLHKEYAGQKKScfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTA---GEVELKGCS 1350
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP---------AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1351 ------SVLG-HLGYCPQEnvlwPM-----LTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGIT 1418
Cdd:COG1123 73 llelseALRGrRIGMVFQD----PMtqlnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1419 RKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1498
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
..
gi 27436953 1499 HL 1500
Cdd:COG1123 229 EI 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
502-695 |
3.85e-25 |
|
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: 105.07 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIyEGQITAILGHSGAGKSSLLNILNGLSVPTEGSV----TIY-----NKNLSEMQdleeiRKItGVCPQFNVQFDILT 572
Cdd:cd03297 19 FDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLfdsrkKINLPPQQ-----RKI-GLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 573 VKENLsLFAkIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQ 652
Cdd:cd03297 92 VRENL-AFG-LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 653 VWSLLRERRADHVI--LFSTQSMDEADILADRKVIMSNGRLKCAG 695
Cdd:cd03297 170 LLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
478-696 |
4.85e-25 |
|
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: 104.88 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 557
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDiLTVKENLSLFAK---------IKGIHLKEVeqeVQRILLELDMQnIQDNlAKHLSEGQKRKLTFGIT 628
Cdd:cd03244 80 ISIIPQDPVLFS-GTIRSNLDPFGEysdeelwqaLERVGLKEF---VESLPGGLDTV-VEEG-GENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEadIL-ADRKVIMSNGRLKCAGS 696
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDT--IIdSDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
477-711 |
5.25e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYK-GKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM---QDLE 552
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 553 EIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELdmqNIQDNLAKH----LSEGQKRKLTFGI 627
Cdd:PRK13641 82 KLRKKVSLVFQFpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV---GLSEDLISKspfeLSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 628 TILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRL--KCAGSSMFLKRRW 704
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEW 238
|
....*..
gi 27436953 705 GLGYHLS 711
Cdd:PRK13641 239 LKKHYLD 245
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
478-691 |
5.81e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 105.35 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:PRK11614 6 LSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLfakikGIHLKEVEQEVQRI---------LLELDMQNiqdnlAKHLSEGQKRKLTFGIT 628
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFQERIkwvyelfprLHERRIQR-----AGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFST-QSMDEADILADRKVIMSNGRL 691
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENGHV 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1272-1500 |
6.46e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.15 E-value: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1272 DEKPVIIASCLHKEYAGqkkscfSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--- 1348
Cdd:COG1123 256 AAEPLLEVRNLSKRYPV------RGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1349 -------CSSVLGHLGYCPQ--ENVLWPMLTLREHL-EVYAAVKGLRKADARLAIARLVSAFKLHEQ-LNVPV------Q 1411
Cdd:COG1123 330 tklsrrsLRELRRRVQMVFQdpYSSLNPRMTVGDIIaEPLRLHGLLSRAERRERVAELLERVGLPPDlADRYPhelsggQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1412 KLTAGITRklcfVLSLlgNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG1123 410 RQRVAIAR----ALAL--EPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
....*....
gi 27436953 1492 RCIGSIQHL 1500
Cdd:COG1123 484 VEDGPTEEV 492
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
477-705 |
6.47e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.91 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEirk 556
Cdd:NF033858 1 VARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 itgVCPQF---------NVQFDiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGI 627
Cdd:NF033858 74 ---VCPRIaympqglgkNLYPT-LSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 628 TILGDPQILLLDEPTTGLDPFSRDQVWSL---LRERRADHVILFSTQSMDEADILaDRKVIMSNGRLKCAGSSMFLKRRW 704
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELidrIRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLART 228
|
.
gi 27436953 705 G 705
Cdd:NF033858 229 G 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
478-691 |
6.71e-25 |
|
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: 105.46 E-value: 6.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQ--DLEEIR 555
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITG-VCPQFNVqFDILTVKEN-----LSLFAKIKGIHLKEVEQEVQRILLELDMQNIQD---NLAKHLSEGQKRKLTFG 626
Cdd:TIGR02315 79 RRIGmIFQHYNL-IERLTVLENvlhgrLGYKPTWRSLLGRFSEEDKERALSALERVGLADkayQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 627 ITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
477-696 |
7.47e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 7.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYK-GKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYN---KNLSEMQDLE 552
Cdd:PRK13649 2 GINLQNVSYTYQaGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtliTSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 553 EIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRillELDMQNIQDNLAK----HLSEGQKRKLTFGI 627
Cdd:PRK13649 82 QIRKKVGLVFQFpESQLFEETVLKDVAFGPQNFGVSQEEAEALARE---KLALVGISESLFEknpfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 628 TILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
478-695 |
8.08e-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: 103.16 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDleEIRKI 557
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQfnvqfdiltvkeNLSLFAkikgihlkeveqevqrilleldmQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03247 77 ISVLNQ------------RPYLFD-----------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHVILFST---QSMDEadilADRKVIMSNGRLKCAG 695
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWIThhlTGIEH----MDKILFLENGKIIMQG 178
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-763 |
9.73e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.10 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYK------GKSG-----------KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT 539
Cdd:COG4586 1 IIEVENLSKTYRvyekepGLKGalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 540 IYNKNLSEmQDLEEIRKITGVCPQFNvQ--FDiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSE 617
Cdd:COG4586 81 VLGYVPFK-RRKEFARRIGVVFGQRS-QlwWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 618 GQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH---VILfsTqSMDEADI--LADRKVIMSNGRLK 692
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgttILL--T-SHDMDDIeaLCDRVIVIDHGRII 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 693 CAGSSMFLKRRWGLGYHLSLHRNEICNPEQITSFIthhipdaklKTENKEKLVYTLPLERTNTFPDLFSDL 763
Cdd:COG4586 235 YDGSLEELKERFGPYKTIVLELAEPVPPLELPRGG---------EVIEREGNRVRLEVDPRESLAEVLARL 296
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
474-696 |
1.19e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 474 GKEAIRIRNVKKEYKGKSGKVE--ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDL 551
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 552 EEIRKITGVCPQfN---------VQFDILTVKENLslfakikGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRK 622
Cdd:PRK13633 81 WDIRNKAGMVFQ-NpdnqivatiVEEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 623 LTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEAdILADRKVIMSNGRLKCAGS 696
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
496-696 |
1.20e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 104.81 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 496 ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRkiTGVCPQF---NVqFDILT 572
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIAR--LGIGRKFqkpTV-FEELT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 573 VKENL------------SLFAKIKGihlkEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDE 640
Cdd:COG4674 102 VFENLelalkgdrgvfaSLFARLTA----EERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 641 PTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:COG4674 178 PVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1295-1496 |
1.98e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG------HLGYCPQENVLWP 1367
Cdd:COG3842 12 SKRyGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG-RDVTGlppekrNVGMVFQDYALFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAG------ITRKLcfVlsllgNSP-VLLLDEPS 1440
Cdd:COG3842 91 HLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvaLARAL--A-----PEPrVLLLDEPL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1441 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:COG3842 164 SALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1290-1509 |
2.37e-24 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 104.65 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1290 KKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------------------CSS 1351
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkkISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1352 VLGHLGYCPQENVLwpmltlrEHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNS 1431
Cdd:cd03294 107 VFQSFALLPHRTVL-------ENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1432 PVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYI 1509
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYV 257
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1299-1495 |
3.23e-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: 101.36 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1299 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------SVLGHLGYCPQenvlwpmltl 1371
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkELARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 rehlevyaavkglrkADARLAIARLvsAFKlheqlnvPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQM 1451
Cdd:cd03214 81 ---------------ALELLGLAHL--ADR-------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 1452 WQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
478-696 |
3.41e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 557
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQfNVQFDIL--TVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:PRK13652 80 VGLVFQ-NPDDQIFspTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
478-690 |
3.99e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKE-YKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRK 556
Cdd:COG1101 2 LELKNLSKTfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 I--------TGVCPQfnvqfdiLTVKENLSLFA---KIKGIHL---KEVEQEVQRIL--LELDMQNIQDNLAKHLSEGQK 620
Cdd:COG1101 82 IgrvfqdpmMGTAPS-------MTIEENLALAYrrgKRRGLRRgltKKRRELFRELLatLGLGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 621 RKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVI--LFSTQSMDEADILADRKVIMSNGR 690
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLttLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
478-692 |
4.01e-24 |
|
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: 102.48 E-value: 4.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 557
Cdd:TIGR03740 1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVqfdiLTVKENLSLFAKIKGIHlkevEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:TIGR03740 76 IESPPLYEN----LTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRLK 692
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
478-691 |
1.07e-23 |
|
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: 100.95 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD--LEEIR 555
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1302-1491 |
1.26e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.04 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcssvlghlgycpqenvlwpmltlrehlevyAAV 1381
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------------------KEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1382 KGLRKADARLAIARLVSafklheQLNVPVQKLTAgITRklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKN 1461
Cdd:cd03216 65 SFASPRDARRAGIAMVY------QLSVGERQMVE-IAR------ALARNARLLILDEPTAALTPAEVERLFKVIRR-LRA 130
|
170 180 190
....*....|....*....|....*....|
gi 27436953 1462 TERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03216 131 QGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
478-695 |
2.61e-23 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 100.49 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkveaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdlEEIRKI 557
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP--PEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 tGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03299 74 -SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAG 695
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
477-696 |
4.21e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.03 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVP---TEGSVTIYNKNLSEmQDLEE 553
Cdd:PRK13640 5 IVEFKHVSFTYP--DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTA-KTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 554 IRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF-GITILG 631
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIaGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 632 dPQILLLDEPTTGLDPFSRDQVWSLLRERRAD-HVILFS-TQSMDEADiLADRKVIMSNGRLKCAGS 696
Cdd:PRK13640 162 -PKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1305-1483 |
4.53e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 100.19 E-value: 4.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQENVLWPMLTLRehLEVYAAVK-G 1383
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI----GYVPQKLYLDTTLPLT--VNRFLRLRpG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1384 LRKADARLAIARlVSAFKLHEQlnvPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTE 1463
Cdd:PRK09544 96 TKKEDILPALKR-VQAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELD 171
|
170 180
....*....|....*....|
gi 27436953 1464 RGVLLTTHNLAEAEALCDRV 1483
Cdd:PRK09544 172 CAVLMVSHDLHLVMAKTDEV 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1294-1491 |
6.36e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 98.01 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTA--GEVELKGCSSVL----GHLGYCPQENVLWP 1367
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKrsfrKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLEVYAAVKGL----RKadaRLAIArlvsafklheqlnvpvqkltagitrklcfvLSLLGNSPVLLLDEPSTGI 1443
Cdd:cd03213 96 TLTVRETLMFAAKLRGLsggeRK---RVSIA------------------------------LELVSNPSLLFLDEPTSGL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27436953 1444 DPTGQQQMWQAIQAVVkNTERGVLLTTHNL-AEAEALCDRVAIMVSGRL 1491
Cdd:cd03213 143 DSSSALQVMSLLRRLA-DTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
484-690 |
9.52e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 105.13 E-value: 9.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 484 KKEYKGKSGKVEALKGLLFDI----YEGQITAILGHSGAGKSSLLNILNGLS---VPTEGSVTIYNKNLsemqDLEEIRK 556
Cdd:TIGR00955 24 VSRLRGCFCRERPRKHLLKNVsgvaKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPI----DAKEMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFNVQFDILTVKENLSLFAKIK---GIHLKEVEQEVQRILLELDMQNIQD------NLAKHLSEGQKRKLTFGI 627
Cdd:TIGR00955 100 ISAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 628 TILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGR 690
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlaQKGKTIICTIHQPSSELFELFDKIILMAEGR 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
478-695 |
1.17e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.10 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENL----SLFAKIKGIHL---KEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITIL 630
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigrHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRERRAD-HVILFSTQSMDEADILADRKVIMSNGRLKCAG 695
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1304-1490 |
1.45e-22 |
|
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: 96.30 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMlTLREHLe 1376
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldLESLRKNIAYVPQDPFLFSG-TIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 vyaavkgL----RKadaRLAIARlvsafklheqlnvpvqkltagitrklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQMW 1452
Cdd:cd03228 97 -------LsggqRQ---RIAIAR------------------------------ALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 27436953 1453 QAIQAVVKntERGVLLTTHNLAEAEaLCDRVAIMVSGR 1490
Cdd:cd03228 137 EALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
478-689 |
1.58e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.06 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtIYNKNLSEMQDLEEIRKI 557
Cdd:PRK13648 8 IVFKNVSFQYQSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVC---P--QF---NVQFDILTVKENLSlfakikgIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITI 629
Cdd:PRK13648 85 IGIVfqnPdnQFvgsIVKYDVAFGLENHA-------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 630 LGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEAdILADRKVIMSNG 689
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKG 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
476-696 |
2.38e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.84 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 476 EAIRIRNVKKEY------------------KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGS 537
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 538 VTIyNKNLSEMqdLEeirkitgvcpqFNVQFD-ILTVKENLSLFAKIKGIHLKEVEQEVQRIL----LE--LDMQniqdn 610
Cdd:COG1134 83 VEV-NGRVSAL--LE-----------LGAGFHpELTGRENIYLNGRLLGLSRKEIDEKFDEIVefaeLGdfIDQP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 611 lAKHLSEGQKRKLTFGITILGDPQILLLDEPT-TGlDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSN 688
Cdd:COG1134 144 -VKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESGRtVIFVSHSMGAVRRLCDRAIWLEK 221
|
....*...
gi 27436953 689 GRLKCAGS 696
Cdd:COG1134 222 GRLVMDGD 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
478-696 |
3.65e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEAdILADRKVIMSNGRLKCAGS 696
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1300-1496 |
4.04e-22 |
|
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: 96.92 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGHLGYCPQENVLWPMLTLREHLEVYA 1379
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-KDITNLPPHKRPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1380 AV------KGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQ 1453
Cdd:cd03300 92 NIafglrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 1454 AIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:cd03300 172 ELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1304-1471 |
4.46e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGHLGYCPQENVLW--------PMLTLREHL 1375
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG--EPIRRQRDEYHQDLLYlghqpgikTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 EVYAAVKGLRKADARLAIARLVSafkLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1455
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEALAQVG---LAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*...
gi 27436953 1456 QAvvkNTERG--VLLTTH 1471
Cdd:PRK13538 173 AQ---HAEQGgmVILTTH 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
497-689 |
5.46e-22 |
|
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: 96.38 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIynknlsemqdleEIRKITGVCPQFNVQFD------I 570
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL------------EGKQITEPGPDRMVVFQnysllpW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 571 LTVKENLSLFAKIKGIHLKEVEQE--VQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPF 648
Cdd:TIGR01184 69 LTVRENIALAVDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 649 SRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNG 689
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
444-691 |
6.19e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 102.17 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 444 QRTNAKV--IEKEIDAEHPSDDYFEPVAPEfQGKEAIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKS 521
Cdd:COG1132 305 QRALASAerIFELLDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKS 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 522 SLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDiLTVKENLSLFAkiKGIHLKEVEQ-----EVQ 596
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIDGVDIRDL-TLESLRRQIGVVPQDTFLFS-GTIRENIRYGR--PDATDEEVEEaakaaQAH 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 597 RILLELDMQ---NIQDNLAKhLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH-VIL----F 668
Cdd:COG1132 457 EFIEALPDGydtVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRtTIViahrL 535
|
250 260
....*....|....*....|....
gi 27436953 669 STqsmdeadIL-ADRKVIMSNGRL 691
Cdd:COG1132 536 ST-------IRnADRILVLDDGRI 552
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1276-1496 |
1.19e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.73 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1276 VIIASCLHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL--KGCSSVL 1353
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddEDISLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1354 GH------LGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIA-RLVSAFKLHEQLNVPVQKLTAGITRKLCFVLS 1426
Cdd:PRK10895 72 LHararrgIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAnELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1427 LLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
476-696 |
1.30e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.99 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 476 EAIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdLEEIR 555
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQ-FNVQFDiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQK------RKLTFGIT 628
Cdd:PRK13548 76 RRRAVLPQhSSLSFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRE---RRADHVILfstqsmdeadIL---------ADRKVIMSNGRLKCAGS 696
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLARQlahERGLAVIV----------VLhdlnlaaryADRIVLLHQGRLVADGT 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-681 |
1.34e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS-----VPTEGSVTIYNKNLSEMQ-D 550
Cdd:PRK14258 7 AIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERRvN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 551 LEEIRK-ITGVCPQFNVqFDiLTVKENLSLFAKIKGIHLK-EVEQEVQRILLELDM-QNIQDNLAK---HLSEGQKRKLT 624
Cdd:PRK14258 83 LNRLRRqVSMVHPKPNL-FP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwDEIKHKIHKsalDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 625 FGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRER--RADHVILFSTQSMDEADILAD 681
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSD 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
502-696 |
1.38e-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: 98.25 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLsemQDLE-------EIRKItGVCPQfnvQ---FDIL 571
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL---QDSArgiflppHRRRI-GYVFQ---EarlFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 TVKENLsLFAkikgihLKEVEQEVQRILLE--LDMQNIQDNLAK---HLSEGQKRKLTFGITILGDPQILLLDEPTTGLD 646
Cdd:COG4148 93 SVRGNL-LYG------RKRAPRAERRISFDevVELLGIGHLLDRrpaTLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 647 PFSRDQVWSLLrERRADHV---ILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:COG4148 166 LARKAEILPYL-ERLRDELdipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1302-1491 |
1.47e-21 |
|
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: 94.96 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVL-GHLGYCPQENVLWpMLTLREH 1374
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpADLrRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 LevyaAVKGLRKADAR-LAIARL--VSAF-KLHEQ-LNVPV----------QKLTAGITRklcfvlSLLGNSPVLLLDEP 1439
Cdd:cd03245 98 I----TLGAPLADDERiLRAAELagVTDFvNKHPNgLDLQIgergrglsggQRQAVALAR------ALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1440 STGIDPTGQQQMWQAIQAVVKntERGVLLTTHNLAeAEALCDRVAIMVSGRL 1491
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1295-1498 |
1.83e-21 |
|
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: 95.10 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-----CSSVLGHLGYCPQENVLWPML 1369
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnLPPEKRDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHLEVyaavkGLR-KADARLAIARLVS--AFKLH--EQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:cd03299 87 TVYKNIAY-----GLKkRKVDKKEIERKVLeiAEMLGidHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27436953 1445 PTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1498
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
473-691 |
4.32e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 99.11 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 473 QGKEAIRIRNVKKEYKG-KSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI-YNKNLSEMQD 550
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 551 LE-----EIRKITGVCPQFNVQFDILTVKENL----SL-----FAKIKGIH-LKEV---EQEVQRILleldmqniqDNLA 612
Cdd:TIGR03269 355 PGpdgrgRAKRYIGILHQEYDLYPHRTVLDNLteaiGLelpdeLARMKAVItLKMVgfdEEKAEEIL---------DKYP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 613 KHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVW-SLLRERRA-DHVILFSTQSMDEADILADRKVIMSNGR 690
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
.
gi 27436953 691 L 691
Cdd:TIGR03269 506 I 506
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1305-1500 |
4.51e-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: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlgHLGYCP---------QENVLWPMLTLREHL 1375
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD----LTALPPaerpvsmlfQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 EVyaavkGLRK-----ADARLAIARLVSAFKLHEQLN-VPV-----QKLTAGITRklCfvlsLLGNSPVLLLDEPSTGID 1444
Cdd:COG3840 93 GL-----GLRPglkltAEQRAQVEQALERVGLAGLLDrLPGqlsggQRQRVALAR--C----LVRKRPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1445 PTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
478-647 |
5.61e-21 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 93.44 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 557
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDIlTVKENLSLFakikgiHLKEVEQEVQRILLELDMQNIQDNL-----------AKHLSEGQKRKLTFG 626
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLpngydtvlgenGGNLSQGERQLLAIA 151
|
170 180
....*....|....*....|.
gi 27436953 627 ITILGDPQILLLDEPTTGLDP 647
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDT 172
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
477-691 |
7.78e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.66 E-value: 7.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI------YNKNLSEMQD 550
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 551 L-EEIRKITG-VCPQFNVqFDILTVKENLSLFAKI-KGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGI 627
Cdd:PRK11264 79 LiRQLRQHVGfVFQNFNL-FPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 628 TILGDPQILLLDEPTTGLDPFSRDQVWSLLR---ERRADHVILfsTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRqlaQEKRTMVIV--THEMSFARDVADRAIFMDQGRI 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
475-691 |
9.06e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 475 KEAIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL-----SVPTEGSVTIYNKNL-SEM 548
Cdd:PRK14267 2 KFAIETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIySPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 549 QDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKGI-----HLKE-VEQEVQRILLELDMQNIQDNLAKHLSEGQKRK 622
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkskkELDErVEWALKKAALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 623 LTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
477-691 |
1.01e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIynknlsemqDLEEIRk 556
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI---------DGKPVR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGvcPQ-------------FNVqFDILTVKENLSLFAKIKG---IHLKEVEQEVQRIL----LELDMqniqDNLAKHLS 616
Cdd:COG3845 71 IRS--PRdaialgigmvhqhFML-VPNLTVAENIVLGLEPTKggrLDRKAARARIRELSerygLDVDP----DAKVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 617 EGQKRKltfgITIL----GDPQILLLDEPTTGLDPFSRDQVWSLLRERRAD-HVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:COG3845 144 VGEQQR----VEILkalyRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
477-696 |
1.10e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.54 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRK 556
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ItGVCPQFNVQFDILTVKEN----LSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGD 632
Cdd:PRK10851 76 V-GFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 633 PQILLLDEPTTGLDPFSRDQVWSLLRERRAD--HVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
492-662 |
1.40e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNlsemQDLEEIR-KITGVCPQfNVQFDI 570
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAeACHYLGHR-NAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 571 LTVKENLSLFAKIKGIHLKEVEQEVQRIllelDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSR 650
Cdd:PRK13539 88 LTVAENLEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170
....*....|..
gi 27436953 651 DQVWSLLRERRA 662
Cdd:PRK13539 164 ALFAELIRAHLA 175
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1301-1491 |
3.50e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.25 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1301 IAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSV----------LGhLGYCPQENVLWPMLT 1370
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-KPVrirsprdaiaLG-IGMVHQHFMLVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHLeVYAAVKG----LRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPt 1446
Cdd:COG3845 97 VAENI-VLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27436953 1447 gqqqmwQAIQ---AVVKN-TERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG3845 175 ------QEADelfEILRRlAAEGksIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
479-691 |
3.55e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.13 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 479 RIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYnknlsemqdlEEIRKIT 558
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID----------GQEMRFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 559 GVCPQFNVQFDI----------LTVKENL---SLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTF 625
Cdd:PRK11288 72 STTAALAAGVAIiyqelhlvpeMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 626 GITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRAD-HVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
492-659 |
3.70e-20 |
|
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: 90.11 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDL--EEIRKI---TGVCPQfnv 566
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENILYLghlPGLKPE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 567 qfdiLTVKENLSLFAKIKGIHLKEVEQEvqriLLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLD 646
Cdd:TIGR01189 88 ----LSALENLHFWAAIHGGAQRTIEDA----LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170
....*....|...
gi 27436953 647 PFSRDQVWSLLRE 659
Cdd:TIGR01189 160 KAGVALLAGLLRA 172
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
445-658 |
4.17e-20 |
|
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: 96.28 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 445 RTNAKVIEKEIDAEHPSDDYFEPVA-PEFQGKEAIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSL 523
Cdd:TIGR02868 301 RAAAERIVEVLDAAGPVAEGSAPAAgAVGLGKPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 524 LNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDIlTVKENLsLFAKiKGIHLKEVEQEVQRILLELD 603
Cdd:TIGR02868 378 LATLAGLLDPLQGEVTLDGVPVSSL-DQDEVRRRVSVCAQDAHLFDT-TVRENL-RLAR-PDATDEELWAALERVGLADW 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 604 MQNIQDNL-------AKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLR 658
Cdd:TIGR02868 454 LRALPDGLdtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL 515
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
478-696 |
4.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:PRK13644 2 IRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQIL 636
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 637 LLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADIlADRKVIMSNGRLKCAGS 696
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
478-696 |
4.48e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.49 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSG-KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYN---KNLSEMQDLEE 553
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 554 IRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRillELDMQNIQDNLAK----HLSEGQKRKLTFGIT 628
Cdd:PRK13643 82 VRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEkspfELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
478-690 |
5.59e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.58 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkvealkgLLFD--IYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiR 555
Cdd:COG3840 2 LRLDDLTYRYGDFP--------LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCpQFNVQFDILTVKENLSLfakikGIH--LK---EVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITIL 630
Cdd:COG3840 72 PVSMLF-QENNLFPHLTVAQNIGL-----GLRpgLKltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGR 690
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
477-691 |
5.66e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM-------- 548
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsprdaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 549 ------QDLeeirkitGVCPQfnvqfdiLTVKENLSL---FAKIKGIHLKEVEQEVQRILLELDMqNIQ-DNLAKHLSEG 618
Cdd:COG1129 80 giaiihQEL-------NLVPN-------LSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 619 QK------RKLTFgitilgDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:COG1129 145 QQqlveiaRALSR------DARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
484-696 |
7.03e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.94 E-value: 7.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 484 KKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD--LEEIR--KITG 559
Cdd:PRK10070 31 KEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaeLREVRrkKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 560 VCPQFNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLD 639
Cdd:PRK10070 111 VFQSFAL-MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 640 EPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
478-691 |
7.39e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 7.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL-----SVPTEGSVTIYNKNLSEMqDLE 552
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-DVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 553 EIRKITGVCPQFNVQFDILTVKENLSLFAKIKGI--HLKEVEQEVQRIL----LELDMQNIQDNLAKHLSEGQKRKLTFG 626
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALekaqLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 627 ITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1295-1495 |
7.99e-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: 89.62 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------------CSSVLghlgycpQ 1361
Cdd:cd03301 7 TKRfGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrdIAMVF-------Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1362 ENVLWPMLTLREHLEVYAAVKGLRKA--DAR-LAIARLVsafKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDE 1438
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDeiDERvREVAELL---QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1439 PSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1306-1471 |
8.05e-20 |
|
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: 89.47 E-value: 8.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGHLGYCPQENVLW--------PMLTLREHLEV 1377
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG--GPLDFQRDSIARGLLYlghapgikTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 YAAVKGLRKADARLAIARLvSAFKlheqlNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1457
Cdd:cd03231 97 WHADHSDEQVEEALARVGL-NGFE-----DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
170
....*....|....*.
gi 27436953 1458 vvkNTERG--VLLTTH 1471
Cdd:cd03231 171 ---HCARGgmVVLTTH 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1268-1489 |
8.29e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.12 E-value: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1268 TSILDEKPVIIASCLHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELK 1347
Cdd:PRK15439 3 TSDTTAPPLLCARSISKQYSGVE-----------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1348 G-----CSSVLGH-LG-Y-CPQENVLWPMLTLREHLEVyaavkGL---RKADARLA--IARLVSAFKLHEQ---LNVPVQ 1411
Cdd:PRK15439 72 GnpcarLTPAKAHqLGiYlVPQEPLLFPNLSVKENILF-----GLpkrQASMQKMKqlLAALGCQLDLDSSagsLEVADR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1412 KLTAgITRklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSG 1489
Cdd:PRK15439 147 QIVE-ILR------GLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
478-699 |
8.42e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.31 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKgKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:PRK13642 5 LEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEAdILADRKVIMSNGRL--KCAGSSMF 699
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
477-686 |
1.05e-19 |
|
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: 95.05 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 556
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA-DADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFNVQFDIlTVKENLsLFAKiKGIHLKEVEQEVQRI-LLELDM---QNIQDNLAKH---LSEGQKRKLTFGITI 629
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENI-RLAR-PDASDAEIREALERAgLDEFVAalpQGLDTPIGEGgagLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 630 LGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSmDEADILADRKVIM 686
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
478-690 |
1.06e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRKI 557
Cdd:PRK11607 20 LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:PRK11607 94 NMMFQSYAL-FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 638 LDEPTTGLDPFSRD----QVWSLLRERRADHVILfsTQSMDEADILADRKVIMSNGR 690
Cdd:PRK11607 173 LDEPMGALDKKLRDrmqlEVVDILERVGVTCVMV--THDQEEAMTMAGRIAIMNRGK 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1304-1502 |
1.06e-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: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS----------SVLGHLGYCPQ-----------E 1362
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglsekelyELRRRIGMLFQggalfdsltvfE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1363 NVLWPmltLREH------------LEVYAAVkGLRKADA------------RLAIARlvsafklheqlnvpvqkltagit 1418
Cdd:COG1127 102 NVAFP---LREHtdlseaeirelvLEKLELV-GLPGAADkmpselsggmrkRVALAR----------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1419 rklcfvlSLLGNSPVLLLDEPSTGIDPtgqqQMWQAIQAVVK--NTERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCI 1494
Cdd:COG1127 155 -------ALALDPEILLYDEPTAGLDP----ITSAVIDELIRelRDELGltSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
....*...
gi 27436953 1495 GSIQHLKN 1502
Cdd:COG1127 224 GTPEELLA 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
478-691 |
1.22e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.79 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsEMQDLEEIRKI 557
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRlhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1304-1510 |
1.51e-19 |
|
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: 95.29 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQENVLWPMlTLREHL- 1375
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpASLRRQIGVVLQDVFLFSG-TIRENIt 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 ---------EVYAAvkglrkadARLA-IARLVSAfkLHEQLNVPV----QKLTAGITRKLCFVLSLLGNSPVLLLDEPST 1441
Cdd:COG2274 571 lgdpdatdeEIIEA--------ARLAgLHDFIEA--LPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1442 GIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYIL 1510
Cdd:COG2274 641 ALDAETEAIILENLRRLLKG--RTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
481-692 |
2.29e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.10 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 481 RNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLE--EIR-KI 557
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILaDRKVIMSNGRLK 692
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1302-1496 |
2.37e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.36 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLG--------HLGYCPQENVLWPMLTLRE 1373
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFtnlpprerRVGFVFQHYALFPHMTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNV-PVQkltagitrklcfvLS--------L---LGNSP-VLLLDEPS 1440
Cdd:COG1118 95 NIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRyPSQ-------------LSggqrqrvaLaraLAVEPeVLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1441 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1295-1496 |
2.41e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR-KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGHLGycPQE-NV-------- 1364
Cdd:COG3839 10 SKSyGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG--RDVTDLP--PKDrNIamvfqsya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1365 LWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAG----------ITRklcfvlsllgNSPVL 1434
Cdd:COG3839 86 LYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvalgraLVR----------EPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1435 LLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
474-795 |
2.43e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 91.72 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 474 GKEAIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAG--KSSLLNILNGlsvPTEGSVTIynKNLSEMQDL 551
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 552 EEIRKITGVC-PQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITIL 630
Cdd:NF000106 81 RALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRER-RADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSMFLKRRWGlGYH 709
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 710 LSLHRNEICNPEQITSFITHHIPDAKL-KTENKEKLVYTLPLERTNTFPDLFSDLdkcSDQG--VTGYDISMSTLNEVFM 786
Cdd:NF000106 240 LQIRPAHAAELDRMVGAIAQAGLDGIAgATADHEDGVVNVPIVSDEQLSAVVGML---GERGftISGHQHPSAQL*EVFL 316
|
....*....
gi 27436953 787 KLEGQSTIE 795
Cdd:NF000106 317 AITGQKTSE 325
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
481-646 |
2.73e-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: 87.68 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 481 RNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG--LSVPTEGSVTIYNKNLSemqdlEEIRKIT 558
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD-----KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 559 GVCPQFNVQFDILTVKENLSLFAKIKGihlkeveqevqrilleldmqniqdnlakhLSEGQKRKLTFGITILGDPQILLL 638
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFL 132
|
....*...
gi 27436953 639 DEPTTGLD 646
Cdd:cd03232 133 DEPTSGLD 140
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
478-722 |
3.41e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLL---NILNGL--SVPTEGSVTIYNKNLSEMQ-DL 551
Cdd:PRK14243 11 LRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLipGFRVEGKVTFHGKNLYAPDvDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 552 EEIRKITGVCPQFNVQFDiLTVKENLSLFAKIKGIH--LKE-VEQEVQRILLeldMQNIQDNL---AKHLSEGQKRKLTF 625
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFP-KSIYDNIAYGARINGYKgdMDElVERSLRQAAL---WDEVKDKLkqsGLSLSGGQQQRLCI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 626 GITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADrKVIMSNGRLKCAGSSMflkrrwg 705
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD-MTAFFNVELTEGGGRY------- 234
|
250
....*....|....*....
gi 27436953 706 lGYHLSLHRNEIC--NPEQ 722
Cdd:PRK14243 235 -GYLVEFDRTEKIfnSPQQ 252
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1302-1486 |
4.27e-19 |
|
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: 93.12 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMlTLREH 1374
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 LEVY---AAVKGLRKADARLAIARLVSAfkLHEQLNVPVQK----LTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1447
Cdd:TIGR02857 416 IRLArpdASDAEIREALERAGLDEFVAA--LPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 27436953 1448 QQQMWQAIQAVVKNteRGVLLTTHNLAEAEaLCDRVAIM 1486
Cdd:TIGR02857 494 EAEVLEALRALAQG--RTVLLVTHRLALAA-LADRIVVL 529
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
478-696 |
5.06e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSG-KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYN----KNLSEMQDLE 552
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 553 EIRKITGVCPQF-NVQFDILTVKENLSLfakiKGIHLKEVEQEVQRILLEL-DMQNIQDNLAK----HLSEGQKRKLTFG 626
Cdd:PRK13645 87 RLRKEIGLVFQFpEYQLFQETIEKDIAF----GPVNLGENKQEAYKKVPELlKLVQLPEDYVKrspfELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 627 ITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYkkRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1294-1496 |
5.25e-19 |
|
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: 88.13 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------SVLGHLGYCPQENVLW 1366
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDireqdpvELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1367 PMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQ--LNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:cd03295 88 PHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1445 PTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:cd03295 168 PITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1282-1500 |
5.63e-19 |
|
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: 87.64 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1282 LHKEYAGQKKscfskrkKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVL-------- 1353
Cdd:cd03258 7 VSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1354 --GHLGYCPQE-NVLWPmLTLREHLEVYAAVKGLRKADARLAIARLVSAFKL-HEQLNVPV-----QKLTAGITRKlcfv 1424
Cdd:cd03258 80 arRRIGMIFQHfNLLSS-RTVFENVALPLEIAGVPKAEIEERVLELLELVGLeDKADAYPAqlsggQKQRVGIARA---- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1425 lslLGNSP-VLLLDEPSTGIDPTGQQQMWQAIQAVvkNTERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:cd03258 155 ---LANNPkVLLCDEATSALDPETTQSILALLRDI--NRELGltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
474-691 |
7.71e-19 |
|
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: 85.95 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 474 GKEAIRIRNVkkeykgkSGKvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK-----NLSEM 548
Cdd:cd03215 1 GEPVLEVRGL-------SVK-GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 549 QDL------EEiRKITGVCPQFnvqfdilTVKENLSLfakikgihlkeveqevqrilleldmqniqdnlAKHLSEGQKRK 622
Cdd:cd03215 73 IRAgiayvpED-RKREGLVLDL-------SVAENIAL--------------------------------SSLLSGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 623 LTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQsMDEADILADRKVIMSNGRL 691
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGkaVLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1302-1505 |
1.01e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.79 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIrMISGITKPTAGE---------VELKGCSSVLGHlgYCPQENVLWPMLTLR 1372
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRrpwrf*twcANRRALRRTIG*--HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1452
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1453 QAIQAVVKNTERgVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLG 1505
Cdd:NF000106 185 DEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1304-1502 |
1.37e-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: 86.79 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHL----GYCPQ-----------E 1362
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglSEAELYRLrrrmGMLFQsgalfdsltvfE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1363 NVLWPmltLREHLEVYAAVkglrkadarlaIARLVsAFKLH-------EQLnVPVQkLTAGITRKLCFVLSLLGNSPVLL 1435
Cdd:cd03261 97 NVAFP---LREHTRLSEEE-----------IREIV-LEKLEavglrgaEDL-YPAE-LSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1436 LDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1502
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
502-676 |
1.54e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.49 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLsEMQDLEeIRKITGVCPQFnvqFDI---LTVKENLS 578
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIA-TRRRVGYMSQA---FSLygeLTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 579 LFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLR 658
Cdd:NF033858 362 LHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLI 441
|
170 180
....*....|....*....|
gi 27436953 659 E-RRADHVILF-STQSMDEA 676
Cdd:NF033858 442 ElSREDGVTIFiSTHFMNEA 461
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1302-1490 |
1.75e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.11 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELkgcssvLGH------------LGYCPQENVLWPML 1369
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL------FGQpvdagdiatrrrVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1449
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 1450 QMWQAIQAVVKntERGV--LLTTHNLAEAEaLCDRVAIMVSGR 1490
Cdd:NF033858 435 MFWRLLIELSR--EDGVtiFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
477-689 |
2.26e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSE--------M 548
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvvF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 549 QDleeirkiTGVCPQFNVQfdiltvkENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGIT 628
Cdd:PRK11248 77 QN-------EGLLPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNG 689
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1304-1532 |
2.40e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSV----------LGhLGYCPQENVLWPMLTLRE 1373
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG-EPVrfrsprdaqaAG-IAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 --HLEVYAAVKGL--RKADARLAiARLVSAFKLHEQLNVPVQKLTAG------ITRklcfvlSLLGNSPVLLLDEPSTGI 1443
Cdd:COG1129 99 niFLGREPRRGGLidWRAMRRRA-RELLARLGLDIDPDTPVGDLSVAqqqlveIAR------ALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1444 DPTGQQQMWQAIQAVvknTERGV--LLTTHNLAEAEALCDRVAIMVSGRlrcigsiqhlknklgkdYILELKVKETSQVT 1521
Cdd:COG1129 172 TEREVERLFRIIRRL---KAQGVaiIYISHRLDEVFEIADRVTVLRDGR-----------------LVGTGPVAELTEDE 231
|
250
....*....|....*
gi 27436953 1522 LVHT----EILKLFP 1532
Cdd:COG1129 232 LVRLmvgrELEDLFP 246
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1302-1486 |
3.31e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.21 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQENVL---WPmLTLREHLEV- 1377
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV----AYVPQRSEVpdsLP-LTVRDLVAMg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 -YAAVKGLRK--ADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1454
Cdd:NF040873 82 rWARRGLWRRltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170 180 190
....*....|....*....|....*....|..
gi 27436953 1455 IQAVVKnTERGVLLTTHNLAEAeALCDRVAIM 1486
Cdd:NF040873 162 LAEEHA-RGATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1300-1491 |
3.49e-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: 84.02 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGH--------LGYCP---QENVLWPM 1368
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprdairagIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1369 LTLREHlevyaavkglrkadarLAIARLVSAFklheqlNvpVQKLtagitrklcfVLS--LLGNSPVLLLDEPSTGIDPT 1446
Cdd:cd03215 93 LSVAEN----------------IALSSLLSGG------N--QQKV----------VLArwLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 1447 GQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03215 139 AKAEIYRLIRELADAG-KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
466-691 |
3.90e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 466 EPVAPefqGKEAIRIRNVkkEYKGKSGkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL 545
Cdd:COG3845 249 APAEP---GEVVLEVENL--SVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 546 S-----EMQDL------EEiRKITGVCPQFnvqfdilTVKENLSL-------FAKIKGIHLKEVEQEVQRILLELD--MQ 605
Cdd:COG3845 323 TglsprERRRLgvayipED-RLGRGLVPDM-------SVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDvrTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 606 NIqDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKV 684
Cdd:COG3845 395 GP-DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAaVLLISEDLDEILALSDRIA 473
|
....*..
gi 27436953 685 IMSNGRL 691
Cdd:COG3845 474 VMYEGRI 480
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
482-696 |
4.11e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 482 NVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVC 561
Cdd:PRK10895 8 NLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 562 PQFNVQFDILTVKENLSLFAKI-KGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDE 640
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 641 PTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
478-710 |
4.79e-18 |
|
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: 85.28 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 557
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD-LNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDIlTVKENLSLfakikGIHLKEVEQEVQRILLeldmQNIQDNLAK--------------HLSEGQKRKL 623
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRY-----GKPDATDEEVEEAAKK----ANIHDFIMSlpdgydtlvgergsQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 624 TFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH---VI---LFSTQSmdeadilADRKVIMSNGRLKCAGSS 697
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRttiVIahrLSTIRN-------ADLIAVLQNGQVVEQGTH 221
|
250
....*....|...
gi 27436953 698 MFLKRRWGLGYHL 710
Cdd:cd03249 222 DELMAQKGVYAKL 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1294-1491 |
6.41e-18 |
|
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: 86.65 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP---TAGEVELKGcSSVLG------------HLG 1357
Cdd:COG0444 11 FPTRRGVVKAvDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDG-EDLLKlsekelrkirgrEIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1358 YCPQE--NVLWPMLTLREHL-EVYAAVKGLRKADARlaiARLVSAFKL--------------HE----QLnvpvQKltAG 1416
Cdd:COG0444 90 MIFQDpmTSLNPVMTVGDQIaEPLRIHGGLSKAEAR---ERAIELLERvglpdperrldrypHElsggMR----QR--VM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 1417 ITRklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG0444 161 IAR------ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
441-696 |
6.79e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.50 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 441 FQH--------QRTNaKVIEKEIDAEHPSDDYFEPVAPefqgkeAIRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAI 512
Cdd:PRK11160 301 FQHlgqviasaRRIN-EITEQKPEVTFPTTSTAAADQV------SLTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 513 LGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDlEEIRKITGVCPQ----FNVqfdilTVKENLsLFAKIKGI-- 586
Cdd:PRK11160 372 LGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQAISVVSQrvhlFSA-----TLRDNL-LLAAPNASde 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 587 HLKEVEQEVQ-RILLE----LDMQnIQDnLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERR 661
Cdd:PRK11160 445 ALIEVLQQVGlEKLLEddkgLNAW-LGE-GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA 522
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 27436953 662 ADHVILFST------QSMdeadilaDRKVIMSNGRLKCAGS 696
Cdd:PRK11160 523 QNKTVLMIThrltglEQF-------DRICVMDNGQIIEQGT 556
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
473-696 |
6.81e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.70 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 473 QGKEAIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdlE 552
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 553 EIRKITGVCPQFNVqFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGD 632
Cdd:PRK09452 84 ENRHVNTVFQSYAL-FPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 633 PQILLLDEPTTGLDPFSRDQVWSLLR--ERRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
478-696 |
6.91e-18 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 84.59 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdLEEIRKI 557
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDIlTVKENLSlFAKiKGIHLKEVEqEVQRI--LLELDMQ-------NIQDNLAKhLSEGQKRKLTFGIT 628
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA-YGR-PGATREEVE-EAARAanAHEFIMElpegydtVIGERGVK-LSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLR---ERRADHVIL--FSTqsmdeadIL-ADRKVIMSNGRLKCAGS 696
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALErlmKNRTTFVIAhrLST-------IEnADRIVVLEDGKIVERGT 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
478-696 |
8.13e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 8.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TgVCPQFNVQFDILTVKE--------NLSLFAKIKGihlkEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITI 629
Cdd:PRK11231 79 A-LLPQHHLTPEGITVRElvaygrspWLSLWGRLSA----EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 630 LGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH----VILfstQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGktvvTVL---HDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
478-696 |
8.29e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 8.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKI 557
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLsLFAKIKGihlKEVEQEVQRILLELDMQNIQDNLAKHL--SEGQKRKLTFGitILGDPQI 635
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENI-LFGLPKR---QASMQKMKQLLAALGCQLDLDSSAGSLevADRQIVEILRG--LMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1306-1495 |
8.32e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLGHL-GYCPQENVLWPMLTLRE----- 1373
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealSARAASRRvASVPQDTSLSFEFDVRQvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 ---HLEVYAAVKGLRKADARLAIARL-VSAFklheqLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1449
Cdd:PRK09536 102 rtpHRSRFDTWTETDRAAVERAMERTgVAQF-----ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27436953 1450 QMWQAIQAVVkNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:PRK09536 177 RTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
477-690 |
1.02e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYkgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEeiRK 556
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVcpqFnvQFDIL----TVKENLSLFAKIKGIHLKEVEQEVQ---RIL-LE--LDMQNIQdnlakhLSEGQKRKLTFG 626
Cdd:PRK11650 78 IAMV---F--QNYALyphmSVRENMAYGLKIRGMPKAEIEERVAeaaRILeLEplLDRKPRE------LSGGQRQRVAMG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 627 ITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGR 690
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRlhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1310-1491 |
1.05e-17 |
|
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: 83.70 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1310 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLGYCP-----QENVLWPMLTLREHLEVyAAVKGL 1384
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPvsmlfQENNLFAHLTVEQNVGL-GLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1385 R-KADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTE 1463
Cdd:cd03298 100 KlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETK 179
|
170 180
....*....|....*....|....*...
gi 27436953 1464 RGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1304-1491 |
1.07e-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: 82.26 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC------SSVLG-HLGYCPQENVLWPMlTLREHLe 1376
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdPNELGdHVGYLPQDDELFSG-SIAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 vyaAVKGLRKadaRLAIARlvsafklheqlnvpvqkltagitrklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQ 1456
Cdd:cd03246 97 ---LSGGQRQ---RLGLAR------------------------------ALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*
gi 27436953 1457 AvVKNTERGVLLTTHNLaEAEALCDRVAIMVSGRL 1491
Cdd:cd03246 141 A-LKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
478-709 |
1.20e-17 |
|
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: 83.82 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 557
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-TLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDIlTVKENLSL------------FAKIKGIH--LKEVEQEVQRILLELDMQniqdnlakhLSEGQKRKL 623
Cdd:cd03253 77 IGVVPQDTVLFND-TIGYNIRYgrpdatdeevieAAKAAQIHdkIMRFPDGYDTIVGERGLK---------LSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 624 TFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEAdILADRKVIMSNGRLKCAGSSMFLKRR 703
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
....*.
gi 27436953 704 WGLgYH 709
Cdd:cd03253 226 GGL-YA 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1299-1507 |
1.63e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.03 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1299 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVElkgcssVLG--------------HLGYCPQ--- 1361
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE------VLGgdmadarhrravcpRIAYMPQglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1362 ENvLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKlcfvLSL---LGNSPVLL-LD 1437
Cdd:NF033858 87 KN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQK----LGLccaLIHDPDLLiLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1438 EPSTGIDPTGQQQMWQAIQAVvkNTERG---VLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLGKD 1507
Cdd:NF033858 162 EPTTGVDPLSRRQFWELIDRI--RAERPgmsVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGAD 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1290-1489 |
1.78e-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: 82.69 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1290 KKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLgycpQENVLWPML 1369
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER----RKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHL---EVYAAVK-GLRKADARLAIAR-LVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:cd03226 79 DVDYQLftdSVREELLlGLKELDAGNEQAEtVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 1445 PTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSG 1489
Cdd:cd03226 159 YKNMERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
486-647 |
1.99e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 486 EYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD------------LEE 553
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 554 IR-KITGVCPQFNVqFDILTVKENLsLFAKIKGIHLKEVEQEvQRILLELDMQNI----QDNLAKHLSEGQKRKLTFGIT 628
Cdd:PRK10619 90 LRtRLTMVFQHFNL-WSHMTVLENV-MEAPIQVLGLSKQEAR-ERAVKYLAKVGIderaQGKYPVHLSGGQQQRVSIARA 166
|
170
....*....|....*....
gi 27436953 629 ILGDPQILLLDEPTTGLDP 647
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDP 185
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1305-1498 |
2.19e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.67 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLG---------HLGYCPQENVL-WPmLTLRE- 1373
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP--LAdwspaelarRRAVLPQHSSLsFP-FTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 -------HLEVYAAVKGLrkADARLAIARLvSAFKlheqlNVPVQKLTAG------ITRKLCFVLSLLGNSPVLLLDEPS 1440
Cdd:PRK13548 97 vamgrapHGLSRAEDDAL--VAAALAQVDL-AHLA-----GRDYPQLSGGeqqrvqLARVLAQLWEPDGPPRWLLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1441 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1498
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
478-691 |
2.77e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.11 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEIRKI 557
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-WDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQfnvqfDILtvkenlsLFAKikgihlkeveqevqrilleldmqNIQDNLakhLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03246 78 VGYLPQ-----DDE-------LFSG-----------------------SIAENI---LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1304-1490 |
3.48e-17 |
|
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: 82.83 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV--------------ELK---GCSSVLGHLGYCPQENVLw 1366
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgerrggedvwELRkriGLVSPALQLRFPRDETVL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1367 pmltlrehlEV-----YAAVkGLRK----ADARLAiARLVSAFKLHEQLNVPVQKLTAGITRKlcfVL---SLLGNSPVL 1434
Cdd:COG1119 99 ---------DVvlsgfFDSI-GLYReptdEQRERA-RELLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1435 LLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
509-696 |
3.59e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 509 ITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemqDLE-------EIRKItGVCPQFNVQFDILTVKENL---- 577
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF---DAEkgiclppEKRRI-GYVFQDARLFPHYKVRGNLrygm 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 578 -----SLFAKIKGIhlkeveqevqrilleLDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLD-PFSRD 651
Cdd:PRK11144 102 aksmvAQFDKIVAL---------------LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27436953 652 qvwsLLR--ERRADHV---ILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK11144 167 ----LLPylERLAREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-697 |
3.66e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.17 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 474 GKEAIRIRNVKKEYKGKSGKVeALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL------SVPTEGSVTIYNKNLSE 547
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 548 MqDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKIKGIHLKE-----VEQEVQRILLELDMQNIQDNLAKHLSEGQKRK 622
Cdd:PRK14246 83 I-DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 623 LTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSS 697
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
496-686 |
5.66e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.74 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 496 ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiynknlsemqdleeiRKITGVCPQFNVQ-------F 568
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------------RRAGGARVAYVPQrsevpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 569 DiLTVKE--NLSLFAKIK--GIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTG 644
Cdd:NF040873 71 P-LTVRDlvAMGRWARRGlwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 645 LDPFSRDQVWSLLRERRADHV-ILFSTQSMDEAdILADRKVIM 686
Cdd:NF040873 150 LDAESRERIIALLAEEHARGAtVVVVTHDLELV-RRADPCVLL 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
502-691 |
6.16e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.94 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqdlEEIRKITGVCPQFNVQFDILTVKENLSLfa 581
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT---PPSRRPVSMLFQENNLFSHLTVAQNIGL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 582 kikGIH--LK---EVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSL 656
Cdd:PRK10771 95 ---GLNpgLKlnaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 27436953 657 LRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK10771 172 VSQvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
480-691 |
7.81e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.32 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD--LEEIRKi 557
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdaLAQLRR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 tgvcPQFNVQFDI------LTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILG 631
Cdd:PRK10535 86 ----EHFGFIFQRyhllshLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 632 DPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADiLADRKVIMSNGRL 691
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
474-696 |
8.94e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 474 GKEAIRIRNVKKEYKGK-SGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT---IYNK------ 543
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdIYIGdkknnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 544 ------NLSEMQDLEEIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQ-NIQDNLAKHL 615
Cdd:PRK13631 98 elitnpYSKKIKNFKELRRRVSMVFQFpEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 616 SEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFS-TQSMDEADILADRKVIMSNGRLKCA 694
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFViTHTMEHVLEVADEVIVMDKGKILKT 257
|
..
gi 27436953 695 GS 696
Cdd:PRK13631 258 GT 259
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1307-1500 |
1.68e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1307 SFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlgHLGYCP---------QENVLWPMLTLREHLEV 1377
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPsrrpvsmlfQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 YAAvKGLR-KADARLAIARLVSAFKLHEQLN-VPVQkLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1455
Cdd:PRK10771 95 GLN-PGLKlNAAQREKLHAIARQMGIEDLLArLPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 1456 QAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
478-710 |
2.49e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 80.22 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSeMQDLEEIRKI 557
Cdd:cd03252 1 ITFEHVRFRYKPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDiLTVKENLSLfaKIKGIHLKEVEqEVQRIL--------LELDMQNIQDNLAKHLSEGQKRKLTFGITI 629
Cdd:cd03252 78 VGVVLQENVLFN-RSIRDNIAL--ADPGMSMERVI-EAAKLAgahdfiseLPEGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 630 LGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMdEADILADRKVIMSNGRLKCAGSSMFLKRRWGLGYH 709
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
.
gi 27436953 710 L 710
Cdd:cd03252 233 L 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
478-691 |
3.15e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGksGKvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEE--IR 555
Cdd:PRK10908 2 IRFEHVSKAYLG--GR-QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQI 635
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 636 LLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
478-691 |
3.59e-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: 79.44 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSeMQDLEEIRKI 557
Cdd:cd03248 12 VKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDiLTVKENLSLfaKIKGIHLKEVEQEVQRI-------LLELDMQNIQDNLAKHLSEGQKRKLTFGITIL 630
Cdd:cd03248 90 VSLVGQEPVLFA-RSLQDNIAY--GLQSCSFECVKEAAQKAhahsfisELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADiLADRKVIMSNGRL 691
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1302-1496 |
3.88e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.19 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlghLGYCP----------QENVLWPMLTL 1371
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-----LSHVPpyqrpinmmfQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQM 1451
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 1452 WQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:PRK11607 189 QLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
449-651 |
4.08e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 449 KVIEK--EIDAEHPSDD-YFEPVAPEFQGKEAIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLN 525
Cdd:COG0488 284 KALEKleREEPPRRDKTvEIRFPPPERLGKKVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 526 ILNGLSVPTEGSVTIyNKNLSemqdleeirkiTGVCPQFNVQFDI-LTVKENLSLFAkiKGIHLKEVEQEVQRILLELDM 604
Cdd:COG0488 360 LLAGELEPDSGTVKL-GETVK-----------IGYFDQHQEELDPdKTVLDELRDGA--PGGTEQEVRGYLGRFLFSGDD 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27436953 605 qniQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRD 651
Cdd:COG0488 426 ---AFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLE 469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1294-1497 |
4.36e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 80.25 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLG-HLGYCPQenvlwpmLTLR 1372
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAiSAGLSGQ-------LTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1452
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 1453 QAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSI 1497
Cdd:PRK13546 184 DKIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
478-691 |
4.66e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 79.37 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYN-KNLSEMQDLEEIRK 556
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITG-VCPQFNVqFDILTVKENLsLFA--KIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDP 633
Cdd:PRK09493 78 EAGmVFQQFYL-FPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 634 QILLLDEPTTGLDPFSRDQVWSLLR---ERRADHVILfsTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIV--THEIGFAEKVASRLIFIDKGRI 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1296-1491 |
4.90e-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: 78.85 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1296 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISG---ITKPTAGEVELKGCSS----VLGHLGYCPQENVLWPM 1368
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRkpdqFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1369 LTLREHLeVYAAVKGLRKADARLAIARLVSAFKL----HEQL-NVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGI 1443
Cdd:cd03234 96 LTVRETL-TYTAILRLPRKSSDAIRKKRVEDVLLrdlaLTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27436953 1444 DP-TGQQQMWQAIQAVVKNteRGVLLTTHN-LAEAEALCDRVAIMVSGRL 1491
Cdd:cd03234 175 DSfTALNLVSTLSQLARRN--RIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
497-658 |
5.22e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDlEEIRKITGVCPQFNVQfDILTVKEN 576
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIK-TTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 577 LSLFAKIKGihlkevEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSL 656
Cdd:cd03231 94 LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
..
gi 27436953 657 LR 658
Cdd:cd03231 168 MA 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
478-697 |
5.58e-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: 82.93 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS--VPTEGSVtIYNKNLSEMQDLEEIR 555
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IYHVALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGV-CP-------QFNVQFDILTVKENLSLFAKIkGIHLK------------------------EVEQEVQRILLELD 603
Cdd:TIGR03269 76 SKVGEpCPvcggtlePEEVDFWNLSDKLRRRIRKRI-AIMLQrtfalygddtvldnvlealeeigyEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 604 MQNIQD---NLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH---VILFS--TQSMDE 675
Cdd:TIGR03269 155 MVQLSHritHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgisMVLTShwPEVIED 234
|
250 260
....*....|....*....|..
gi 27436953 676 adiLADRKVIMSNGRLKCAGSS 697
Cdd:TIGR03269 235 ---LSDKAIWLENGEIKEEGTP 253
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
473-647 |
5.79e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 79.46 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 473 QGKEAIRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL------- 545
Cdd:COG4598 4 TAPPALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 546 -----SEMQDLEEIR-KITGVCPQFNVqFDILTVKENLsLFAKI--KGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSE 617
Cdd:COG4598 80 gelvpADRRQLQRIRtRLGMVFQSFNL-WSHMTVLENV-IEAPVhvLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190
....*....|....*....|....*....|
gi 27436953 618 GQKRKLTFGITILGDPQILLLDEPTTGLDP 647
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1297-1491 |
6.81e-16 |
|
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: 78.76 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGI-----TKPTAGEVELKGcsSVLGHLGYCP----------- 1360
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDG--KDIYDLDVDVlelrrrvgmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1361 QENVLWPMlTLREHLEVYAAVKGLRKADARLAIARlvSAFK---LHEQLN--VPVQKLTAGITRKLCFVLSLLGNSPVLL 1435
Cdd:cd03260 88 QKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVE--EALRkaaLWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1436 LDEPSTGIDPTGQQQMWQAIQAVvkNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
478-691 |
6.99e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEY-KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKN------------ 544
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 545 -----------LSEMQDLEEIRKITGVCPQF-NVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRI--LLELDMQNIQDN 610
Cdd:PRK13651 83 vleklviqktrFKKIKKIKEIRRRVGVVFQFaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYieLVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 611 lAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNG 689
Cdd:PRK13651 163 -PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 27436953 690 RL 691
Cdd:PRK13651 242 KI 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1304-1491 |
9.76e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.97 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP----TAGEVELKG----CSSVLGHLGYCPQEN---VLWPMLTLR 1372
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGkpvaPCALRGRKIATIMQNprsAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKGLRKADARLAIArlVSAFKLHEQLNV----PVQkLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1448
Cdd:PRK10418 100 THARETCLALGKPADDATLTAA--LEAVGLENAARVlklyPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 1449 QQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
499-673 |
1.01e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.54 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 499 GLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM-----QDLEEIRKITGVCPQfnvqfdiLTV 573
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhQDLLYLGHQPGIKTE-------LTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 574 KENLSLFAKIKGihlkevEQEVQRILLELDMQNIQ---DNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSR 650
Cdd:PRK13538 92 LENLRFYQRLHG------PGDDEALWEALAQVGLAgfeDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|....*.
gi 27436953 651 DQVWSLLrERRADH---VILFSTQSM 673
Cdd:PRK13538 166 ARLEALL-AQHAEQggmVILTTHQDL 190
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1305-1491 |
1.37e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------------SVLGHLGYCPQENVLWPMLTL 1371
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpsekairLLRQKVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHL-EVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1450
Cdd:COG4161 100 MENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27436953 1451 MWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG4161 180 VVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
495-696 |
1.40e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 495 EALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL--SEMQDLEEIRKITGVCPQFNVQFDILT 572
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 573 VKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQ 652
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27436953 653 VWSLLRE--RRADHVILfSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK13638 175 MIAIIRRivAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1268-1495 |
1.69e-15 |
|
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: 81.39 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1268 TSILDEKPVIIASCLHKEYagqkksCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELK 1347
Cdd:TIGR03269 271 CEVEVGEPIIKVRNVSKRY------ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1348 --------------GCSSVLGHLGYCPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSA-F---KLHEQLNVP 1409
Cdd:TIGR03269 345 vgdewvdmtkpgpdGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVgFdeeKAEEILDKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1410 VQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSG 1489
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
....*.
gi 27436953 1490 RLRCIG 1495
Cdd:TIGR03269 505 KIVKIG 510
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1274-1439 |
1.82e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1274 KPVIIASCLHKEYAGqkkscfskrkKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVElkgcssvL 1353
Cdd:COG0488 313 KKVLELEGLSKSYGD----------KTLL-DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-------L 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1354 GH---LGYCPQENvlwpmLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLH-EQLNVPVQKLTAGITRKLCFVLSLLG 1429
Cdd:COG0488 375 GEtvkIGYFDQHQ-----EELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170
....*....|
gi 27436953 1430 NSPVLLLDEP 1439
Cdd:COG0488 450 PPNVLLLDEP 459
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
476-690 |
1.88e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 77.47 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 476 EAIRIRNVKKEYK-----GKsgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK----NLS 546
Cdd:COG4778 3 TLLEVENLSKTFTlhlqgGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 547 EMQDLE--EIRKIT-GVCPQF-NV-----QFDIltVKEnlSLFAkiKGIHLKEVEQEVQRILLELdmqNIQDNLAkHL-- 615
Cdd:COG4778 81 QASPREilALRRRTiGYVSQFlRViprvsALDV--VAE--PLLE--RGVDREEARARARELLARL---NLPERLW-DLpp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 616 ---SEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRAD--------HvilfstqsmDEA--DILADR 682
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgtaiigifH---------DEEvrEAVADR 221
|
....*...
gi 27436953 683 KVIMSNGR 690
Cdd:COG4778 222 VVDVTPFS 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1302-1496 |
2.38e-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: 77.38 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHL-----GYCPQENVLWPMLTLREHLE 1376
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqernvGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 VYAAVKGLRKADARLAIARlvsafKLHEQLNV----------PVQkLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1446
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRA-----KVHELLKLvqldwladryPAQ-LSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27436953 1447 GQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:cd03296 171 VRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
496-690 |
2.77e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 496 ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKitGVCPQF-NVQ-FDILTV 573
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM--GVVRTFqHVRlFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 574 KENL----------SLFAK-IKGIHLKEVEQE--------VQRILLeLDMQNIQdnlAKHLSEGQKRKLTFGITILGDPQ 634
Cdd:PRK11300 98 IENLlvaqhqqlktGLFSGlLKTPAFRRAESEaldraatwLERVGL-LEHANRQ---AGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 635 ILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGR 690
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1304-1496 |
3.47e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.59 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQENVLWPMlTLREHL- 1375
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltlESLRRQIGVVPQDTFLFSG-TIRENIr 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 ---------EVYAAvkgLRKADA----------------------------RLAIARlvsafklheqlnvpvqkltagit 1418
Cdd:COG1132 436 ygrpdatdeEVEEA---AKAAQAhefiealpdgydtvvgergvnlsggqrqRIAIAR----------------------- 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1419 rklcfvlSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGS 1496
Cdd:COG1132 490 -------ALLKDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1290-1509 |
3.61e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1290 KKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSV-----------LGHLGY 1358
Cdd:PRK10070 31 KEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaelrevrRKKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1359 CPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDE 1438
Cdd:PRK10070 111 VFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 1439 PSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYI 1509
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1302-1503 |
4.41e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLGH-------LGYCPQENVLWPMLTLRE 1373
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINyNKLDHklaaqlgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HLEV----YAAVKGLRKAD---ARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1446
Cdd:PRK09700 100 NLYIgrhlTKKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1447 GQQQMWqAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1503
Cdd:PRK09700 180 EVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1282-1491 |
4.61e-15 |
|
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: 76.03 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1282 LHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---------SV 1352
Cdd:cd03262 6 LHKSFGDFH-----------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkkninEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1353 LGHLGYCPQENVLWPMLTLREHL-EVYAAVKGLRKADARlAIAR-LVSAFKLHEQLNVPVQKLTAG------ITRKLCFv 1424
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENItLAPIKVKGMSKAEAE-ERALeLLEKVGLADKADAYPAQLSGGqqqrvaIARALAM- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1425 lsllgNSPVLLLDEPSTGIDPtgqqQMWQAIQAVVKN-TERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03262 153 -----NPKVMLFDEPTSALDP----ELVGEVLDVMKDlAEEGmtMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1304-1439 |
6.43e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 6.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-KGCSsvlghLGYCPQENVLWPMLTLRE-----HLEV 1377
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLR-----IGYLPQEPPLDDDLTVLDtvldgDAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 YAAVKGLRKADARLA---------------------------IARLVSAFKLH-EQLNVPVQKLTAGITRKLCFVLSLLG 1429
Cdd:COG0488 90 RALEAELEELEAKLAepdedlerlaelqeefealggweaearAEEILSGLGFPeEDLDRPVSELSGGWRRRVALARALLS 169
|
170
....*....|
gi 27436953 1430 NSPVLLLDEP 1439
Cdd:COG0488 170 EPDLLLLDEP 179
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1294-1491 |
7.38e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.81 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGHL------------GYCP 1360
Cdd:COG1135 11 FPTKGGPVTAlDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG--VDLTALserelraarrkiGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1361 Q-----------ENVLWPMltlrEHLEVYAA-----VK------GLR-KADA-----------RLAIARlvsAfklheql 1406
Cdd:COG1135 89 QhfnllssrtvaENVALPL----EIAGVPKAeirkrVAellelvGLSdKADAypsqlsggqkqRVGIAR---A------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1407 nvpvqkltagitrklcfvlslLGNSP-VLLLDEPSTGIDP-TGQQqmwqaIQAVVK--NTERG--VLLTTHNLAEAEALC 1480
Cdd:COG1135 155 ---------------------LANNPkVLLCDEATSALDPeTTRS-----ILDLLKdiNRELGltIVLITHEMDVVRRIC 208
|
250
....*....|.
gi 27436953 1481 DRVAIMVSGRL 1491
Cdd:COG1135 209 DRVAVLENGRI 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
478-692 |
1.16e-14 |
|
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: 74.37 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKI 557
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDiLTVKENLSLFAkikgihlkevEQEVQRILLELDMQNIQDNlakhLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03369 84 LTIIPQDPTLFS-GTIRSNLDPFD----------EYSDEEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEAdILADRKVIMSNGRLK 692
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTI-IDYDKILVMDAGEVK 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
497-692 |
1.56e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdlEEIR-----KITGVCPQFNVQFDIL 571
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD--EEARaklraKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 TVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRD 651
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 652 QVWSLLRERRADHVILFSTQSMDEAdiLA---DRKVIMSNGRLK 692
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQ--LAarcDRRLRLVNGQLQ 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
448-664 |
1.71e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 79.38 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 448 AKVIEKEIDAEHPSDDYFEPVAPEFQGKEAIRI-RNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNI 526
Cdd:TIGR00956 729 AGEVLGSTDLTDESDDVNDEKDMEKESGEDIFHwRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 527 LNG---LSVPTEGSVTIynkNLSEMQdlEEIRKITGVCPQFNVQFDILTVKENLSLFAKI---KGIHLKEVEQEVQRILL 600
Cdd:TIGR00956 809 LAErvtTGVITGGDRLV---NGRPLD--SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIK 883
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 601 ELDMQNIQDNLAKHLSEG----QKRKLTFGITILGDPQILL-LDEPTTGLDPFSrdqVWSLLRERR--ADH 664
Cdd:TIGR00956 884 LLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT---AWSICKLMRklADH 951
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
492-716 |
2.15e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.35 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVeALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLsVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQfNVQFDIL 571
Cdd:PRK11174 362 GKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPESWRKHLSWVGQ-NPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 TVKENLSLfAKIKgIHLKEVEQEVQR---------ILLELDMQnIQDNLAKhLSEGQKRKLTFGITILGDPQILLLDEPT 642
Cdd:PRK11174 438 TLRDNVLL-GNPD-ASDEQLQQALENawvseflplLPQGLDTP-IGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 643 TGLDPFSRDQVWSLLRERRADHVILFSTQSMDEadiLA--DRKVIMSNGRLKCAGSSMFLKRRWGLGYHLSLHRNE 716
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRQTTLMVTHQLED---LAqwDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1304-1480 |
2.64e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.45 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS------SVLGHLGYCPQENVLWPMLTLREHlev 1377
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdlcTYQKQLCFVGHRSGINPYLTLREN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 yaAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1457
Cdd:PRK13540 95 --CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170 180
....*....|....*....|....*...
gi 27436953 1458 VVKNTErGVLLTTH-----NLAEAEALC 1480
Cdd:PRK13540 173 HRAKGG-AVLLTSHqdlplNKADYEEYH 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1304-1491 |
3.14e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGH--------LGYCP---QENVLWPMLTLR 1372
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdairagIAYVPedrKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 E-----HLEVYAAVKGLRKADARLAIARLVsafklhEQLNV-------PVQKLTAGITRKLcfVLS--LLGNSPVLLLDE 1438
Cdd:COG1129 349 EnitlaSLDRLSRGGLLDRRRERALAEEYI------KRLRIktpspeqPVGNLSGGNQQKV--VLAkwLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1439 PSTGIDPTGQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG1129 421 PTRGIDVGAKAEIYRLIRELAAEG-KAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
34-376 |
4.54e-14 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 75.50 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 34 WGLSILLGLCIALFSSSMRNVQFPGMAPQNLGRVDKFNSSslmvvytpisnLTQQIMNKTALAPLLKGTSVIgaPNKTHM 113
Cdd:pfam12698 4 LIITLLLPILLILLLGLIFSNAVNDPEELPVAVVDEDNSS-----------LSRQLVRALEASPTVNLVQYV--DSEEEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 114 DEiLLENLPYAMGIIFNETFSYKLIFFQGYNSPLWKEDFSAHcwdgygefsctltkywnrGFVALQTAINTAIIEITTNH 193
Cdd:pfam12698 71 KE-ALKNGKIDGLLVIPKGFSKDLLKGESATVTVYINSSNLL------------------VSKLILNALQSLLQQLNASA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 194 PVMEELMSVTAITMKTLPFITKN-LLHNEMFILFFLLHFSPLVYF--ISLNVTKER-KKSKNLMKMMGLQDSAFWLSWGL 269
Cdd:pfam12698 132 LVLLLEALSTSAPIPVESTPLFNpQSGYAYYLVGLILMIIILIGAaiIAVSIVEEKeSRIKERLLVSGVSPLQYWLGKIL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 270 IYAGFIFIISIFVTIIITFTQIIvMTGFMVIFILFFLYGLSLVALVFLMSVLLKKAVLTNLVVFLLTL-FWGCLGFTVFY 348
Cdd:pfam12698 212 GDFLVGLLQLLIILLLLFGIGIP-FGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILlLSGFFGGLFPL 290
|
330 340
....*....|....*....|....*...
gi 27436953 349 EQLPSSLEWILNICSPFAFTTGMIQIIK 376
Cdd:pfam12698 291 EDPPSFLQWIFSIIPFFSPIDGLLRLIY 318
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1266-1496 |
4.56e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.75 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1266 LTTSILDEKPVIIASCLHKEYAGqkkscfskrkkKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVE 1345
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDG-----------KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1346 LKGCssVLGHLgycPQE----NVLWPMLTLREHLEVYAAVK-GLR-KADARLAIARLVS-AFK---LHEQLNVPVQKLTA 1415
Cdd:PRK09452 73 LDGQ--DITHV---PAEnrhvNTVFQSYALFPHMTVFENVAfGLRmQKTPAAEITPRVMeALRmvqLEEFAQRKPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1416 G------ITRKLCfvlsllgNSP-VLLLDEPSTGIDPTGQQQMwqaiQAVVKNTERGVLLT----THNLAEAEALCDRVA 1484
Cdd:PRK09452 148 GqqqrvaIARAVV-------NKPkVLLLDESLSALDYKLRKQM----QNELKALQRKLGITfvfvTHDQEEALTMSDRIV 216
|
250
....*....|..
gi 27436953 1485 IMVSGRLRCIGS 1496
Cdd:PRK09452 217 VMRDGRIEQDGT 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1298-1491 |
4.82e-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: 71.96 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1298 KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcssvlghlgycpqenvlwpmltlrehLEV 1377
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG--------------------------VPV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 YAAVKGLRKADARLAIARLVSAFKLHEQLNVPvqkLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1457
Cdd:cd03247 67 SDLEKALSSLISVLNQRPYLFDTTLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFE 143
|
170 180 190
....*....|....*....|....*....|....
gi 27436953 1458 VVKNteRGVLLTTHNLAEAEALcDRVAIMVSGRL 1491
Cdd:cd03247 144 VLKD--KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
480-646 |
6.06e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIyNKNLSeM----QD----- 550
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR-IgylpQEppldd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 551 ----LEEIrkITGVCPQFNVQFDILTVKENLS-----------LFAKIKGIHLKEVEQEVQRILLELDM-QNIQDNLAKH 614
Cdd:COG0488 75 dltvLDTV--LDGDAELRALEAELEELEAKLAepdedlerlaeLQEEFEALGGWEAEARAEEILSGLGFpEEDLDRPVSE 152
|
170 180 190
....*....|....*....|....*....|..
gi 27436953 615 LSEGQKRKLTFGITILGDPQILLLDEPTTGLD 646
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1291-1498 |
7.21e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 76.47 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1291 KSCFSKRKK---KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGhlgycpQENVLWP 1367
Cdd:PRK13545 25 KDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA------ISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1447
Cdd:PRK13545 99 QLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27436953 1448 QQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1498
Cdd:PRK13545 179 TKKCLDKMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIK 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
495-691 |
1.36e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 495 EALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD----------LEEIRKITG----- 559
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvyLPEDRQSSGlylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 560 -----VC--PQFNVQFDILTVKEN--LSLFAKIKGIHLKEVEQEVQRilleldmqniqdnlakhLSEGQKRKLTFGITIL 630
Cdd:PRK15439 357 plawnVCalTHNRRGFWIKPARENavLERYRRALNIKFNHAEQAART-----------------LSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1282-1491 |
1.44e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.07 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1282 LHKEYAGqkkscfsKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLG------ 1354
Cdd:PRK11153 7 ISKVFPQ-------GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDlTALSekelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1355 ---HLGYCPQ-----------ENVLWPmltlrehLEvyaaVKGLRKADARLAIARLVSAFKLHEQLNV-PV-----QKLT 1414
Cdd:PRK11153 80 arrQIGMIFQhfnllssrtvfDNVALP-------LE----LAGTPKAEIKARVTELLELVGLSDKADRyPAqlsggQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1415 AGITRKlcfvlslLGNSP-VLLLDEPSTGIDPtgqqQMWQAIQAVVK--NTERG--VLLTTHNLAEAEALCDRVAIMVSG 1489
Cdd:PRK11153 149 VAIARA-------LASNPkVLLCDEATSALDP----ATTRSILELLKdiNRELGltIVLITHEMDVVKRICDRVAVIDAG 217
|
..
gi 27436953 1490 RL 1491
Cdd:PRK11153 218 RL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1305-1502 |
1.65e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGH-------------LGYCPQENVLWPMLTL 1371
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsdkairelrrnVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHL-EVYAAVKGLRKADA---------RLAIARLVSAFKLHeqlnvpvqkLTAGITRKLCFVLSLLGNSPVLLLDEPST 1441
Cdd:PRK11124 100 QQNLiEAPCRVLGLSKDQAlaraeklleRLRLKPYADRFPLH---------LSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1442 GIDPTGQQQMWQAIQAVvknTERGV--LLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1502
Cdd:PRK11124 171 ALDPEITAQIVSIIREL---AETGItqVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
478-659 |
2.06e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.01 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIynknlsemqdleeirki 557
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 tgvcpqfnvqfdiltvkenlslfakIKGIHLKEVEQevqrilleldmqniqdnlakhLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03221 60 -------------------------GSTVKIGYFEQ---------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180
....*....|....*....|..
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE 659
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE 115
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1500 |
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 27436953 1293 CFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLGHLGYCPQE 1362
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenireVRKFVGLVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1363 NVLWPmlTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTG 1442
Cdd:PRK13652 90 QIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1443 IDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
502-691 |
2.06e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QD--------LEEIRKITGVcpqfnvqfdIL 571
Cdd:PRK10762 273 FTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspQDglangivyISEDRKRDGL---------VL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 --TVKENLSL-----FAKiKGIHLKEvEQEVQRILLELDMQNI----QDNLAKHLSEGQKRKLTFGITILGDPQILLLDE 640
Cdd:PRK10762 344 gmSVKENMSLtalryFSR-AGGSLKH-ADEQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 641 PTTGLDPFSRDQVWSLLRERRAD--HVILFSTQsMDEADILADRKVIMSNGRL 691
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEglSIILVSSE-MPEVLGMSDRILVMHEGRI 473
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-691 |
2.25e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 509 ITAILGHSGAGKSSLLNILNGLSVPTEG-----SVTIYNKNLSEMQDLEEIRKITGVCPQFNVQFDILTVKENLSLFAKI 583
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 584 KGIHLKEVEQEVQRILLELDMQN-IQDNLAK---HLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE 659
Cdd:PRK14271 129 KLVPRKEFRGVAQARLTEVGLWDaVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190
....*....|....*....|....*....|..
gi 27436953 660 RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK14271 209 LADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1297-1494 |
3.36e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--------CSSVLGHLGYCPQ---ENVL 1365
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprspLDAVKKGMAYITEsrrDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1366 WPMLTLREHLEVYAAVK--------GL--RKADARLA-IARLVSAFKLHeQLNVPVQKLTAGITRKLCFVLSLLGNSPVL 1434
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKdggykgamGLfhEVDEQRTAeNQRELLALKCH-SVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1435 LLDEPSTGIDPTGQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRLRCI 1494
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
480-691 |
3.88e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDleEIRkitg 559
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE--DTR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 560 vcpqfnVQFD---IL---TVKENLSLfaKIKGiHLKEveqEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDP 633
Cdd:PRK11247 85 ------LMFQdarLLpwkKVIDNVGL--GLKG-QWRD---AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 634 QILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1299-1491 |
4.03e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1299 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVLG-HLGYCPQENVLWPMLTL 1371
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlSSRQLArRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHLEV----YAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTG 1447
Cdd:PRK11231 94 RELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27436953 1448 Q-------QQMWQAIQAVVKntergVLlttHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK11231 174 QvelmrlmRELNTQGKTVVT-----VL---HDLNQASRYCDHLVVLANGHV 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1306-1499 |
4.65e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLG--------YCP----QENVLwPMLTLRE 1373
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagimLCPedrkAEGII-PVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HLEVYAAVKGLR----------KADARLAIARLVSAFKLHEQlnvPVQKLTAGITRKLcfVLS--LLGNSPVLLLDEPST 1441
Cdd:PRK11288 351 NINISARRHHLRagclinnrweAENADRFIRSLNIKTPSREQ---LIMNLSGGNQQKA--ILGrwLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1442 GIDPTGQQQMWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRLRciGSIQH 1499
Cdd:PRK11288 426 GIDVGAKHEIYNVIYEL---AAQGvaVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1295-1491 |
4.86e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.08 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1295 SKR--KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLGHL------------GYCP 1360
Cdd:COG2884 8 SKRypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD--LSRLkrreipylrrriGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1361 Q-----------ENVlwpMLTLRehlevyaaVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAG------ITRklcf 1423
Cdd:COG2884 86 QdfrllpdrtvyENV---ALPLR--------VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGeqqrvaIAR---- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1424 vlSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVvkNtERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG2884 151 --ALVNRPELLLADEPTGNLDPETSWEIMELLEEI--N-RRGttVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1304-1498 |
5.10e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.91 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------CSSVL-GHLGYCPQENVL-WPmLTLRE-- 1373
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawSPWELaRRRAVLPQHSSLaFP-FTVEEvv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 --HLEVYAAVKGLRKADARLAIARL-VSAFKlheqlNVPVQKLTAG------ITRKLCFVLSLLGNSP-VLLLDEPSTGI 1443
Cdd:COG4559 97 alGRAPHGSSAAQDRQIVREALALVgLAHLA-----GRSYQTLSGGeqqrvqLARVLAQLWEPVDGGPrWLFLDEPTSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1444 DPTGQQQMwqaIQAVVKNTERG--VLLTTH--NLAeaeAL-CDRVAIMVSGRLRCIGSIQ 1498
Cdd:COG4559 172 DLAHQHAV---LRLARQLARRGggVVAVLHdlNLA---AQyADRILLLHQGRLVAQGTPE 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
480-703 |
5.52e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.44 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSE--MQDleeiRKI 557
Cdd:PRK11432 9 LKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsIQQ----RDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCpQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:PRK11432 81 CMVF-QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRLKCAGSSMFLKRR 703
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRElqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
474-691 |
7.28e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 474 GKEAIRIRNVKKEYKGKsgkveaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLE- 552
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDa 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 553 ---------EIRKITGVCPQFnvqfdilTVKENLSLFAKIK--------GIHLKEVEQ---EVQRILLELDMQNIQDNLA 612
Cdd:PRK09700 336 vkkgmayitESRRDNGFFPNF-------SIAQNMAISRSLKdggykgamGLFHEVDEQrtaENQRELLALKCHSVNQNIT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 613 KhLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRAD-HVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK09700 409 E-LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1302-1500 |
7.72e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV---------ELKGCSSVLGHLGYCPQ--ENVLWPMlT 1370
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidySRKGLMKLRESVGMVFQdpDNQLFSA-S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1450
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27436953 1451 MWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1302-1491 |
1.18e-12 |
|
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: 68.97 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLG--------HLGYCPQENVLWPMLTL 1371
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdVSDLRGraipylrrKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTgqqQM 1451
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD---TT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 1452 WQAIQAVVKNTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:cd03292 173 WEIMNLLKKINKAGttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1282-1476 |
1.62e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.34 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1282 LHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLG---HLGY 1358
Cdd:PRK11248 7 LYADYGGKP-----------ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-KPVEGpgaERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1359 CPQENVLWPMLTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDE 1438
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 27436953 1439 PSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEA 1476
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1297-1489 |
1.73e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcsSVLGH----------LGYCPQ-ENVL 1365
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI------SILGQptrqalqknlVAYVPQsEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1366 WPMLTLREHLEV---YAAVKGLRKADAR------LAIARLVSAFKLHEQLNvpvqKLTAGITRKLCFVLSLLGNSPVLLL 1436
Cdd:PRK15056 91 WSFPVLVEDVVMmgrYGHMGWLRRAKKRdrqivtAALARVDMVEFRHRQIG----ELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1437 DEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDrVAIMVSG 1489
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1312-1483 |
1.74e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.97 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1312 EGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlghLGYCPQENVLWPMLTLREHLevYAAVKGL-RKADAR 1390
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----VSYKPQYIKADYEGTVRDLL--SSITKDFyTHPYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1391 LAIARLVSAFKLHEQLnvpVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTT 1470
Cdd:cd03237 97 TEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVE 173
|
170
....*....|...
gi 27436953 1471 HNLAEAEALCDRV 1483
Cdd:cd03237 174 HDIIMIDYLADRL 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1306-1471 |
1.74e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLG----HLGYCPQENVLWPMLTLREHLEVYAAV 1381
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdrsrFMAYLGHLPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1382 KGLRK---ADARLAIARLVSafklHEQlnVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAV 1458
Cdd:PRK13543 110 HGRRAkqmPGSALAIVGLAG----YED--TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAH 183
|
170
....*....|...
gi 27436953 1459 VKnTERGVLLTTH 1471
Cdd:PRK13543 184 LR-GGGAALVTTH 195
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1302-1491 |
1.89e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.72 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG------------CSSVLGHLGYCPQENVLWPml 1369
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkslleVRKTVGIVFQNPDDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1449
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 1450 QMWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK13639 175 QIMKLLYDL---NKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
462-691 |
1.90e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 462 DDYFEPVAPEfQGKEAIRIRNVKKEykgksgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIY 541
Cdd:COG1129 242 EDLFPKRAAA-PGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 542 NKNLS-----EMQD-----LEEIRKITGVCPqfnvqfdILTVKENLSL-----FAKIKGIHLKEVEQEVQRILLELD--M 604
Cdd:COG1129 313 GKPVRirsprDAIRagiayVPEDRKGEGLVL-------DLSIRENITLasldrLSRGGLLDRRRERALAEEYIKRLRikT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 605 QNIqDNLAKHLSEG--QKrkltfgiTILG-----DPQILLLDEPTTGLDPFSRDQVWSLLRERRAD--HVILFSTQsMDE 675
Cdd:COG1129 386 PSP-EQPVGNLSGGnqQK-------VVLAkwlatDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgkAVIVISSE-LPE 456
|
250
....*....|....*.
gi 27436953 676 ADILADRKVIMSNGRL 691
Cdd:COG1129 457 LLGLSDRILVMREGRI 472
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
497-692 |
2.07e-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: 69.50 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLsVPTEGSVTIYNKNLSEMQdLEEIRKITGVCPQFNVQFDiLTVKEN 576
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKAFGVIPQKVFIFS-GTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 577 LSLFAKIKGIHLKEVEQEVQ-RILLE-----LDMQNIQDNLAkhLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSR 650
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGlKSVIEqfpgqLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 651 DQVWSLLRERRADHVILFSTQSMdEADILADRKVIMSNGRLK 692
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1302-1503 |
2.35e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.89 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGIT---KPTAGEVELKG----CSSVLG--------HLGYCPQENVLW 1366
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrtvqREGRLArdirksraNTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1367 PMLTLREHLEVYAA------------VKGLRKADARLAIARLVSAFKLHEQlnvpVQKLTAGITRKLCFVLSLLGNSPVL 1434
Cdd:PRK09984 99 NRLSVLENVLIGALgstpfwrtcfswFTREQKQRALQALTRVGMVHFAHQR----VSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1435 LLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1503
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1294-1474 |
2.58e-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: 68.02 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQENVLW 1366
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrKSLRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1367 PMlTLREHLEV---YAAVKGLRKADARLAIARLVSAFK--LHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPST 1441
Cdd:cd03254 90 SG-TIMENIRLgrpNATDEEVIEAAKEAGAHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190
....*....|....*....|....*....|...
gi 27436953 1442 GIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLA 1474
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKG--RTSIIIAHRLS 199
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1279-1491 |
2.98e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1279 ASCLHKEYAGQkkSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvLGHL-- 1356
Cdd:PRK10419 6 VSGLSHHYAHG--GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP--LAKLnr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1357 -------------------GYCPQENVLWpmlTLRE---HLevyaavKGLRKADARLAIARLVSAFKLHEQL--NVPVQk 1412
Cdd:PRK10419 82 aqrkafrrdiqmvfqdsisAVNPRKTVRE---IIREplrHL------LSLDKAERLARASEMLRAVDLDDSVldKRPPQ- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1413 LTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1291-1500 |
3.14e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1291 KSCFSKRK-KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPtagevELKGCSSVL--GHL----------G 1357
Cdd:TIGR00955 28 RGCFCRERpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK-----GVKGSGSVLlnGMPidakemraisA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1358 YCPQENVLWPMLTLREHLEVYAAVK---GLRKADARLAIARLVSAFKL----HEQLNVP--VQKLTAGITRKLCFVLSLL 1428
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLrkcaNTRIGVPgrVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1429 GNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVkNTERGVLLTTHN-LAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1300-1510 |
3.46e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLG-------------HLGYCPQENVLW 1366
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGkdifqidaiklrkEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1367 PMLTLREHLEVYAAVKGLRKADARLAIA----RLVSAFK-LHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPST 1441
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVeeclRKVGLWKeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1442 GIDPTGQQQMWQAIQAVVKntERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL----KNKLGKDYIL 1510
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
478-697 |
5.28e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSG-----KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLsEMQDL- 551
Cdd:PRK15112 5 LEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 552 ---EEIRKI-----TGVCPQFNV-QFDILTVKENLSLfakikgihlkEVEQEVQRILLELDMQNIQDNLAKH----LSEG 618
Cdd:PRK15112 84 yrsQRIRMIfqdpsTSLNPRQRIsQILDFPLRLNTDL----------EPEQREKQIIETLRQVGLLPDHASYyphmLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 619 QKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVI--LFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
.
gi 27436953 697 S 697
Cdd:PRK15112 234 T 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1304-1483 |
5.59e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.78 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQenvlwpmLTLREHlevyaavkg 1383
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI----GYFEQ-------LSGGEK--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1384 lrkadARLAIARLvsafklheqlnvpvqkltagitrklcfvlsLLGNSPVLLLDEPSTGIDPTGQqqmwQAIQAVVKNTE 1463
Cdd:cd03221 77 -----MRLALAKL------------------------------LLENPNLLLLDEPTNHLDLESI----EALEEALKEYP 117
|
170 180
....*....|....*....|
gi 27436953 1464 RGVLLTTHNLAEAEALCDRV 1483
Cdd:cd03221 118 GTVILVSHDRYFLDQVATKI 137
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1302-1491 |
5.82e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLG------HLG----YcpQENVLWPMLTL 1371
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAsttaalAAGvaiiY--QELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 RE-----HLEVYAAV--KGLRKADARLAIARLvsafKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:PRK11288 97 AEnlylgQLPHKGGIvnRRLLNYEAREQLEHL----GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27436953 1445 PTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK11288 173 AREIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1315-1500 |
6.14e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.20 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1315 ILGLLGPNGAGKSSSIRMISGITKPTAG-----EVELKGCS-----SVLG---HLGYCPQENVLWPMLTLREHLEVYAAV 1381
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSifnyrDVLEfrrRVGMLFQRPNPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1382 KGLRK------ADARLAIARLVSAFKlhEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1455
Cdd:PRK14271 129 KLVPRkefrgvAQARLTEVGLWDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 1456 QAVVKNTErgVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK14271 207 RSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1293-1505 |
6.20e-12 |
|
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: 67.26 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1293 CFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVL 1365
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtLDSLRRAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1366 WPMlTLREHL----------EVYAAVKglrKADarlaIARLVSAFKlhEQLNVPVQ----KLTAGITRKLCFVLSLLGNS 1431
Cdd:cd03253 87 FND-TIGYNIrygrpdatdeEVIEAAK---AAQ----IHDKIMRFP--DGYDTIVGerglKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 1432 PVLLLDEPSTGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQHLKNKLG 1505
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1304-1491 |
6.51e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLG----------HLGYCPQENVLWPMLTLR 1372
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmSKLSsaakaelrnqKLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1452
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 27436953 1453 QAIQAVVKNTERGVLLTTHNLAEAEALcDRVAIMVSGRL 1491
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
492-659 |
6.68e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKItGVCPQFNVQFDIL 571
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI-GLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 TVKENLS--------LFAKIKgihlKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTT 643
Cdd:PRK10253 97 TVQELVArgryphqpLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170
....*....|....*.
gi 27436953 644 GLDPFSRDQVWSLLRE 659
Cdd:PRK10253 173 WLDISHQIDLLELLSE 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1294-1500 |
7.17e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAA-RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVElkgCSSVL------------------- 1353
Cdd:PRK10261 22 FMQEQQKIAAvRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ---CDKMLlrrrsrqvielseqsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1354 -----GHLGYCPQENV--LWPMLTLREHL-EVYAAVKGLRKADARLAIARLVSAFKLHEQLNV----PVQkLTAGITRKL 1421
Cdd:PRK10261 99 rhvrgADMAMIFQEPMtsLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsryPHQ-LSGGMRQRV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1422 CFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
467-692 |
7.59e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 467 PVAPEFQGKEAIRIRNVKKeYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGlSVPT--EGSVTIYNKN 544
Cdd:TIGR02633 247 PHEPHEIGDVILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKP 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 545 LSEMQDLEEI----------RKITGVCPQFNVQFDI-LTVkenLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLA- 612
Cdd:TIGR02633 325 VDIRNPAQAIragiamvpedRKRHGIVPILGVGKNItLSV---LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPi 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 613 KHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQsMDEADILADRKVIMSNGR 690
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEGK 480
|
..
gi 27436953 691 LK 692
Cdd:TIGR02633 481 LK 482
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1306-1491 |
8.73e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITkPTAGEVELKG-----CS-SVLGHL-GYCPQENVLWPMLTLREHLEVY 1378
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGrplsdWSaAELARHrAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1379 AAvKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPV-------LLLDEPSTGIDPTGQQQM 1451
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTinpegqlLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 1452 WQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG4138 173 DRLLREL---CQQGitVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1304-1510 |
9.99e-12 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 66.74 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMlTLREHLE 1376
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladPAWLRRQVGVVLQENVLFNR-SIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 VYAAVKGLRK--ADARLAIARlvsAF--KLHEQLNVPVQK----LTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1448
Cdd:cd03252 98 LADPGMSMERviEAAKLAGAH---DFisELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1449 QQMWQAIQAVVKNteRGVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLGKDYIL 1510
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
493-646 |
1.02e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 70.26 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 493 KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVP--TEGSVTI--YNKNLsemqdlEEIRKITGVCPQFNVQF 568
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRIsgFPKKQ------ETFARISGYCEQNDIHS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 569 DILTVKENL--SLFAKIKgihlKEVEQE-----VQRILLELDMQNIQDNLA-----KHLSEGQKRKLTFGITILGDPQIL 636
Cdd:PLN03140 966 PQVTVRESLiySAFLRLP----KEVSKEekmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSII 1041
|
170
....*....|
gi 27436953 637 LLDEPTTGLD 646
Cdd:PLN03140 1042 FMDEPTSGLD 1051
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1306-1491 |
1.08e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITkPTAGEVELKGCS------SVLGHL-GY-CPQENVL-----WPMLTLr 1372
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPleawsaAELARHrAYlSQQQTPPfampvFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 eHLEVyaavkGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSP-------VLLLDEPSTGIDP 1445
Cdd:PRK03695 93 -HQPD-----KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27436953 1446 TGQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK03695 167 AQQAALDRLLSELCQQG-IAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
495-710 |
1.17e-11 |
|
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: 69.77 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 495 EALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDiLTVK 574
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHTLRQFINYLPQEPYIFS-GSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 575 ENLSLFAKiKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSE-------GQKRKLTFGITILGDPQILLLDEPTTGLDP 647
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEegssisgGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 648 FSRDQVWSLLRERRaDHVILFSTQSMDEADiLADRKVIMSNGRLKCAGSSMFLKRRWGLGYHL 710
Cdd:TIGR01193 645 ITEKKIVNNLLNLQ-DKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1304-1496 |
1.54e-11 |
|
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: 65.59 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSI----RMISgitkPTAGEVELKGCS-SVLG------HLGYCPQENVLWPMlTLR 1372
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILIDGVDiSKIGlhdlrsRISIIPQDPVLFSG-TIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHL---------EVYAAVKglrkadaRLAIARLVSAfkLHEQLNVPVQK----LTAGITRKLCFVLSLLGNSPVLLLDEP 1439
Cdd:cd03244 96 SNLdpfgeysdeELWQALE-------RVGLKEFVES--LPGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1440 STGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLaEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:cd03244 167 TASVDPETDALIQKTIREAFKD--CTVLTIAHRL-DTIIDSDRILVLDKGRVVEFDS 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1301-1490 |
4.37e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.01 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1301 IAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGHLGYCPQ--------ENV-LWPMLTL 1371
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG-QHIEGLPGHQIArmgvvrtfQHVrLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHLEVYA-------------AVKGLRKADaRLAIARLVSAFK---LHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLL 1435
Cdd:PRK11300 98 IENLLVAQhqqlktglfsgllKTPAFRRAE-SEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 1436 LDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1310-1487 |
4.47e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.50 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1310 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVE--LKgcssvlghLGYCPQE-NVLWPMlTLREHLevYAAVKglRK 1386
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedLK--------ISYKPQYiSPDYDG-TVEEFL--RSANT--DD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1387 ADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGV 1466
Cdd:COG1245 430 FGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTA 509
|
170 180
....*....|....*....|.
gi 27436953 1467 LLTTHNLAEAEALCDRvaIMV 1487
Cdd:COG1245 510 MVVDHDIYLIDYISDR--LMV 528
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1315-1496 |
4.54e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1315 ILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlghLGYCPQEnvlwpMLTLREHL------------------E 1376
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-----LDYSKRG-----LLALRQQVatvfqdpeqqifytdidsD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 VYAAVKGLRKADARlaIAR-------LVSAFKLHEQlnvPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1449
Cdd:PRK13638 99 IAFSLRNLGVPEAE--ITRrvdealtLVDAQHFRHQ---PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27436953 1450 QMWQAIQAVVKNTERgVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:PRK13638 174 QMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
502-691 |
5.66e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEI----------RKITGVCPQFNVQFD-- 569
Cdd:PRK10982 269 FDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalvteeRRSTGIYAYLDIGFNsl 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 570 ILTVKENLSLFAKIKGIHLKEVEQEVqrilleLDMQNI----QDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGL 645
Cdd:PRK10982 349 ISNIRNYKNKVGLLDNSRMKSDTQWV------IDSMRVktpgHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27436953 646 DPFSRDQVWSLLRE-RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK10982 423 DVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1304-1491 |
6.65e-11 |
|
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: 64.03 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLGH------LGYCPQENVLWPMlTLREHL- 1375
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkPISQYEHkylhskVSLVGQEPVLFAR-SLQDNIa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 ---------EVYAAVKglrKADARLAIARLVSAFklHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1446
Cdd:cd03248 110 yglqscsfeCVKEAAQ---KAHAHSFISELASGY--DTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 1447 GQQQMWQAIQAvvKNTERGVLLTTHNLAEAEAlCDRVAIMVSGRL 1491
Cdd:cd03248 185 SEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1300-1538 |
6.69e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.72 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLGH------LGYCPQen 1363
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeykRAKYIGRvfqdpmMGTAPS-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1364 vlwpmLTLREHLEVyAAVKG----LRKA--DARLAIAR-LVSAFK--LHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVL 1434
Cdd:COG1101 97 -----MTIEENLAL-AYRRGkrrgLRRGltKKRRELFReLLATLGlgLENRLDTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1435 LLDEPSTGIDP-TGQQQMwQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLrcigsiqhlknklgkdyILELK 1513
Cdd:COG1101 171 LLDEHTAALDPkTAALVL-ELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI-----------------ILDVS 232
|
250 260
....*....|....*....|....*
gi 27436953 1514 VKETSQVTLvhTEILKLFPQAAGQE 1538
Cdd:COG1101 233 GEEKKKLTV--EDLLELFEEIRGEE 255
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
467-690 |
7.18e-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: 66.77 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 467 PVAPEFQGKEA-IRIRNVKKEYKGKSgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL 545
Cdd:COG5265 346 PDAPPLVVGGGeVRFENVSFGYDPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 546 SEMQdLEEIRKITGVCPQ----FNvqfDilTVKENLSlFAKIkGIHLKEVEQEVQrilleldMQNIQDNLAK-------- 613
Cdd:COG5265 423 RDVT-QASLRAAIGIVPQdtvlFN---D--TIAYNIA-YGRP-DASEEEVEAAAR-------AAQIHDFIESlpdgydtr 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 614 ------HLSEGQKRKLtfGI--TILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH---VI---LfSTqSMDeadil 679
Cdd:COG5265 488 vgerglKLSGGEKQRV--AIarTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRttlVIahrL-ST-IVD----- 558
|
250
....*....|.
gi 27436953 680 ADRKVIMSNGR 690
Cdd:COG5265 559 ADEILVLEAGR 569
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1299-1503 |
8.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1299 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-----------KGCSSVLGHLGYCPQ--ENVL 1365
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetgnKNLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1366 WPMlTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQL-NVPVQKLTAGITRKLCfVLSLLGNSP-VLLLDEPSTGI 1443
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVA-IAGVMAYEPeILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1444 DPTGQQQMWQaiqaVVKNTERG---VLLTTHNLAEAEALCDRVAIMVSGRLrcigsIQHLKNK 1503
Cdd:PRK13641 177 DPEGRKEMMQ----LFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1304-1532 |
9.21e-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: 64.49 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSS----SIRMISgitkpTAGEVELKGCSSVLGHL-------GYCPQENVLWPMlTLR 1372
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGDIQIDGVSWNSVPLqkwrkafGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKG--LRKADARLAIARLVSAF--KLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTgq 1448
Cdd:cd03289 95 KNLDPYGKWSDeeIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1449 qqMWQAIQAVVKNTERG--VLLTTHNLaEAEALCDRVAIMVSGRLRCIGSIQHLKNKlgkdyilelkvKETSQVTLVHTE 1526
Cdd:cd03289 173 --TYQVIRKTLKQAFADctVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFKQAISPSD 238
|
....*.
gi 27436953 1527 ILKLFP 1532
Cdd:cd03289 239 RLKLFP 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
481-690 |
9.70e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 63.05 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 481 RNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPT---EGSVTiYNkNLSEMQDLEEIRKI 557
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIH-YN-GIPYKEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGihlkeveqevqrilleldmqniqDNLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 638 LDEPTTGLDPFSRDQVWSLLRE--RRADHVILFS-TQSMDEADILADRKVIMSNGR 690
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTmaDVLKTTTFVSlYQASDEIYDLFDKVLVLYEGR 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
478-691 |
1.06e-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: 66.25 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNILNGLSVPTEGSVTIYNKNLSEM--QDL 551
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLseREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 552 EEIR--KI--------TGVCPQFNV--QfdiltVKENLSLFAKIKGihlkevEQEVQRILLELDMQNIQDNLAK-----H 614
Cdd:COG4172 87 RRIRgnRIamifqepmTSLNPLHTIgkQ-----IAEVLRLHRGLSG------AAARARALELLERVGIPDPERRldaypH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 615 -LSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADH--VILFSTQsmdeaDI-----LADRKVIM 686
Cdd:COG4172 156 qLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITH-----DLgvvrrFADRVAVM 230
|
....*
gi 27436953 687 SNGRL 691
Cdd:COG4172 231 RQGEI 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1304-1505 |
1.21e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.00 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------------SVLghlgycPQENVLWPMlT 1370
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseaalrqaiSVV------SQRVHLFSA-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHLEVYAAvkglRKADARL-AIARLVSAFKLHEQ---LNVPV----QKLTAGITRKLCFVLSLLGNSPVLLLDEPSTG 1442
Cdd:PRK11160 430 LRDNLLLAAP----NASDEALiEVLQQVGLEKLLEDdkgLNAWLgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1443 IDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAEALcDRVAIMVSGRLRCIGSIQHLKNKLG 1505
Cdd:PRK11160 506 LDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1305-1521 |
1.51e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.98 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcsSVLGHLgyCPQENVlWpmlTLREHLE-------- 1376
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI------IIDGDL--LTEENV-W---DIRHKIGmvfqnpdn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 --VYAAV----------KGLRKADARLAIAR---LV--SAFKLHEQlnvpvQKLTAGITRKLCFVLSLLGNSPVLLLDEP 1439
Cdd:PRK13650 93 qfVGATVeddvafglenKGIPHEEMKERVNEaleLVgmQDFKEREP-----ARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1440 STGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQHLKNKLGKDYILELKVKETSQ 1519
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGLDIPFTTS 246
|
..
gi 27436953 1520 VT 1521
Cdd:PRK13650 247 LV 248
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
478-691 |
1.64e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYK-----GKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLE 552
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL-NRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 553 EIR------------KITGVCPQFNVQfDILtvKENLSlfakikgiHL---KEVEQE--VQRILLELDMQ-NIQDNLAKH 614
Cdd:PRK10419 83 QRKafrrdiqmvfqdSISAVNPRKTVR-EII--REPLR--------HLlslDKAERLarASEMLRAVDLDdSVLDKRPPQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 615 LSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
496-732 |
1.84e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 496 ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemQDLEEirKITGVCPQFN-VQFDILTVK 574
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQK--NLVAYVPQSEeVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 575 ENLSLFAKIKGIHL-----KEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFS 649
Cdd:PRK15056 98 EDVVMMGRYGHMGWlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 650 RDQVWSLLRERRAD-HVILFSTQSMDEADILADRKV-----IMSNGRLKCAGSSMFLKRRW-GLGYHLSLHRNEicnpEQ 722
Cdd:PRK15056 178 EARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVmvkgtVLASGPTETTFTAENLELAFsGVLRHVALNGSE----ES 253
|
250
....*....|....*
gi 27436953 723 ITS-----FITHHIP 732
Cdd:PRK15056 254 IITdderpFISHRPA 268
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
469-710 |
1.98e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.51 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 469 APEF-QGKeaIRIRNVKKEYKGKSgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSE 547
Cdd:TIGR00958 471 APLNlEGL--IEFQDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 548 MqDLEEIRKITGVCPQFNVQFDiLTVKENLSL---FAKIKGIHLKEVEQEVQRILLELDmQNIQDNLAKH---LSEGQKR 621
Cdd:TIGR00958 548 Y-DHHYLHRQVALVGQEPVLFS-GSVRENIAYgltDTPDEEIMAAAKAANAHDFIMEFP-NGYDTEVGEKgsqLSGGQKQ 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 622 KLTFGITILGDPQILLLDEPTTGLDPfsrdQVWSLLRE--RRADHVILFSTQSMDEADiLADRKVIMSNGRLKCAGSSMF 699
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDA----ECEQLLQEsrSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQ 699
|
250
....*....|.
gi 27436953 700 LKRRWGLGYHL 710
Cdd:TIGR00958 700 LMEDQGCYKHL 710
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1305-1490 |
2.02e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKS----SSIRMISgiTKP---TAGEVELKGcSSVL------------GHLGYCPQENV- 1364
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPvvyPSGDIRFHG-ESLLhaseqtlrgvrgNKIAMIFQEPMv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1365 -LWPMLTLREHL-EVYAAVKGLRKADARLAIARLVSAFKLHE---QLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEP 1439
Cdd:PRK15134 104 sLNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27436953 1440 STGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1304-1491 |
2.04e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV-----ELKGCSSV----LGhLGYCPQEN----------V 1364
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRImlngkEINALSTAqrlaRG-LVYLPEDRqssglyldapL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1365 LWPMLTLREH--------------LEVYAAVKGLRKADArlaiarlvsafklhEQlnvPVQKLTAGITRKLCFVLSLLGN 1430
Cdd:PRK15439 359 AWNVCALTHNrrgfwikparenavLERYRRALNIKFNHA--------------EQ---AARTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1431 SPVLLLDEPSTGIDPTGQQQMWQAIQAVVK-NTerGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAqNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1302-1490 |
2.07e-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: 62.45 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLGYCPQEnvlwpMLTLREH------- 1374
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPRE-----ILALRRRtigyvsq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 ----------LEVYAA---VKGLRKADARLAIARLVSAFKLHEQL-NVPVQKLTAG------ITRklcfvlSLLGNSPVL 1434
Cdd:COG4778 101 flrviprvsaLDVVAEpllERGVDREEARARARELLARLNLPERLwDLPPATFSGGeqqrvnIAR------GFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1435 LLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
492-695 |
2.08e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.86 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVcPQ-----FNv 566
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV-PQdtslsFE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 567 qFDILTVKE-----NLSLFAKIKGIHLKEVEQEVQRIllelDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEP 641
Cdd:PRK09536 92 -FDVRQVVEmgrtpHRSRFDTWTETDRAAVERAMERT----GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 642 TTGLDPFSRDQVWSLLRERRAD-HVILFSTQSMDEADILADRKVIMSNGRLKCAG 695
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1300-1497 |
2.17e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.53 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---------CSSVLGHLGYCPQenvlWPMLT 1370
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvkLSDIRKKVGLVFQ----YPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHlEVYAAVK------GLRKADARLAIARLVSAFKL-HEQL--NVPVQkLTAGITRKLCFVLSLLGNSPVLLLDEPST 1441
Cdd:PRK13637 96 LFEE-TIEKDIAfgpinlGLSEEEIENRVKRAMNIVGLdYEDYkdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1442 GIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSI 1497
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1310-1485 |
2.31e-10 |
|
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: 61.43 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1310 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlgYCPQEnvlwpmltlrehlevyaavkglrkada 1389
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-----YKPQY--------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1390 rlaiarlvsafklheqlnvpvQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLT 1469
Cdd:cd03222 70 ---------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVV 128
|
170
....*....|....*.
gi 27436953 1470 THNLAEAEALCDRVAI 1485
Cdd:cd03222 129 EHDLAVLDYLSDRIHV 144
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1302-1496 |
2.65e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.08 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV-----------ELKGCSSVLGHLGYCPQENVLWPmlT 1370
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsKLQGIRKLVGIVFQNPETQFVGR--T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGitRKLCFVLS-LLGNSP-VLLLDEPSTGIDPTGQ 1448
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGG--QGQCVALAgILTMEPeCLIFDEVTSMLDPDSG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27436953 1449 QQMWQAIQavvKNTERG--VLLTTHNLAEAEAlCDRVAIMVSGRLRCIGS 1496
Cdd:PRK13644 173 IAVLERIK---KLHEKGktIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1304-1491 |
2.66e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGH----------------------LGYCPQ 1361
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglangivyisedrkrdglvLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1362 ENVlwpMLTLREHLEvYAAVKgLRKADARLAIARLVSAFKLH----EQlnvPVQKLTAGITRKLCFVLSLLGNSPVLLLD 1437
Cdd:PRK10762 349 ENM---SLTALRYFS-RAGGS-LKHADEQQAVSDFIRLFNIKtpsmEQ---AIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27436953 1438 EPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQ-FKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
477-646 |
2.73e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKSGKVeaLKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 556
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF-GLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFNVQFDiLTVKENLSLFAK---------IKGIHLKEVeqeVQRILLELDMQNIQDnlAKHLSEGQKRKLTFGI 627
Cdd:PLN03130 1314 VLGIIPQAPVLFS-GTVRFNLDPFNEhndadlwesLERAHLKDV---IRRNSLGLDAEVSEA--GENFSVGQRQLLSLAR 1387
|
170
....*....|....*....
gi 27436953 628 TILGDPQILLLDEPTTGLD 646
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVD 1406
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1305-1500 |
2.99e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG---CSSVLGHLGYCP--QENVLWPMLTLREHLEVYA 1379
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQRDICMvfQSYALFPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1380 AVKGLRKADARlaiARLVSAFKLHEQLNVP---VQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQ 1456
Cdd:PRK11432 104 KMLGVPKEERK---QRVKEALELVDLAGFEdryVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 1457 AVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK11432 181 ELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1306-1491 |
3.42e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTA-----GEVELKGCSSVLG----------HLGYCPQENVLWPMLT 1370
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTARSLSQqkglirqlrqHVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREH-LEVYAAVKGLRKADArLAIAR-LVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1448
Cdd:PRK11264 102 VLENiIEGPVIVKGEPKEEA-TARAReLLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 1449 QQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK11264 181 GEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
478-697 |
4.24e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL----SVPtEGSVTIYNKNLSE----MQ 549
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSA-GSHIELLGRTVQRegrlAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 550 DLEEIRKITG-VCPQFNVqFDILTVKEN---------------LSLFAKIKgihlkevEQEVQRILLELDMQNIQDNLAK 613
Cdd:PRK09984 80 DIRKSRANTGyIFQQFNL-VNRLSVLENvligalgstpfwrtcFSWFTREQ-------KQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 614 HLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE-RRADHVILFST-QSMDEADILADRKVIMSNGRL 691
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTlHQVDYALRYCERIVALRQGHV 231
|
....*.
gi 27436953 692 KCAGSS 697
Cdd:PRK09984 232 FYDGSS 237
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
478-640 |
4.35e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.14 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVEALKGLL----------------FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiy 541
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDLFfrskdgeyhyalnnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 542 nknlsemqDLEEIRKITGVCPQFNVQfdiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKR 621
Cdd:PRK13545 82 --------DIKGSAALIAISSGLNGQ---LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKS 150
|
170
....*....|....*....
gi 27436953 622 KLTFGITILGDPQILLLDE 640
Cdd:PRK13545 151 RLGFAISVHINPDILVIDE 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1305-1474 |
5.12e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKgcSSVlgHLGYCPQEnvlwpmltlREHLE----VYAA 1380
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETV--KLAYVDQS---------RDALDpnktVWEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1381 VK--------GLRKADARLAIARLvsAFKLHEQlNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1452
Cdd:TIGR03719 407 ISggldiiklGKREIPSRAYVGRF--NFKGSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALE 483
|
170 180
....*....|....*....|....*....
gi 27436953 1453 QAIQ-----AVVKNTERGVL--LTTHNLA 1474
Cdd:TIGR03719 484 EALLnfagcAVVISHDRWFLdrIATHILA 512
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
502-675 |
5.59e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDlEEIRKITGVCPQFNVQF-DilTVKENLSLF 580
Cdd:PRK10247 28 FSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFgD--TVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 581 AKIKGIH--LKEVEQEVQRILLELDM--QNIQDnlakhLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSL 656
Cdd:PRK10247 105 WQIRNQQpdPAIFLDDLERFALPDTIltKNIAE-----LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
|
170 180
....*....|....*....|.
gi 27436953 657 LRERRADHVI--LFSTQSMDE 675
Cdd:PRK10247 180 IHRYVREQNIavLWVTHDKDE 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1310-1487 |
5.78e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1310 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV--ELKgcssvlghLGYCPQEnvlwpmLTLREHLEVYAAvkgLRKA 1387
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpELK--------ISYKPQY------IKPDYDGTVEDL---LRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1388 DARLA----IARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTE 1463
Cdd:PRK13409 425 TDDLGssyyKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEERE 504
|
170 180
....*....|....*....|....
gi 27436953 1464 RGVLLTTHNLAEAEALCDRvaIMV 1487
Cdd:PRK13409 505 ATALVVDHDIYMIDYISDR--LMV 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1310-1486 |
5.83e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1310 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcssvlghlgycPQENVL--WPMLTLREHLE-VYA------- 1379
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEP-----------SWDEVLkrFRGTELQNYFKkLYNgeikvvh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1380 ----------AVKG-----LRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:PRK13409 165 kpqyvdlipkVFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 1445 PTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAEALCDRVAIM 1486
Cdd:PRK13409 245 IRQRLNVARLIRELAEG--KYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
467-696 |
6.30e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 467 PVAPEFQGKEAIRIRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNILNGLSVPTE-GSVTIY 541
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQcDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 542 NKN-----LSEMQD--LEEIR----------KITGVCPQFNVQFDIltvKENLSLFakiKGIHLKEVEQEVQRILLELDM 604
Cdd:PRK10261 82 RRSrqvieLSEQSAaqMRHVRgadmamifqePMTSLNPVFTVGEQI---AESIRLH---QGASREEAMVEAKRMLDQVRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 605 QNIQDNLAKH---LSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLR--ERRADHVILFSTQSMDEADIL 679
Cdd:PRK10261 156 PEAQTILSRYphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEI 235
|
250
....*....|....*..
gi 27436953 680 ADRKVIMSNGRLKCAGS 696
Cdd:PRK10261 236 ADRVLVMYQGEAVETGS 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1302-1500 |
7.50e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.43 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP---TAGEVELKGcSSVLG----HLGYCPQENVLW----PMLT 1370
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNG-REILNlpekELNKLRAEQISMifqdPMTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHL-------EVYAAVKGLRKADARLAIARLVSAFKLHE---QLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPS 1440
Cdd:PRK09473 110 LNPYMrvgeqlmEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1441 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
478-690 |
7.76e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 60.18 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSGKVE-ALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKnlsemqdleeirk 556
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 iTGVCPQFN-VQFDilTVKENLsLFakikgiHLKEVEQEVQRIL----LELDMQNIQDNLAKH-------LSEGQKRKLT 624
Cdd:cd03250 68 -IAYVSQEPwIQNG--TIRENI-LF------GKPFDEERYEKVIkacaLEPDLEILPDGDLTEigekginLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 625 FGITILGDPQILLLDEPTTGLDPFSRDQVW-SLLRERRADH--VILfSTQSMdeaDIL--ADRKVIMSNGR 690
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNktRIL-VTHQL---QLLphADQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1304-1490 |
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 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTA---GEVELKG------CSSVLGHLGYCPQENVLWPMLTLREH 1374
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGipykefAEKYPGEIIYVSEEDVHFPTLTVRET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 LEVYAAVKGlrkadarlaiarlvsafklheqlNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1454
Cdd:cd03233 104 LDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 27436953 1455 IQAVVKNTERGVLLTTHNLA-EAEALCDRVAIMVSGR 1490
Cdd:cd03233 161 IRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGR 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-669 |
9.27e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLsVPTEGSVTIYNKNLSEMQdLEEIRKITGVCPQFNVQFDiLTVKEN 576
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFGVIPQKVFIFS-GTFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 577 LSLFAKIKGIHLKEVEQEVQ-RILLE-----LDMQNIQDNLAkhLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSR 650
Cdd:TIGR01271 1312 LDPYEQWSDEEIWKVAEEVGlKSVIEqfpdkLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTL 1389
|
170
....*....|....*....
gi 27436953 651 DQVWSLLRERRADHVILFS 669
Cdd:TIGR01271 1390 QIIRKTLKQSFSNCTVILS 1408
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1304-1505 |
9.32e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.59 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPM-------- 1368
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydHHYLHRQVALVGQEPVLFSGsvreniay 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1369 -LTLREHLEVYAAVKglrKADARLAIARLVSAFklHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDptg 1447
Cdd:TIGR00958 578 gLTDTPDEEIMAAAK---AANAHDFIMEFPNGY--DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD--- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1448 qQQMWQAIQAVVKNTERGVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLG 1505
Cdd:TIGR00958 650 -AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1302-1491 |
9.60e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGH-LGYCPQENVLWPMLTLRE 1373
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqTAKIMREaVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HLevyaAVKGL--RKADARLAIARLVSAF-KLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1450
Cdd:PRK11614 100 NL----AMGGFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 1451 MWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK11614 176 IFDTIEQL---REQGmtIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
479-690 |
9.74e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 479 RIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtIYNKNLSEMQDLEEI---- 554
Cdd:PRK11701 8 SVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-HYRMRDGQLRDLYALseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 -----RKITGVCPQF-------------NVQFDILTVKENlsLFAKIKGIH---LKEVEQEVQRIlleldmqniqDNLAK 613
Cdd:PRK11701 83 rrrllRTEWGFVHQHprdglrmqvsaggNIGERLMAVGAR--HYGDIRATAgdwLERVEIDAARI----------DDLPT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 614 HLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGR 690
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1299-1509 |
1.03e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.94 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1299 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMIS--GITKPtagEVELKGCSSVLGHLGYCPQENVL----------- 1365
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNP---EVTITGSIVYNGHNIYSPRTDTVdlrkeigmvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1366 ----WPMlTLREHLevyaaVKGLR----KADARLAIA---RLVSAF---KLHEQLNVPVQKLTAGITRKLCfVLSLLGNS 1431
Cdd:PRK14239 94 qpnpFPM-SIYENV-----VYGLRlkgiKDKQVLDEAvekSLKGASiwdEVKDRLHDSALGLSGGQQQRVC-IARVLATS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1432 P-VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTErgVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL----KNKLGK 1506
Cdd:PRK14239 167 PkIILLDEPTSALDPISAGKIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMfmnpKHKETE 244
|
...
gi 27436953 1507 DYI 1509
Cdd:PRK14239 245 DYI 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1304-1491 |
1.36e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS----SV-----LGhLGYCPQE---NVLWPMLTL 1371
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitglSPrerrrLG-VAYIPEDrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHL-----EVYAAVKG--LRKADARLAIARLVSAFKL-HEQLNVPVQKLTAGITRKlcFVLS--LLGNSPVLLLDEPST 1441
Cdd:COG3845 354 AENLilgryRRPPFSRGgfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQK--VILAreLSRDPKLLIAAQPTR 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27436953 1442 GIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG3845 432 GLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
477-691 |
1.48e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKgkSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRK 556
Cdd:PLN03232 1234 SIKFEDVHLRYR--PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF-GLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFNVQFDiLTVKENLSLFAK------IKGIHLKEVEQEVQRILLELDMQNIQDnlAKHLSEGQKRKLTFGITIL 630
Cdd:PLN03232 1311 VLSIIPQSPVLFS-GTVRFNIDPFSEhndadlWEALERAHIKDVIDRNPFGLDAEVSEG--GENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 631 GDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEAdILADRKVIMSNGRL 691
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQV 1447
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1296-1471 |
1.48e-09 |
|
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: 59.18 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1296 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSS-----SIRMISGITKptaGEVELKG---CSSVLGHLGYCPQENVLWP 1367
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlAGRKTAGVIT---GEILINGrplDKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLEVYAAVKGL----RKadaRLAIA-RLVSafklheqlnvpvqkltagitrklcfvlsllgnSPVLL-LDEPST 1441
Cdd:cd03232 93 NLTVREALRFSALLRGLsveqRK---RLTIGvELAA--------------------------------KPSILfLDEPTS 137
|
170 180 190
....*....|....*....|....*....|..
gi 27436953 1442 GIDptgQQQMWQAIQAVVK--NTERGVLLTTH 1471
Cdd:cd03232 138 GLD---SQAAYNIVRFLKKlaDSGQAILCTIH 166
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1286-1496 |
1.59e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1286 YAGQKKSCFSKRkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV---------------ELKGCS 1350
Cdd:PRK13645 14 YTYAKKTPFEFK----ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipanlkkikEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1351 SVLGHLGYCPQENVLWPmlTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQL--NVPVQkLTAGITRKLCF--VLS 1426
Cdd:PRK13645 90 KEIGLVFQFPEYQLFQE--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYvkRSPFE-LSGGQKRRVALagIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1427 LLGNSpvLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:PRK13645 167 MDGNT--LVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1294-1492 |
2.25e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKpTAGEVELKGCSSVLGHLGYCPQENV--------- 1364
Cdd:PRK14258 15 FYYDTQKIL-EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1365 ------LWPMlTLREHLEVYAAVKGLR-KADARLAIARLVSAFKLHEQLNVPVQK----LTAGITRKLCFVLSLLGNSPV 1433
Cdd:PRK14258 93 vhpkpnLFPM-SVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1434 LLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLR 1492
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1304-1478 |
2.49e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.03 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP---TAGEVELKGCSSVLG-----HLGYCPQENVLWPMLTLREHL 1375
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALpaeqrRIGILFQDDLLFPHLSVGENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 eVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQM---- 1451
Cdd:COG4136 98 -AFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFrefv 176
|
170 180
....*....|....*....|....*....
gi 27436953 1452 WQAIQavvkntERG--VLLTTHNLAEAEA 1478
Cdd:COG4136 177 FEQIR------QRGipALLVTHDEEDAPA 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1302-1503 |
2.74e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.13 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYC---PQENVLwpMLTL 1371
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevnaenEKWVRSKVGLVfqdPDDQVF--SSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHLEVYAAVKGLRKA--DARLAIA-RLVSAFKLHEQlnvPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1448
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDevERRVEEAlKAVRMWDFRDK---PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 1449 QQMwQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1503
Cdd:PRK13647 175 ETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1304-1496 |
2.82e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 59.71 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC------SSVLG-HLGYCPQENVLWPMLTLREhLe 1376
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAkRLAILRQENHINSRLTVRE-L- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 V----YAAVKG-LRKADaRLAIARLVSAFKLHEQLNVPVQKLTAGiTRKLCFV-LSLLGNSPVLLLDEPSTGIDPTGQQQ 1450
Cdd:COG4604 96 VafgrFPYSKGrLTAED-REIIDEAIAYLDLEDLADRYLDELSGG-QRQRAFIaMVLAQDTDYVLLDEPLNNLDMKHSVQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27436953 1451 MWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:COG4604 174 MMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1298-1444 |
2.88e-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: 61.49 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1298 KKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQENVLWPMLTLREHLEv 1377
Cdd:TIGR03719 17 KKEIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKV----GYLPQEPQLDPTKTVRENVE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 yAAVKGLRKADARL-AI------------------ARL------VSAFKLHEQLNV------------PVQKLTAGITRK 1420
Cdd:TIGR03719 91 -EGVAEIKDALDRFnEIsakyaepdadfdklaaeqAELqeiidaADAWDLDSQLEIamdalrcppwdaDVTKLSGGERRR 169
|
170 180
....*....|....*....|....
gi 27436953 1421 LCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1503 |
2.93e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.00 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1290 KKSCFSKRK-KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSsvlghlgyCPQENVLWpm 1368
Cdd:PRK13632 11 ENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT--------ISKENLKE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1369 ltLREHLE----------VYAAV----------KGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCF--VLS 1426
Cdd:PRK13632 81 --IRKKIGiifqnpdnqfIGATVeddiafglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIasVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1427 LlgNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQH-LKNK 1503
Cdd:PRK13632 159 L--NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1299-1476 |
3.01e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1299 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMLTL 1371
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaSKEVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 RE--------HLEVYAAvkgLRKADARlAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGI 1443
Cdd:PRK10253 99 QElvargrypHQPLFTR---WRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 27436953 1444 DPTGQQQMWQAIQAVvkNTERGVLLTT--HNLAEA 1476
Cdd:PRK10253 175 DISHQIDLLELLSEL--NREKGYTLAAvlHDLNQA 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
497-646 |
3.02e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL--SVPTEGSVTIYNKNLSEmqdleEIRKITGVCPQFNVQFDILTVK 574
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 575 ENL---SLFAKIKGIHLKEVEQEVQRILLELDMQN-----IQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLD 646
Cdd:PLN03211 159 ETLvfcSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
478-696 |
3.12e-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: 58.31 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS--VPTEGSVTIYNKNLSEMQDLEEIR 555
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVCPQFNVQFDILTVKENL-SLFAKIKGIHLKEVEqevqriLLELDMQNiqdnlakhlsegqkrkltfgitilgdPQ 634
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLrYVNEGFSGGEKKRNE------ILQLLLLE--------------------------PD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 635 ILLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEAD-ILADRKVIMSNGRLKCAGS 696
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKsVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1310-1492 |
3.12e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1310 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS---------SVL--GHLGYCPQENVLWPMLTLREHLEVY 1378
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqmdeearAKLraKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1379 AAVKGLRKADARLAIARLVSAFKLHEQLN-VPVQkLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1457
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDhLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 27436953 1458 VVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRLR 1492
Cdd:PRK10584 192 LNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1304-1496 |
3.26e-09 |
|
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: 58.58 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSV-LGHL----GYCPQENVLWpMLTLREHLE 1376
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidISTIpLEDLrsslTIIPQDPTLF-SGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 VYAavkglRKADARLAIARLVSAFKLHeqlnvpvqkLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDptgqQQMWQAIQ 1456
Cdd:cd03369 104 PFD-----EYSDEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASID----YATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 1457 AVVKNTERG--VLLTTHNLAEAeALCDRVAIMVSGRLRCIGS 1496
Cdd:cd03369 166 KTIREEFTNstILTIAHRLRTI-IDYDKILVMDAGEVKEYDH 206
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1310-1486 |
3.45e-09 |
|
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: 59.30 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1310 VQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLGHLGYCPQENVLWPML--TLREHL------EVYAA 1380
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdWDEILDEFRGSELQNYFTKLLegDVKVIVkpqyvdLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1381 VKG-----LRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1455
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170 180 190
....*....|....*....|....*....|.
gi 27436953 1456 QAVVKNtERGVLLTTHNLAEAEALCDRVAIM 1486
Cdd:cd03236 183 RELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
476-692 |
4.14e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 476 EAIRIRNVKKEY----------------KGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT 539
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 540 IYNknlsemqDLEEIRKITGVCPQfnvqfdiLTVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQ 619
Cdd:PRK13546 83 RNG-------EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 620 KRKLTFGITILGDPQILLLDEP-TTGLDPFSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRLK 692
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
455-690 |
5.56e-09 |
|
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: 60.85 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 455 IDAEhPSddyFEPVAPEFQGKEAIRIRNVKKEYKGKSG-------KVEALKGLLFDIYEGQITAILGHSGAGKSSL-LNI 526
Cdd:COG4172 257 LAAE-PR---GDPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 527 LnGLsVPTEGSVTIYNKNLSEM--QDLEEIRKitgvcpQFNVQF--------------DILTvkENLslfaKIKGIHL-- 588
Cdd:COG4172 333 L-RL-IPSEGEIRFDGQDLDGLsrRALRPLRR------RMQVVFqdpfgslsprmtvgQIIA--EGL----RVHGPGLsa 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 589 KEVEQEVQRILLELDMqniqDNLAKH-----LSEGQK------RKLtfgitILgDPQILLLDEPTTGLDPFSRDQVWSLL 657
Cdd:COG4172 399 AERRARVAEALEEVGL----DPAARHrypheFSGGQRqriaiaRAL-----IL-EPKLLVLDEPTSALDVSVQAQILDLL 468
|
250 260 270
....*....|....*....|....*....|....*
gi 27436953 658 RERRADHVI--LFSTQSMDEADILADRKVIMSNGR 690
Cdd:COG4172 469 RDLQREHGLayLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1300-1505 |
5.77e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITkPTAGEVELKGC-------SSVLGHLGYCPQEnvlwPML--- 1369
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldpESWRKHLSWVGQN----PQLphg 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHL----------EVYAAvkgLRKADARLAIARLVSAfklheqLNVPVQKLTAGIT----RKLCFVLSLLGNSPVLL 1435
Cdd:PRK11174 438 TLRDNVllgnpdasdeQLQQA---LENAWVSEFLPLLPQG------LDTPIGDQAAGLSvgqaQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1436 LDEPSTGIDPTGQQQMWQAIQAVVKNTErgVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLG 1505
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQT--TLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1304-1532 |
5.78e-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: 61.08 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSsirMISGITK--PTAGEVELKGCS--SVL-----GHLGYCPQENVLWPMlTLREH 1374
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRllSTEGEIQIDGVSwnSVTlqtwrKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 LEVYA--AVKGLRKADARLAIARLVSAF--KLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1450
Cdd:TIGR01271 1312 LDPYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQI 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1451 MWQAIQAVVKNTErgVLLTTHNLaEAEALCDRVAIMVSGRLRCIGSIQHLKNklgkdyilelkvkETSQVTLV--HTEIL 1528
Cdd:TIGR01271 1392 IRKTLKQSFSNCT--VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLN-------------ETSLFKQAmsAADRL 1455
|
....
gi 27436953 1529 KLFP 1532
Cdd:TIGR01271 1456 KLFP 1459
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1304-1490 |
6.12e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.86 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSsirMISGITkptaGEVE-LKGCSSVLGHLGYCPQ----------ENVLW--PML- 1369
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSS---LLSALL----GELEkLSGSVSVPGSIAYVSQepwiqngtirENILFgkPFDe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 ----------TLREHLEVYAA-------VKGL-----RKadARLAIARlvsafklheqlnvpvqkltagitrklcfvlSL 1427
Cdd:cd03250 95 eryekvikacALEPDLEILPDgdlteigEKGInlsggQK--QRISLAR------------------------------AV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 1428 LGNSPVLLLDEPSTGIDP-TGQQQMWQAIQAVVKNtERGVLLTTHNLAEAEAlCDRVAIMVSGR 1490
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAhVGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1305-1492 |
6.31e-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: 60.61 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGiTKPTAGE---------VELKGCSSVLGH-----------LGYCPQ--- 1361
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEgnvfingkpVDIRNPAQAIRAgiamvpedrkrHGIVPIlgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1362 -ENVLWPML---TLREHLEVYAAVKGLRKADARLAIaRLVSAFklheqlnVPVQKLTAGITRKLCFVLSLLGNSPVLLLD 1437
Cdd:TIGR02633 357 gKNITLSVLksfCFKMRIDAAAELQIIGSAIQRLKV-KTASPF-------LPIGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1438 EPSTGIDPTGQQQMWQAIQAVVKnteRGV--LLTTHNLAEAEALCDRVAIMVSGRLR 1492
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
507-646 |
6.57e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.65 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 507 GQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVcPQFNVQFDILTVKENLSL----FAK 582
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL-PQQLPAAEGMTVRELVAIgrypWHG 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 583 IKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLD 646
Cdd:PRK10575 116 ALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1297-1505 |
6.80e-09 |
|
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: 58.32 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMl 1369
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnLRWLRSQIGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHL----------EVYAAVKglrKADARLAIArlvsafKLHEQLNVPV----QKLTAGITRKLCFVLSLLGNSPVLL 1435
Cdd:cd03249 92 TIAENIrygkpdatdeEVEEAAK---KANIHDFIM------SLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1436 LDEPSTGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAEAEAlCDRVAIMVSGRLRCIGSIQHLKNKLG 1505
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKG--RTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
478-646 |
6.95e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKSgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNK-NLSEMqDLEEIRK 556
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDI-NLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQ----------FNVQFDILTVKE---------------------NLSLFAKIKG--------------IHLK-- 589
Cdd:PTZ00265 461 KIGVVSQdpllfsnsikNNIKYSLYSLKDlealsnyynedgndsqenknkRNSCRAKCAGdlndmsnttdsnelIEMRkn 540
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436953 590 -------EVEQEVQRILLELDMQNIQDNL-------AKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLD 646
Cdd:PTZ00265 541 yqtikdsEVVDVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1304-1495 |
7.53e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.66 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGE----------VELKGCSsvlghLGYCPQENVLWPMLTLRE 1373
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDlfigekrmndVPPAERG-----VGMVFQSYALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HLEVYAAVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQ 1453
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27436953 1454 AIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIG 1495
Cdd:PRK11000 175 EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1286-1512 |
7.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.64 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1286 YAGQKKSCFSKRkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-----------KGCSSVLG 1354
Cdd:PRK13646 10 YTYQKGTPYEHQ----AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditithktkdKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1355 HLGYCPQ--ENVLWPMLTLREHLEVYAAVK-GLRKADARlaiarlvsAFKLHEQL----NV----PVQkLTAGITRKLCF 1423
Cdd:PRK13646 86 RIGMVFQfpESQLFEDTVEREIIFGPKNFKmNLDEVKNY--------AHRLLMDLgfsrDVmsqsPFQ-MSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1424 VLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1503
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
250
....*....|.
gi 27436953 1504 LGK--DYILEL 1512
Cdd:PRK13646 237 KKKlaDWHIGL 247
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1286-1496 |
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 27436953 1286 YAGQKKSCFSKRkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV--------------ELKGCSS 1351
Cdd:PRK13643 9 YTYQPNSPFASR----ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstskqkEIKPVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1352 VLGHLGYCPQENVLWPmlTLREHLEVYAAVKGLRKADARLAIARLVSAFKLHEQL--NVPVQkLTAGITRKLCFVLSLLG 1429
Cdd:PRK13643 85 KVGVVFQFPESQLFEE--TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFweKSPFE-LSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1430 NSPVLLLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
480-659 |
9.05e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYKGKSGK---------VEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQD 550
Cdd:PRK15079 11 VADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 551 LE--EIRK---------ITGVCPQFNVQfDIltVKENLSLFAkiKGIHLKEVEQEVQRILLELDM-QNIQDNLAKHLSEG 618
Cdd:PRK15079 91 DEwrAVRSdiqmifqdpLASLNPRMTIG-EI--IAEPLRTYH--PKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 619 QKRKLtfGIT---ILgDPQILLLDEPTTGLDPFSRDQVWSLLRE 659
Cdd:PRK15079 166 QCQRI--GIAralIL-EPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1285-1500 |
9.22e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.49 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1285 EYAGQKKSCFSKRkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVelkgcssvlgHLGycpqENV 1364
Cdd:PRK13634 9 EHRYQYKTPFERR----ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV----------TIG----ERV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1365 LWP------MLTLR----------EHLEVYAAVK----------GLRKADARLAIARLVSAFKLHEQL--NVPVQkLTAG 1416
Cdd:PRK13634 71 ITAgkknkkLKPLRkkvgivfqfpEHQLFEETVEkdicfgpmnfGVSEEDAKQKAREMIELVGLPEELlaRSPFE-LSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1417 ITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
....
gi 27436953 1497 IQHL 1500
Cdd:PRK13634 230 PREI 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-677 |
9.33e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSE-----MQDLEEIRKITGVCPQfnvqfdiL 571
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctyQKQLCFVGHRSGINPY-------L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 TVKENlSLFakikGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRD 651
Cdd:PRK13540 90 TLREN-CLY----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180 190
....*....|....*....|....*....|
gi 27436953 652 QVWSLLRERRAD--HVILFSTQ--SMDEAD 677
Cdd:PRK13540 165 TIITKIQEHRAKggAVLLTSHQdlPLNKAD 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
480-682 |
1.04e-08 |
|
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: 57.80 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYKGKSGKVEALKGllfDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSemqdleeiRKITG 559
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 560 VCPQFNVqfdilTVKENLSLFAKIKGIHlkevEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLD 639
Cdd:cd03237 70 IKADYEG-----TVRDLLSSITKDFYTH----PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27436953 640 EPTTGLDPFSRDQVWSLLR------ERRA---DHVILFstqsmdeADILADR 682
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRrfaennEKTAfvvEHDIIM-------IDYLADR 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1306-1491 |
1.07e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.18 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLGHLGYCPQENVLWPmlTLREHL 1375
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnLRRKIGMVFQNPDNQFVGA--TVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1376 EVYAAVKGL-------RKADARLAIARLvsAFKLHEQlnvpvQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQ 1448
Cdd:PRK13642 104 AFGMENQGIpreemikRVDEALLAVNML--DFKTREP-----ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 1449 QQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRL 1491
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1299-1500 |
1.09e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.10 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1299 KKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcsSVLGhlgycpQENVlWpmlTLREHLE-- 1376
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG--MVLS------EETV-W---DVRRQVGmv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1377 --------VYAAVK-----GL-----------RKADARLAIARLvSAFKLHEqlnvPvQKLTAGITRKLCfVLSLLGNSP 1432
Cdd:PRK13635 87 fqnpdnqfVGATVQddvafGLenigvpreemvERVDQALRQVGM-EDFLNRE----P-HRLSGGQKQRVA-IAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1433 -VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK13635 160 dIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1294-1471 |
1.20e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.80 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAARNISFCvqEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSS---VLGHLGYCPQENVLWPMLT 1370
Cdd:PRK13541 9 FNIEQKNLFDLSITFL--PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniAKPYCTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHL----EVYAAVKGLRKAdarlaiarlVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1446
Cdd:PRK13541 87 VFENLkfwsEIYNSAETLYAA---------IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180
....*....|....*....|....*.
gi 27436953 1447 GQQQMWQAIqaVVKNTERG-VLLTTH 1471
Cdd:PRK13541 158 NRDLLNNLI--VMKANSGGiVLLSSH 181
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1304-1477 |
1.28e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.74 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-CSSVLG----------HLGYCPQENVLWPMLTLR 1372
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqDVATLDadalaqlrreHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLEVYAAVKGLRKAdARLAIAR-LVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDP-TGQQQ 1450
Cdd:PRK10535 105 QNVEVPAVYAGLERK-QRLLRAQeLLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDShSGEEV 183
|
170 180 190
....*....|....*....|....*....|...
gi 27436953 1451 MwqaiqAVVKN-TERG--VLLTTHN---LAEAE 1477
Cdd:PRK10535 184 M-----AILHQlRDRGhtVIIVTHDpqvAAQAE 211
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
500-647 |
1.29e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 500 LLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqdlEEIRKIT--GVCPQFNVQFDILtvkENL 577
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAylGHLPGLKADLSTL---ENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 578 SLFAKIKGIHLKEVEQEVQRILlelDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDP 647
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
467-691 |
1.48e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 467 PVAPEFQGKEAIRIRNVKKEYKGKSGkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLS 546
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAYQDNGF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 547 eMQDLEEIRKItgvcpqfnvqfdILTVKENLSLFAKIKGIHLKEVEQE-VQRILLELDMQN---IQDN--LAKHLSEGQK 620
Cdd:PRK10522 389 -AEQPEDYRKL------------FSAVFTDFHLFDQLLGPEGKPANPAlVEKWLERLKMAHkleLEDGriSNLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 621 RKLTFGITILGDPQILLLDEPTTGLDP-FSRDQVWSLLRERRADHVILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPhFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1304-1509 |
1.54e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK--PTA---GEVELKGCS---------SVLGHLGYCPQENVLWPML 1369
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNiyspdvdpiEVRREVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1370 TLREHLEVYAAVKGLRKA----DARLAIARLVSAF--KLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGI 1443
Cdd:PRK14267 101 TIYDNVAIGVKLNGLVKSkkelDERVEWALKKAALwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANI 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1444 DPTGQQQMWQAIQAVvkNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL----KNKLGKDYI 1509
Cdd:PRK14267 181 DPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVfenpEHELTEKYV 248
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1294-1506 |
1.77e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.20 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQEnvlw 1366
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtrASLRRNIAVVFQD---- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1367 PML---TLREHL----------EVYAAvkgLRKADARLAIARLVSAFKLH--EQLNvpvqKLTAGITRKLCFVLSLLGNS 1431
Cdd:PRK13657 418 AGLfnrSIEDNIrvgrpdatdeEMRAA---AERAQAHDFIERKPDGYDTVvgERGR----QLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1432 PVLLLDEPSTGIDPTGQQQMWQAIQAVVKNteRGVLLTTHNLAE-AEAlcDRVAIMVSGRLRCIGSIQHLKNKLGK 1506
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKG--RTTFIIAHRLSTvRNA--DRILVFDNGRVVESGSFDELVARGGR 562
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
478-646 |
2.04e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYkgksGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiynknlsEMQDLEEIrki 557
Cdd:PRK09544 5 VSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLRI--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 tGVCPQfNVQFDI---LTVKENLSLFAKIKGIHLKEVEQEVQRI-LLELDMQNiqdnlakhLSEGQKRKLTFGITILGDP 633
Cdd:PRK09544 70 -GYVPQ-KLYLDTtlpLTVNRFLRLRPGTKKEDILPALKRVQAGhLIDAPMQK--------LSGGETQRVLLARALLNRP 139
|
170
....*....|...
gi 27436953 634 QILLLDEPTTGLD 646
Cdd:PRK09544 140 QLLVLDEPTQGVD 152
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
502-646 |
2.11e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtIYNKNL--SEMQDlEEIRKITGvcpqfNVqFDIltVKENLSL 579
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLivARLQQ-DPPRNVEG-----TV-YDF--VAEGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 580 FA-KIKGIH--LKEVEQE--------VQRILLELDMQN-------IQDNLAK----------HLSEGQKRKLTFGITILG 631
Cdd:PRK11147 94 QAeYLKRYHdiSHLVETDpseknlneLAKLQEQLDHHNlwqlenrINEVLAQlgldpdaalsSLSGGWLRKAALGRALVS 173
|
170
....*....|....*
gi 27436953 632 DPQILLLDEPTTGLD 646
Cdd:PRK11147 174 NPDVLLLDEPTNHLD 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1311-1486 |
2.17e-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: 59.03 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1311 QEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-SSVLGHlgYCPQEnvlwpmltLREHLE-VYA--------- 1379
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSwDEVLKR--FRGTE--------LQDYFKkLANgeikvahkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1380 --------AVKG-----LRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1446
Cdd:COG1245 167 qyvdlipkVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27436953 1447 GQQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIM 1486
Cdd:COG1245 247 QRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1305-1483 |
2.28e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.65 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-SVLG------HLGYCPQEnvlwPML---TLREH 1374
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKpeiyrqQVSYCAQT----PTLfgdTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 LEVYAAVKGlrKADARLAIARLVSAFKLHEQ-LNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQ 1453
Cdd:PRK10247 101 LIFPWQIRN--QQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170 180 190
....*....|....*....|....*....|
gi 27436953 1454 AIQAVVKNTERGVLLTTHNLAEAEAlCDRV 1483
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1304-1509 |
2.42e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK--PTA---GEVELKG-------CSSVLGHLGYCPQENVLWPMLTL 1371
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGqdifkmdVIELRRRVQMVFQIPNPIPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REH----LEVYAAVKGLRKADAR----LAIARLVSAFKlhEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGI 1443
Cdd:PRK14247 100 FENvalgLKLNRLVKSKKELQERvrwaLEKAQLWDEVK--DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1444 DPTGQQQMWQAIQAVVKntERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL----KNKLGKDYI 1509
Cdd:PRK14247 178 DPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVftnpRHELTEKYV 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1313-1446 |
3.31e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1313 GEILGLLGPNGAGKSSSIRMISGITKPT--AGEV---ELKGCSSVLGHLGYCPQENVLWPMLTLREHLeVYAAV----KG 1383
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTIlanNRKPTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLlrlpKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1384 LRKADARLAIARLVSAFKLHEQLNVPV-----QKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPT 1446
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1305-1491 |
4.23e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCsSVLG----------HLGYCPQENVLWPMLTLreh 1374
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL-KVNDpkvderlirqEAGMVFQQFYLFPHLTA--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 LEVYA----AVKGLRKADARlAIAR-LVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQ 1449
Cdd:PRK09493 95 LENVMfgplRVRGASKEEAE-KQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 1450 QMWQAIQAVvknTERG--VLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK09493 174 EVLKVMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
499-690 |
4.28e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.79 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 499 GLLFDIYEGQITAILGHSGAGKS-SLLNILNGLSVP----TEGSVTIYNKNL--SEMQDLEEIR--KITGVCPQFNVQFD 569
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhASEQTLRGVRgnKIAMIFQEPMVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 570 IL-TVK----ENLSLFakiKGIHLKEVEQEVQRILLELDMQNIQDNLAKH---LSEGQKRKLTFGITILGDPQILLLDEP 641
Cdd:PRK15134 107 PLhTLEkqlyEVLSLH---RGMRREAARGEILNCLDRVGIRQAAKRLTDYphqLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27436953 642 TTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGR 690
Cdd:PRK15134 184 TTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1305-1498 |
4.76e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG--CSSVLG---HLGYCPQENVLWPMLTLREHLEVYA 1379
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdVSRLHArdrKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1380 AVKGLRKADARLAI----ARLVSAFKL-HEQLNVPVQkLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQA 1454
Cdd:PRK10851 100 TVLPRRERPNAAAIkakvTQLLEMVQLaHLADRYPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 1455 IQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQ 1498
Cdd:PRK10851 179 LRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
502-692 |
5.24e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGlSVP--TEGSVTIYNKNLSEMQDLEEI----------RKITGVCPQFNVQFD 569
Cdd:PRK13549 283 FSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKIRNPQQAIaqgiamvpedRKRDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 570 I-LTVKENLSLFAKI-KGIHLKEVEQEVQRILLELD--MQNIqdnlaKHLSEGQKRKLTFGITILGDPQILLLDEPTTGL 645
Cdd:PRK13549 362 ItLAALDRFTGGSRIdDAAELKTILESIQRLKVKTAspELAI-----ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27436953 646 DPFSRDQVWSLLRE--RRADHVILFSTQsMDEADILADRKVIMSNGRLK 692
Cdd:PRK13549 437 DVGAKYEIYKLINQlvQQGVAIIVISSE-LPEVLGLSDRVLVMHEGKLK 484
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1298-1530 |
5.37e-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: 57.50 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1298 KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGIT--KPTAGEvelkgcssVLGHLGYCP--------------- 1360
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGR--------IIYHVALCEkcgyverpskvgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1361 ---------QENVLW-PMLTLREHLEVYAAV-------------------KGLRKA--DARLAIARlvsAFKLHEQLNVP 1409
Cdd:TIGR03269 83 pvcggtlepEEVDFWnLSDKLRRRIRKRIAImlqrtfalygddtvldnvlEALEEIgyEGKEAVGR---AVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1410 ------VQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRV 1483
Cdd:TIGR03269 160 hrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 27436953 1484 AIMVSGRLRCIGSIQHLKNKlgkdYILELKVKETSQVTLVHTEILKL 1530
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAV----FMEGVSEVEKECEVEVGEPIIKV 282
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
492-646 |
5.85e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 492 GKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG---LSVpTEGSVTIYNKNLSEMQdlEEIRKITGVCPQFNVQF 568
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKI-LEGDILFKGESILDLE--PEERAHLGIFLAFQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 569 DILTVKE----NLSLFAKIKGIHLKEVEQ-EVQRILLE-LDMQNIQD-----NLAKHLSEGQKRKLTFGITILGDPQILL 637
Cdd:CHL00131 95 EIPGVSNadflRLAYNSKRKFQGLPELDPlEFLEIINEkLKLVGMDPsflsrNVNEGFSGGEKKRNEILQMALLDSELAI 174
|
....*....
gi 27436953 638 LDEPTTGLD 646
Cdd:CHL00131 175 LDETDSGLD 183
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
507-685 |
6.13e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 507 GQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEM--QDLEEIRKITGVCPQFNVQFDILTVKENLSlFAKIK 584
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrSRLYTVRKRMSMLFQSGALFTDMNVFDNVA-YPLRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 585 GIHLKE--VEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERR- 661
Cdd:PRK11831 112 HTQLPAplLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNs 191
|
170 180 190
....*....|....*....|....*....|..
gi 27436953 662 --------ADHVILFSTQSMDEADILADRKVI 685
Cdd:PRK11831 192 algvtcvvVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
477-646 |
6.20e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 477 AIRIRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiynkNLSEMQDLeeirk 556
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSENANI----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 itGVCPQFNV-QFDI-LTVKENLSLFAKIKgihlkEVEQEVQRILLELDMQniQDNL---AKHLSEGQKRKLTFGITILG 631
Cdd:PRK15064 385 --GYYAQDHAyDFENdLTLFDWMSQWRQEG-----DDEQAVRGTLGRLLFS--QDDIkksVKVLSGGEKGRMLFGKLMMQ 455
|
170
....*....|....*
gi 27436953 632 DPQILLLDEPTTGLD 646
Cdd:PRK15064 456 KPNVLVMDEPTNHMD 470
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
478-667 |
6.34e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.34 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGKsgKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQdLEEIRKI 557
Cdd:PRK11176 342 IEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT-LASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQfNVQFDILTVKENLSlFAKiKGIHLKEVEQEVQRILLELD----MQN-----IQDNLAKhLSEGQKRKLTFGIT 628
Cdd:PRK11176 419 VALVSQ-NVHLFNDTIANNIA-YAR-TEQYSREQIEEAARMAYAMDfinkMDNgldtvIGENGVL-LSGGQRQRIAIARA 494
|
170 180 190
....*....|....*....|....*....|....*....
gi 27436953 629 ILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHVIL 667
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
476-659 |
6.57e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 476 EAIRIRNVKKEYK-------GKSGkvealkgllFDIY------EGQITAILGHSGAGKSSLLNILNGLSVPTEGSvtiYN 542
Cdd:PRK13409 64 DAISIVNLPEELEeepvhryGVNG---------FKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 543 KNLS-----------EMQD-LEEIR--KITGVC-PQFnvqFDIL------TVKEnlsLFAKI--KGIhLKEVEQevqril 599
Cdd:PRK13409 132 EEPSwdevlkrfrgtELQNyFKKLYngEIKVVHkPQY---VDLIpkvfkgKVRE---LLKKVdeRGK-LDEVVE------ 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 600 lELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE 659
Cdd:PRK13409 199 -RLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRE 257
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1305-1444 |
8.89e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELkGcSSVlgHLGYCPQEnvlwpmltlREHLE----VYAA 1380
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETV--KLAYVDQS---------RDALDpnktVWEE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1381 VK--------GLRKADARLAIARLvsAFKLHEQlnvpvQKLTAgitrklcfVLS-----------LL---GNspVLLLDE 1438
Cdd:PRK11819 409 ISggldiikvGNREIPSRAYVGRF--NFKGGDQ-----QKKVG--------VLSggernrlhlakTLkqgGN--VLLLDE 471
|
....*.
gi 27436953 1439 PSTGID 1444
Cdd:PRK11819 472 PTNDLD 477
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
417-672 |
9.82e-08 |
|
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: 55.47 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 417 FDKILPYGDERHYSPLFFLNSSSCFQHQRTNAKVIEKEIDAEHPSDDYFEPVA--PEFQGKEAIRIRNVKKEYKGKSGKV 494
Cdd:pfam13304 36 RSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLEREDVEEKLSskPTLLEKRLLLREDSEEREPKFPPEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 495 EALKGLLFDIYEGQITAIL---GHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVCPQFNVQFDIL 571
Cdd:pfam13304 116 EELRLGLDVEERIELSLSElsdLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 TVKENLSLFAKIKGIHLKEVEQEVQRILLELDMQNIQDnlAKHLSEGQKRKLTFGITILGDPQ---ILLLDEPTTGLDPF 648
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELP--AFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPK 273
|
250 260
....*....|....*....|....*
gi 27436953 649 SRDQVWSLLRE-RRADHVILFSTQS 672
Cdd:pfam13304 274 LLRRLLELLKElSRNGAQLILTTHS 298
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1313-1500 |
1.08e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1313 GEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG-------CSSVLGHLGYCPQENVLWPMLTLREHLEV-----YAA 1380
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1381 VKGLRKADARL---AIArLVSAFKLHEQLnvpVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1457
Cdd:PRK10575 117 LGRFGAADREKveeAIS-LVGLKPLAHRL---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 1458 VVKntERG--VLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHL 1500
Cdd:PRK10575 193 LSQ--ERGltVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1304-1491 |
1.09e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.07 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVeLKGcSSVLGH------LGYcpQENVLWPMLTLREHleV 1377
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-TAPLAEaredtrLMF--QDARLLPWKKVIDN--V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 YAAVKGLRKADARLAIArlvsAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQA 1457
Cdd:PRK11247 103 GLGLKGQWRDAALQALA----AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIES 178
|
170 180 190
....*....|....*....|....*....|....
gi 27436953 1458 VVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK11247 179 LWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1302-1491 |
1.13e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 56.62 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKS----SSIRMISGITKPTAGEVELKGcSSVLG------------HLGYCPQEnvl 1365
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG-QDLLGlserelrrirgnRIAMIFQE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1366 wPM------LTLREHL-EVYAAVKGLRKADARLAIARLVSAFKLHEqlnvPVQKLTAgitrkLCFVLS-----------L 1427
Cdd:COG4172 101 -PMtslnplHTIGKQIaEVLRLHRGLSGAAARARALELLERVGIPD----PERRLDA-----YPHQLSggqrqrvmiamA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 1428 LGNSPVLLL-DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:COG4172 171 LANEPDLLIaDEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
476-659 |
1.48e-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: 56.33 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 476 EAIRIRNVKKEYK-------GKSGkvealkgllFDIY------EGQITAILGHSGAGKSSLLNILNGLSVPTEGsvtIYN 542
Cdd:COG1245 64 DAISIVNLPEELEedpvhryGENG---------FRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 543 KNLS-----------EMQD-LEEIR--KITGVC-PQfnvQFDIL------TVKEnlsLFAKI--KGIhLKEVEQevqril 599
Cdd:COG1245 132 EEPSwdevlkrfrgtELQDyFKKLAngEIKVAHkPQ---YVDLIpkvfkgTVRE---LLEKVdeRGK-LDELAE------ 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 600 lELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE 659
Cdd:COG1245 199 -KLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
480-690 |
1.52e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.12 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNIL--NGLsvpTEGSVTIYNK---NLSEMQ- 549
Cdd:PRK09473 15 VKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGR---IGGSATFNGReilNLPEKEl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 550 ---DLEEIRKI-----TGVCPQFNVQFDILTVkenLSLFakiKGIHLKEVEQEVQRILLELDMQNIQD--NLAKH-LSEG 618
Cdd:PRK09473 92 nklRAEQISMIfqdpmTSLNPYMRVGEQLMEV---LMLH---KGMSKAEAFEESVRMLDAVKMPEARKrmKMYPHeFSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 619 QKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFSTQSMDEADILADRKVIMSNGR 690
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1298-1491 |
1.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.71 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1298 KKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSvlghlgycPQENVLWP------MLTL 1371
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT--------SDEENLWDirnkagMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHLEVYAAVK-----------GLRKADARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPS 1440
Cdd:PRK13633 93 NPDNQIVATIVeedvafgpenlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27436953 1441 TGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAeALCDRVAIMVSGRL 1491
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
493-691 |
1.71e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 493 KVEALKG------LLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLEEIRKITGVCPQfNV 566
Cdd:PRK11288 259 RLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPE-DR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 567 QFD----ILTVKENLSLFAKIKGIHL-------KEVEQEVQRIllelDMQNIQ----DNLAKHLSEGQKRKltfgiTILG 631
Cdd:PRK11288 338 KAEgiipVHSVADNINISARRHHLRAgclinnrWEAENADRFI----RSLNIKtpsrEQLIMNLSGGNQQK-----AILG 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 632 -----DPQILLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGRL 691
Cdd:PRK11288 409 rwlseDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVaVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1297-1492 |
1.86e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIaaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK-PTAGEVELKG-------CSSVLGH-LGYCP------- 1360
Cdd:PRK13549 274 HIKRV--DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpvkirnPQQAIAQgIAMVPedrkrdg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1361 -------QENVLWPML---TLREHLEVYAAVKGLRKADARLAIaRLVSAFklheqlnVPVQKLTAGITRKLCFVLSLLGN 1430
Cdd:PRK13549 352 ivpvmgvGKNITLAALdrfTGGSRIDDAAELKTILESIQRLKV-KTASPE-------LAIARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 1431 SPVLLLDEPSTGIDPTGQQQMWQAIQAVVKnteRGV--LLTTHNLAEAEALCDRVAIMVSGRLR 1492
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQ---QGVaiIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1302-1489 |
2.34e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC--------SSVLGHLGYCPQENVLWPMLTLRE 1373
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngpkSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HL----------------EVYA-AVKGLRKADARLAIARLVSAFKLHEQLNVPVQKltagitrklcfVLSLlgNSPVLLL 1436
Cdd:PRK10762 99 NIflgrefvnrfgridwkKMYAeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK-----------VLSF--ESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1437 DEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSG 1489
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRE-LKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1298-1439 |
3.44e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1298 KKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQENVLWPMLTLREHLEv 1377
Cdd:PRK11819 19 KKQIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKV----GYLPQEPQLDPEKTVRENVE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 yAAVKGLRKADARL-AI------------------ARL------VSAFKLHEQLNV------------PVQKLTAGITRK 1420
Cdd:PRK11819 93 -EGVAEVKAALDRFnEIyaayaepdadfdalaaeqGELqeiidaADAWDLDSQLEIamdalrcppwdaKVTKLSGGERRR 171
|
170 180
....*....|....*....|..
gi 27436953 1421 --LCfvlSLLGNSP-VLLLDEP 1439
Cdd:PRK11819 172 vaLC---RLLLEKPdMLLLDEP 190
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
506-681 |
3.46e-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: 53.52 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 506 EGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT--------IYNKNLSEMQDLEEIRKITGVCPQFNVQF-DIL--TVK 574
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPQYvDLIpkAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 575 ENLSLFAKikgihlKEVEQEVQRILLE-LDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQV 653
Cdd:cd03236 105 GKVGELLK------KKDERGKLDELVDqLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180
....*....|....*....|....*....
gi 27436953 654 WSLLRER-RADHVILFSTQSMDEADILAD 681
Cdd:cd03236 179 ARLIRELaEDDNYVLVVEHDLAVLDYLSD 207
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
509-657 |
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 27436953 509 ITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMQDLeeirKITGVCPQFNVQFDiLTVKENLSLFAKIkgihl 588
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP----YCTYIGHNLGLKLE-MTVFENLKFWSEI----- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 589 KEVEQEVQRILLELDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLL 657
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
500-646 |
4.07e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 500 LLFDIYEGQITAILGHSGAGKSSLLNILNGLSvPTEGSVTIYNKNLSEMQDLEEIRKITGVCPQFNVQFdILTVKENLSL 579
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF-AMPVFQYLTL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 580 FakikgIHLKEVEQEVQRILLEL-DMQNIQDNLAKHLS-----EGQKRKLTFGI-----TILGDPQILLLDEPTTGLD 646
Cdd:PRK03695 93 H-----QPDKTRTEAVASALNEVaEALGLDDKLGRSVNqlsggEWQRVRLAAVVlqvwpDINPAGQLLLLDEPMNSLD 165
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1304-1503 |
4.57e-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: 52.14 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGI--TKPTAGEVELKGCS---------SVLGhLGYCPQENVLWPMLTLR 1372
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlppeerARLG-IFLAFQYPPEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHLevyaavkglrkadarlaiaRLVsafklheqlNVpvqKLTAGiTRKLCFVLSLLGNSPVL-LLDEPSTGIDPTGQQQM 1451
Cdd:cd03217 96 DFL-------------------RYV---------NE---GFSGG-EKKRNEILQLLLLEPDLaILDEPDSGLDIDALRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1452 WQAIQAvVKNTERGVLLTTHNLAEAEAL-CDRVAIMVSGRLRCIGS---IQHLKNK 1503
Cdd:cd03217 144 AEVINK-LREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDkelALEIEKK 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
490-691 |
4.92e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 490 KSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGL---SVPTEGSVTiYNKnlsemQDLEEI--RKITGVCPQF 564
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKldpSLKVSGEIT-YNG-----YRLNEFvpRKTSAYISQN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 565 NVQFDILTVKENLSLFAKIKGIH-----LKEV-----------EQEVQRILLELDMQNIQDNL----------------- 611
Cdd:PLN03140 248 DVHVGVMTVKETLDFSARCQGVGtrydlLSELarrekdagifpEAEVDLFMKATAMEGVKSSLitdytlkilgldickdt 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 612 ------AKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRE--RRADHVILFS-TQSMDEADILADR 682
Cdd:PLN03140 328 ivgdemIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQivHLTEATVLMSlLQPAPETFDLFDD 407
|
....*....
gi 27436953 683 KVIMSNGRL 691
Cdd:PLN03140 408 IILLSEGQI 416
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1272-1490 |
4.96e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.01 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1272 DEKPVIIASCLHKEYAGQKkscfskrkkkiAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSS 1351
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRK-----------GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1352 VLGHLGYCPQENVLWPMLT----LREHlevyaAVKGLR---KADARLAiARLVSAFKLH------------EQLNVPVQK 1412
Cdd:PRK11701 71 QLRDLYALSEAERRRLLRTewgfVHQH-----PRDGLRmqvSAGGNIG-ERLMAVGARHygdiratagdwlERVEIDAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1413 L-------TAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAI 1485
Cdd:PRK11701 145 IddlpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
....*
gi 27436953 1486 MVSGR 1490
Cdd:PRK11701 225 MKQGR 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
460-677 |
5.17e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 460 PSDDYFEPVAPEFQGKeaIRIRNVKKEYKgkSGKVeALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVT 539
Cdd:PRK10790 325 PRQQYGNDDRPLQSGR--IDIDNVSFAYR--DDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 540 IYNKNLSEMQDlEEIRKitGVCpqfNVQFD--IL--TVKENLSLFAKIKGIHLKEVEQEVQRILLELDM-QNIQDNLAKH 614
Cdd:PRK10790 400 LDGRPLSSLSH-SVLRQ--GVA---MVQQDpvVLadTFLANVTLGRDISEEQVWQALETVQLAELARSLpDGLYTPLGEQ 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 615 ---LSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRD---QVWSLLRERRADHVILFSTQSMDEAD 677
Cdd:PRK10790 474 gnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQaiqQALAAVREHTTLVVIAHRLSTIVEAD 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1304-1472 |
7.13e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 51.00 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLghlgYCPQENVLwPMLTLREHLeVYAAVKG 1383
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLL----FLPQRPYL-PLGTLREQL-IYPWDDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1384 LRKAD-ARLAIARLvsafklheqlnvpvqkltagITRKLCFVlsllgnspvlLLDEPSTGIDPTGQQQMWQAIQ----AV 1458
Cdd:cd03223 92 LSGGEqQRLAFARL--------------------LLHKPKFV----------FLDEATSALDEESEDRLYQLLKelgiTV 141
|
170
....*....|....
gi 27436953 1459 VKNTERGVLLTTHN 1472
Cdd:cd03223 142 ISVGHRPSLWKFHD 155
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
478-662 |
8.80e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGlsvptegsvtIYNKNLSEMQDLEEIRKI 557
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG----------IYTRDAGSILYLGKEVTF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGvcPQFNVQFDI------------LTVKENLSL----FAKIKGIHLKEVEQEVQRILLELDMQNIQDNLAKHLSEGQKR 621
Cdd:PRK10762 71 NG--PKSSQEAGIgiihqelnlipqLTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27436953 622 KLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRA 662
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS 189
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
465-682 |
9.31e-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: 53.63 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 465 FE--PVAPEFQGKEAIRIRNVKKEYKGKSGKVEAlkGllfDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTiyn 542
Cdd:COG1245 327 FEvhAPRREKEEETLVEYPDLTKSYGGFSLEVEG--G---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 543 knlsemqdlEEIR---KitgvcPQFnVQFDI-LTVKENL-SLFAKIKGIHLKEVEqevqrILLELDMQNIQDNLAKHLSE 617
Cdd:COG1245 399 ---------EDLKisyK-----PQY-ISPDYdGTVEEFLrSANTDDFGSSYYKTE-----IIKPLGLEKLLDKNVKDLSG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 618 GQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLR----ERRA-----DHVILFstqsmdeADILADR 682
Cdd:COG1245 459 GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfaeNRGKtamvvDHDIYL-------IDYISDR 525
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1302-1490 |
1.00e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.50 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP----TA-----GEVELKGCSS-----VLGH--------LGYC 1359
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTAdrmrfDDIDLLRLSPrerrkLVGHnvsmifqePQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1360 --PQENV------LWPMLTLREHlevYAAVKGLRKadaRLAIARLVS-AFKLHEQL--NVPVQkLTAGITRKLCFVLSLl 1428
Cdd:PRK15093 102 ldPSERVgrqlmqNIPGWTYKGR---WWQRFGWRK---RRAIELLHRvGIKDHKDAmrSFPYE-LTEGECQKVMIAIAL- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1429 GNSPVLLL-DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:PRK15093 174 ANQPRLLIaDEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1296-1361 |
1.07e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 1.07e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436953 1296 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLGYCPQ 1361
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQ 87
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
497-689 |
1.15e-06 |
|
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: 52.17 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTiYNKNLSemqdleeirkitgVCPQFNVqfdIL--TVK 574
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGRIS-------------FSSQFSW---IMpgTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 575 ENLSLFAKIKGIHLKEVEQEVQrilLELDMQNI--QDN--LAK---HLSEGQKRKLTFGITILGDPQILLLDEPTTGLDP 647
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVKACQ---LEEDITKFpeKDNtvLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436953 648 FSRDQVW-SLLRERRADHVILFSTQSMDEADIlADRKVIMSNG 689
Cdd:cd03291 193 FTEKEIFeSCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
497-647 |
1.38e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.11 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNG--LSVPTEGSVtiynknlsEMQDLEEIRKITGVcPQFNVQFDILTVK 574
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCV--------DVPDNQFGREASLI-DAIGRKGDFKDAV 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 575 ENLSlfakikgihlkeveqevqrilleldMQNIQDNLA-----KHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDP 647
Cdd:COG2401 117 ELLN-------------------------AVGLSDAVLwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
465-682 |
1.39e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 465 FE--PVAPEFQGKEAIRIRNVKKEYKGKSGKVEAlkGllfDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIyn 542
Cdd:PRK13409 326 FEerPPRDESERETLVEYPDLTKKLGDFSLEVEG--G---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 543 knlsemqdleEIR---KitgvcPQF-NVQFDIlTVKENLSLFAKIKGIHLKEVEqevqrILLELDMQNIQDNLAKHLSEG 618
Cdd:PRK13409 399 ----------ELKisyK-----PQYiKPDYDG-TVEDLLRSITDDLGSSYYKSE-----IIKPLQLERLLDKNVKDLSGG 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 619 QKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLR----ERRA-----DHVILFstqsmdeADILADR 682
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRriaeEREAtalvvDHDIYM-------IDYISDR 523
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1298-1490 |
1.40e-06 |
|
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: 51.49 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1298 KKKIAaRNISFCVQEGEILGLLGPNGAGKSSSIRMISG--ITKPTAGEVELKGcSSVL-------GHLG--YCPQENVLW 1366
Cdd:TIGR01978 12 DKEIL-KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKG-QDLLelepderARAGlfLAFQYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1367 PMLTLREHL-EVYAAVKGLR------------KADARLAIARLVSAFkLHEQLNVPVqkltAGITRKLCFVLSLLGNSPV 1433
Cdd:TIGR01978 90 PGVSNLEFLrSALNARRSARgeepldlldfekLLKEKLALLDMDEEF-LNRSVNEGF----SGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 1434 L-LLDEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALC-DRVAIMVSGR 1490
Cdd:TIGR01978 165 LaILDEIDSGLDIDALKIVAEGINR-LREPDRSFLIITHYQRLLNYIKpDYVHVLLDGR 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1302-1491 |
2.03e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGIT----KPTAGEVELKGcsSVLGHLGYCPQENVLW---------PM 1368
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNG--QDLQRISEKERRNLVGaevamifqdPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1369 LTLR----------EHLEVYAAvkGLRKADARLAIARL--VSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLL 1436
Cdd:PRK11022 100 TSLNpcytvgfqimEAIKVHQG--GNKKTRRQRAIDLLnqVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 1437 DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1272-1490 |
2.09e-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: 52.38 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1272 DEKPVIIASCLHKEYAGQKKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITkPTAGEVELKGCSs 1351
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQD- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1352 vLGHLGycPQEnvlwpMLTLREHLEV-----YAAVkglrkaDARLAIARLVS-AFKLHE-QLNVpvqkltAGITRKLCFV 1424
Cdd:COG4172 349 -LDGLS--RRA-----LRPLRRRMQVvfqdpFGSL------SPRMTVGQIIAeGLRVHGpGLSA------AERRARVAEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1425 LSLLGNSP-----------------------------VLLLDEPSTGIDPTGQQQM---WQAIQAvvkntERGV--LLTT 1470
Cdd:COG4172 409 LEEVGLDPaarhryphefsggqrqriaiaralilepkLLVLDEPTSALDVSVQAQIldlLRDLQR-----EHGLayLFIS 483
|
250 260
....*....|....*....|
gi 27436953 1471 HNLAEAEALCDRVAIMVSGR 1490
Cdd:COG4172 484 HDLAVVRALAHRVMVMKDGK 503
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1302-1490 |
2.51e-06 |
|
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: 52.13 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGItKPTA---GEVELKGCSSVLGH--------LGYCPQENVLWPMLT 1370
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNirdteragIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1371 LREHL----EVyaAVKGLRKADArlaiARLVSAFKLHEQLNV-------PVQKLTAGITRKLCFVLSLLGNSPVLLLDEP 1439
Cdd:TIGR02633 95 VAENIflgnEI--TLPGGRMAYN----AMYLRAKNLLRELQLdadnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1440 STGIDPTGQQQMWQAIQAVvknTERGV--LLTTHNLAEAEALCDRVAIMVSGR 1490
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDL---KAHGVacVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1302-1491 |
2.75e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG----------CSSVLGHLGYCPQENVLWPMLTL 1371
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknreVPFLRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1372 REHLEVYAAVKGLRKADARLAI-ARLVSAFKLHEQLNVPVQkLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDptgqQQ 1450
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVsAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27436953 1451 MWQAIQAVVKNTER---GVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK10908 172 LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1304-1503 |
2.94e-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: 52.22 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKgcssvlGHLGYCPQenVLWPML-TLREHLevyaaVK 1382
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS------GRISFSPQ--TSWIMPgTIKDNI-----IF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1383 GLRKADARLaiARLVSAFKLHEQLNVPVQK-----------LTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQM 1451
Cdd:TIGR01271 510 GLSYDEYRY--TSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27436953 1452 WQAIQAVVKNTERGVLLTT--HNLAEAealcDRVAIMVSGRLRCIGSIQHLKNK 1503
Cdd:TIGR01271 588 FESCLCKLMSNKTRILVTSklEHLKKA----DKILLLHEGVCYFYGTFSELQAK 637
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1306-1491 |
3.41e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGC-------SSVLGHLGYCPQENVLWPMlTLREHLEVY 1378
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvakfglTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1379 AA------VKGLRKADARLAIARlvSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMW 1452
Cdd:PLN03232 1334 SEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190
....*....|....*....|....*....|....*....
gi 27436953 1453 QAIQAVVKNTErgVLLTTHNLaEAEALCDRVAIMVSGRL 1491
Cdd:PLN03232 1412 RTIREEFKSCT--MLVIAHRL-NTIIDCDKILVLSSGQV 1447
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
442-664 |
4.99e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 442 QHQRTnakviEKEIDAEhPSDDyfePVAPEFQGKEAIRIRNVKKEYKGKSGKV-------EALKGLLFDIYEGQITAILG 514
Cdd:PRK15134 249 THPYT-----QKLLNSE-PSGD---PVPLPEPASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 515 HSGAGKSS----LLNILNglsvpTEGSVTIYNK---NLSEMQDLEEIRKITGVC--------PQFNVQfdiLTVKENLSL 579
Cdd:PRK15134 320 ESGSGKSTtglaLLRLIN-----SQGEIWFDGQplhNLNRRQLLPVRHRIQVVFqdpnsslnPRLNVL---QIIEEGLRV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 580 FAKIkgIHLKEVEQEVQRILLELDMqniqDNLAKH-----LSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVW 654
Cdd:PRK15134 392 HQPT--LSAAQREQQVIAVMEEVGL----DPETRHrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
|
250
....*....|
gi 27436953 655 SLLRERRADH 664
Cdd:PRK15134 466 ALLKSLQQKH 475
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
494-529 |
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 27436953 494 VEALKGLLfdiyEGQITAILGHSGAGKSSLLNILNG 529
Cdd:cd01854 76 LDELRELL----KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1297-1471 |
6.66e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK--PTAGEVELkgcssvlghlgycpQENVLWPMLTLREH 1374
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV--------------PDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1375 L----EVYAAVkglrkadARLAIARLVSAFKLHEqlnvPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQ 1450
Cdd:COG2401 106 IgrkgDFKDAV-------ELLNAVGLSDAVLWLR----RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|.
gi 27436953 1451 MWQAIQAVVKNTERGVLLTTH 1471
Cdd:COG2401 175 VARNLQKLARRAGITLVVATH 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1297-1491 |
7.32e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1297 RKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISG-ITKPTA-------GEVELKG-------------CSSVLGH 1355
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGeplaaidaprlarLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1356 LG-----YCPQENVL---WPML-----TLREHLEVyaAVKGLRKADARLAIARLVSAfklheqlnvpvqkLTAGITRKLC 1422
Cdd:PRK13547 91 AAqpafaFSAREIVLlgrYPHArragaLTHRDGEI--AWQALALAGATALVGRDVTT-------------LSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1423 F--VLSLLGNSP-------VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTH--NLAEAEAlcDRVAIMVSGRL 1491
Cdd:PRK13547 156 FarVLAQLWPPHdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHdpNLAARHA--DRIAMLADGAI 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1302-1491 |
7.79e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.85 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELK----GCSSVLGHLGYCPQENVLWPMLTLREHLEV 1377
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYSKKIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1378 ------YAAVK--------------GLRKADARLAIARLVSAFKLHEQ-LNVPVQKLTAGITRKLCFVLSLLGNSPVLLL 1436
Cdd:PRK13631 121 vfqfpeYQLFKdtiekdimfgpvalGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436953 1437 DEPSTGIDPTGQQQMWQAIQAvVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1304-1490 |
8.60e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 48.91 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITK--PTAGEVELKGCS----SV-----LGhLGYCPQENVLWPMLTLR 1372
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDilelSPderarAG-IFLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1373 EHL-EVYAAVKGLrKADARLAIARLVSAFK--------LHEQLNVpvqKLTAGiTRKLCFVLSLLGNSPVL-LLDEPSTG 1442
Cdd:COG0396 96 NFLrTALNARRGE-ELSAREFLKLLKEKMKelgldedfLDRYVNE---GFSGG-EKKRNEILQMLLLEPKLaILDETDSG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1443 IDptgqqqMWqAIQAV------VKNTERGVLLTTHN---LAEAEAlcDRVAIMVSGR 1490
Cdd:COG0396 171 LD------ID-ALRIVaegvnkLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGR 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1305-1503 |
8.62e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.90 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1305 NISFCVQEGEILGLLGPNGAGKSSSIRMISGITKP----TA-----GEVELKGCSS-----VLGH-LGYCPQE--NVLWP 1367
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTAdrfrwNGIDLLKLSPrerrkIIGReIAMIFQEpsSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHL-EVYAA--VKG----LRKADARLAIARL--VsAFKLHEQL--NVPVQkLTAGITRKLCFVLSLlGNSPVLLL 1436
Cdd:COG4170 105 SAKIGDQLiEAIPSwtFKGkwwqRFKWRKKRAIELLhrV-GIKDHKDImnSYPHE-LTEGECQKVMIAMAI-ANQPRLLI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1437 -DEPSTGIDPTGQQQMWQAIQAVVKNTERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKNK 1503
Cdd:COG4170 182 aDEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
494-529 |
8.73e-06 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 49.34 E-value: 8.73e-06
10 20 30
....*....|....*....|....*....|....*.
gi 27436953 494 VEALKGLLfdiyEGQITAILGHSGAGKSSLLNILNG 529
Cdd:COG1162 157 LDELRELL----KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
507-751 |
8.80e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 507 GQITAILGHSGAGKSSLLNIL----NGLSVPTEGSVTiYNKnlsemQDLEEIRK-ITG---VCPQFNVQFDILTVKENLS 578
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVIT-YDG-----ITPEEIKKhYRGdvvYNAETDVHFPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 579 LFAKIKGIHLKEV---EQEVQRILLELDMQ----------NIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGL 645
Cdd:TIGR00956 161 FAARCKTPQNRPDgvsREEYAKHIADVYMAtyglshtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 646 DPFSRDQVWSLLRE--RRADHVILFST-QSMDEADILADRKVIMSNGRLKCAGSS-----MFLKrrwgLGYhlslhrneI 717
Cdd:TIGR00956 241 DSATALEFIRALKTsaNILDTTPLVAIyQCSQDAYELFDKVIVLYEGYQIYFGPAdkakqYFEK----MGF--------K 308
|
250 260 270
....*....|....*....|....*....|....*..
gi 27436953 718 CNPEQITS-FIThHIPDAKLKTENK--EKLVYTLPLE 751
Cdd:TIGR00956 309 CPDRQTTAdFLT-SLTSPAERQIKPgyEKKVPRTPQE 344
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1294-1502 |
1.07e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1294 FSKRKKKIAArNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS----------------SVLGHLG 1357
Cdd:PRK11831 15 FTRGNRCIFD-NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsrsrlytvrkrmSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1358 YCPQ-----ENVLWPmltLREHLEVYAAVkglrkadARLAIARLVSAFKLHEQLNVPVQKLTAGITRKLCFVLSLLGNSP 1432
Cdd:PRK11831 94 ALFTdmnvfDNVAYP---LREHTQLPAPL-------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1433 VLLLDEPSTGIDPTGQQQMWQAIQAVvkNTERGV--LLTTHNLAEAEALCDRVAIMVSGRLRCIGSIQHLKN 1502
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISEL--NSALGVtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
478-717 |
1.16e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.54 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 478 IRIRNVKKEykgksGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNILNGLSVPTEGSVTIYNKNLSemqdLEE 553
Cdd:PRK10418 5 IELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA----PCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 554 IRKITgvcpqfnvqfdILTVKEN-LSLFAKIKGI--HLKE---------VEQEVQRILLELDMQNIQDNLAKH---LSEG 618
Cdd:PRK10418 76 LRGRK-----------IATIMQNpRSAFNPLHTMhtHAREtclalgkpaDDATLTAALEAVGLENAARVLKLYpfeMSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 619 QKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLLRERRADHV--ILFSTQSMDEADILADRKVIMSNGRLKCAGS 696
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
250 260
....*....|....*....|....*...
gi 27436953 697 SMFLKRRWG-------LGYHLSLHRNEI 717
Cdd:PRK10418 225 VETLFNAPKhavtrslVSAHLALYGMEL 252
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1272-1348 |
1.27e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 1.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1272 DEKPVIIASCLHKEYAgQKKSCFSKRKKKIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKG 1348
Cdd:PRK11308 1 SQQPLLQAIDLKKHYP-VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
467-646 |
2.55e-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: 48.78 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 467 PVAPEFqGKEAIRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI------ 540
Cdd:TIGR03719 313 PPGPRL-GDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvkl 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 541 -Y----------NKN----LSEMQDLEEIRKIT----GVCPQFNvqfdiltvkenlslfakIKGihlkeveqevqrille 601
Cdd:TIGR03719 388 aYvdqsrdaldpNKTvweeISGGLDIIKLGKREipsrAYVGRFN-----------------FKG---------------- 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27436953 602 ldmqNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLD 646
Cdd:TIGR03719 435 ----SDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1306-1496 |
2.59e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.30 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1306 ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL------------KGCSSVLghlgycpQENVLWPMLTLRE 1373
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIggrvvnelepadRDIAMVF-------QNYALYPHMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HLEvYA-AVKGLRKADARLAIARLVSAFKLHEQLNVPVQKLTAG----------ITRKlcfvlsllgnsP-VLLLDEPST 1441
Cdd:PRK11650 96 NMA-YGlKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGqrqrvamgraIVRE-----------PaVFLFDEPLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436953 1442 GIDPTGQQQM---WQAIQAVVKNTErgvLLTTHNLAEAEALCDRVAIMVSGRLRCIGS 1496
Cdd:PRK11650 164 NLDAKLRVQMrleIQRLHRRLKTTS---LYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
480-690 |
3.22e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNL---SEMQDLEEirK 556
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALEN--G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 557 ITGVCPQFNvQFDILTVKENLSLFA-KIKGIHL--KEVEQEVQRILLELDMQ-NIQDNLAKhLSEGQKRKLTFGITILGD 632
Cdd:PRK10982 75 ISMVHQELN-LVLQRSVMDNMWLGRyPTKGMFVdqDKMYRDTKAIFDELDIDiDPRAKVAT-LSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436953 633 PQILLLDEPTTGLDPFSRDQVWSLLRERRADHV-ILFSTQSMDEADILADRKVIMSNGR 690
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
480-657 |
3.46e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.98 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKS----SLLNILNGLSVPTEGSVTIYNKNLSEMQdLEEIR 555
Cdd:COG4170 6 IRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLS-PRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 556 KITGVcpqfnvqfDILTVKEN----LSLFAKIkGIHLKEV-------------EQEVQRILLEL-------DMQNIQDNL 611
Cdd:COG4170 85 KIIGR--------EIAMIFQEpsscLDPSAKI-GDQLIEAipswtfkgkwwqrFKWRKKRAIELlhrvgikDHKDIMNSY 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27436953 612 AKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLL 657
Cdd:COG4170 156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLL 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
452-696 |
4.00e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 452 EKEIDAEHPsddyfePVAPefqGKEAIRIRNVKKEYKGKSGKvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS 531
Cdd:PLN03232 598 EERILAQNP------PLQP---GAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 532 VPTEGSVTIynknlsemqdleeIRKITGVCPQFNVQFDIlTVKENLsLFAKikgihlkevEQEVQRILLELDMQNIQDNL 611
Cdd:PLN03232 668 SHAETSSVV-------------IRGSVAYVPQVSWIFNA-TVRENI-LFGS---------DFESERYWRAIDVTALQHDL 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 612 --------------AKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVW-SLLRERRADHVILFSTQSMDEA 676
Cdd:PLN03232 724 dllpgrdlteigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTNQLHFL 803
|
250 260
....*....|....*....|
gi 27436953 677 DiLADRKVIMSNGRLKCAGS 696
Cdd:PLN03232 804 P-LMDRIILVSEGMIKEEGT 822
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
481-657 |
5.89e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 481 RNVKKEYKGKSG------KVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEmQDLEEI 554
Cdd:PRK11308 9 IDLKKHYPVKRGlfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 555 ----RKITGVC--------PQFNVQfDILT--VKENLSLFAkikgihlKEVEQEVQRILLELDMQNIQDNLAKHL-SEGQ 619
Cdd:PRK11308 88 kllrQKIQIVFqnpygslnPRKKVG-QILEepLLINTSLSA-------AERREKALAMMAKVGLRPEHYDRYPHMfSGGQ 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 27436953 620 KRKLTFGITILGDPQILLLDEPTTGLDPFSRDQVWSLL 657
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
497-667 |
7.09e-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: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTIYNKNLSEMqDLEEIRKITGVCPQFNVQFDiLTVKEN 576
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-GLHDLRFKITIIPQDPVLFS-GSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 577 LSLFAKIK------GIHLKEVEQEVQRILLELDMQNIQDnlAKHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSR 650
Cdd:TIGR00957 1380 LDPFSQYSdeevwwALELAHLKTFVSALPDKLDHECAEG--GENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
170
....*....|....*..
gi 27436953 651 DQVWSLLRERRADHVIL 667
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVL 1474
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
474-646 |
7.52e-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: 47.63 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 474 GKEAIRIRNVKkeYKGKSGKVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILnglsvptegsvtiynknLSEMQDLEE 553
Cdd:TIGR00957 633 EGNSITVHNAT--FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----------------LAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 554 IRKITG----VCPQFNVQFDilTVKENLsLFAKikGIHLKEVEQEVQRILLELDMQNI----QDNLAK---HLSEGQKRK 622
Cdd:TIGR00957 694 HVHMKGsvayVPQQAWIQND--SLRENI-LFGK--ALNEKYYQQVLEACALLPDLEILpsgdRTEIGEkgvNLSGGQKQR 768
|
170 180
....*....|....*....|....
gi 27436953 623 LTFGITILGDPQILLLDEPTTGLD 646
Cdd:TIGR00957 769 VSLARAVYSNADIYLFDDPLSAVD 792
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
494-529 |
7.74e-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: 7.74e-05
10 20 30
....*....|....*....|....*....|....*.
gi 27436953 494 VEALKGLLfdiyEGQITAILGHSGAGKSSLLNILNG 529
Cdd:pfam03193 97 IEALKELL----KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
480-646 |
7.76e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 480 IRNVKKEYKGKsgkvEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLS--VPTEGSVTIYNKNLSEMQdlEEIRKI 557
Cdd:PRK09580 4 IKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELS--PEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 558 TGVCPQFNVQFDILTVKENLSLFAKIKGIHLKEVEQEVQRI----LLE-----LDMQniQDNLAKHLSEG-----QKRKL 623
Cdd:PRK09580 78 EGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFdfqdLMEekialLKMP--EDLLTRSVNVGfsggeKKRND 155
|
170 180
....*....|....*....|...
gi 27436953 624 TFGITILgDPQILLLDEPTTGLD 646
Cdd:PRK09580 156 ILQMAVL-EPELCILDESDSGLD 177
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
502-658 |
1.07e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 502 FDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSvtiYNKNLSEMQDL--EEIRKITGVCPQFNvQFDILTVKENLSl 579
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---RQSQFSHITRLsfEQLQKLVSDEWQRN-NTDMLSPGEDDT- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 580 fakikGIHLKEVEQEVQR---ILLELDMQ-NIQDNLA---KHLSEGQKRKLTFGITILGDPQILLLDEPTTGLDPFSRDQ 652
Cdd:PRK10938 99 -----GRTTAEIIQDEVKdpaRCEQLAQQfGITALLDrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
....*.
gi 27436953 653 VWSLLR 658
Cdd:PRK10938 174 LAELLA 179
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1304-1530 |
1.19e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGcSSVLGHLGYCPQENVLWPMLTLREHLEVYAA--- 1380
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG-KKINNHNANEAINHGFALVTEERRSTGIYAYldi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1381 --------VKGLRKADARLAIARLVSAFK-LHEQLNV--PVQK-----LTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:PRK10982 344 gfnslisnIRNYKNKVGLLDNSRMKSDTQwVIDSMRVktPGHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1445 PTGQQQMWQAIQAVVKNtERGVLLTTHNLAEAEALCDRVAIMVSGRLRCIgsiqhlknklgkdyileLKVKETSQvtlvh 1524
Cdd:PRK10982 424 VGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI-----------------VDTKTTTQ----- 480
|
....*.
gi 27436953 1525 TEILKL 1530
Cdd:PRK10982 481 NEILRL 486
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1296-1471 |
1.98e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1296 KRKKKIAARNISFCVQEGEILGLLGPNGAGKSS-----SIRMISGITkpTAGEVELKGC---SSVLGHLGYCPQENVLWP 1367
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTllnvlAERVTTGVI--TGGDRLVNGRpldSSFQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1368 MLTLREHLEVYAAvkgLR---------KADARLAIARLVSAFKLHEQL-NVPVQKLTAGITRKLCFVLSLLGNSPVLL-L 1436
Cdd:TIGR00956 850 TSTVRESLRFSAY---LRqpksvskseKMEYVEEVIKLLEMESYADAVvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|....*..
gi 27436953 1437 DEPSTGIDptgQQQMWQAIQAVVK--NTERGVLLTTH 1471
Cdd:TIGR00956 927 DEPTSGLD---SQTAWSICKLMRKlaDHGQAILCTIH 960
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1313-1455 |
2.14e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1313 GEILGLLGPNGAGKSSSIRMISGITKPTAGEVEL-KGCSsvlghLGYCPQenvlwpmltlrEHLEVYAAVKGLRKADARL 1391
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIK-----LGYFAQ-----------HQLEFLRADESPLQHLARL 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436953 1392 AIARL-------VSAFKLH-EQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGIDPTGQQQMWQAI 1455
Cdd:PRK10636 402 APQELeqklrdyLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1304-1363 |
2.37e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 2.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVlghlGYCPQEN 1363
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANI----GYYAQDH 391
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
494-534 |
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 27436953 494 VEALKGLLfdiyEGQITAILGHSGAGKSSLLN-ILNGLSVPT 534
Cdd:PRK00098 155 LDELKPLL----AGKVTVLAGQSGVGKSTLLNaLAPDLELKT 192
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1304-1375 |
2.61e-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: 44.85 E-value: 2.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKgcssvlGHLGYCPQenVLWPML-TLREHL 1375
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS------GRISFSSQ--FSWIMPgTIKENI 118
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-646 |
3.16e-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: 45.67 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTiYNKNLSemqdleeirkitgVCPQFNVqfdIL--TVK 574
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRIS-------------FSPQTSW---IMpgTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 575 ENLslfakIKGIHLKEVEQE--VQRILLELDMQNI--QDNL-----AKHLSEGQKRKLTFGITILGDPQILLLDEPTTGL 645
Cdd:TIGR01271 505 DNI-----IFGLSYDEYRYTsvIKACQLEEDIALFpeKDKTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
.
gi 27436953 646 D 646
Cdd:TIGR01271 580 D 580
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
497-663 |
3.54e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 497 LKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTiynknlsemqdleeirkitgvCPQfnvQFDIL----- 571
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------------------RPA---GARVLflpqr 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 ------TVKENLSLFAKIKGIHLKEVEQEVQRILLE--LDMQNIQDNLAKHLSEGQKRKLTFGITILGDPQILLLDEPTT 643
Cdd:COG4178 435 pylplgTLREALLYPATAEAFSDAELREALEAVGLGhlAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180
....*....|....*....|
gi 27436953 644 GLDPFSRDQVWSLLRERRAD 663
Cdd:COG4178 515 ALDEENEAALYQLLREELPG 534
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1302-1336 |
4.67e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 4.67e-04
10 20 30
....*....|....*....|....*....|....*
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGI 1336
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV 54
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1304-1444 |
5.18e-04 |
|
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: 44.94 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCS-------SVLGHLGYCPQENVLWPMlTLREHLE 1376
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglhDLRFKITIIPQDPVLFSG-SLRMNLD 1381
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436953 1377 VYAAVKGLRKADArLAIARL---VSAF--KLHEQLNVPVQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:TIGR00957 1382 PFSQYSDEEVWWA-LELAHLktfVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
498-697 |
7.38e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 498 KGLLFD----IYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVtiynknLSEmqdleeiRKITGVcPQfnvQFDIL-- 571
Cdd:PTZ00243 673 KVLLRDvsvsVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAE-------RSIAYV-PQ---QAWIMna 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 572 TVKENLSLFAKIKGIHLKEVEQEVQrilLELDMQNIQDNLAK-------HLSEGQKRKLTFGITILGDPQILLLDEPTTG 644
Cdd:PTZ00243 736 TVRGNILFFDEEDAARLADAVRVSQ---LEADLAQLGGGLETeigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27436953 645 LDPFSRDQ-VWSLLRERRADHVILFSTQSMDEADiLADRKVIMSNGRLKCAGSS 697
Cdd:PTZ00243 813 LDAHVGERvVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSS 865
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1302-1491 |
7.47e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1302 AARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEVELKGCSSVLGHLGYcPQENVLWPMLTLREHLEVYAAV 1381
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTK-EKEKVLEKLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1382 KGLRKadaRLAIARLVSAFKLHEQ------------LNVPVQ---KLTAGITRKLCFVLSLLGNSP-------------- 1432
Cdd:PRK13651 101 KEIRR---RVGVVFQFAEYQLFEQtiekdiifgpvsMGVSKEeakKRAAKYIELVGLDESYLQRSPfelsggqkrrvala 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436953 1433 --------VLLLDEPSTGIDPTGQQQMWQAIQAVVKNTeRGVLLTTHNLAEAEALCDRVAIMVSGRL 1491
Cdd:PRK13651 178 gilamepdFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
479-529 |
1.27e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 27436953 479 RIRNVKKEYKGksgkVEALKGLLFDIYEGQITAILGHSGAGKSSLLNILNG 529
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1289-1344 |
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 27436953 1289 QKKSCFSKRKKKIAARN-ISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV 1344
Cdd:PRK15079 22 DGKQWFWQPPKTLKAVDgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV 78
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1300-1344 |
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 27436953 1300 KIAARNISFCVQEGEILGLLGPNGAGKSSSIRMISGITKPTAGEV 1344
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
866-1167 |
1.39e-03 |
|
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: 42.76 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 866 IFPLIVENIMYAMLNEKIDWEFKNELYFLSPgqlpQEPRTSLLIINNTESNieDFIKSLKHQNILLEVDDFENRNGTDGL 945
Cdd:pfam12698 9 LLPILLILLLGLIFSNAVNDPEELPVAVVDE----DNSSLSRQLVRALEAS--PTVNLVQYVDSEEEAKEALKNGKIDGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 946 SY--NGAIIVSGKQKDYRFSVVCNTKRLHCFPILMNIIsNGLLQMFNHTQ---HIRIESSPFPLSHIGLWTGLPDGSF-- 1018
Cdd:pfam12698 83 LVipKGFSKDLLKGESATVTVYINSSNLLVSKLILNAL-QSLLQQLNASAlvlLLEALSTSAPIPVESTPLFNPQSGYay 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1019 ----FLFLVLCSISPYITMGSISDYKKN-AKSQLWISGLYTSAYWCGQALVDvsFFILILLLMYLIFYIENMQYLLITSQ 1093
Cdd:pfam12698 162 ylvgLILMIIILIGAAIIAVSIVEEKESrIKERLLVSGVSPLQYWLGKILGD--FLVGLLQLLIILLLLFGIGIPFGNLG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436953 1094 IVFALVIVtpgYAASLVFFIYMISFIFRKRRKNSGLWSFYFFFASTIMFSITLINHFDlSILITTMVLVPSYTL 1167
Cdd:pfam12698 240 LLLLLFLL---YGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPP-SFLQWIFSIIPFFSP 309
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1304-1471 |
1.78e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1304 RNISFCVQEGEILGLLGPNGAGKSSSIRMISGitKPTAGEVElkGCSSVLGH----------LGYCPQENVLWPMLTLRE 1373
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE--GDIRISGFpkkqetfariSGYCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 1374 HLeVYAAVKGLRKADARLAIARLV-SAFKLHEQLNVP--------VQKLTAGITRKLCFVLSLLGNSPVLLLDEPSTGID 1444
Cdd:PLN03140 973 SL-IYSAFLRLPKEVSKEEKMMFVdEVMELVELDNLKdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180
....*....|....*....|....*..
gi 27436953 1445 PTGQQQMWQAIQAVVkNTERGVLLTTH 1471
Cdd:PLN03140 1052 ARAAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
583-669 |
2.08e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 42.80 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436953 583 IKGIHLKEVEQEVQRILLELDMQNiQDNLAKHLSEGQKRKLTF--------GITILGDPQILLLDEPTTGLDPFSRDQVW 654
Cdd:COG4694 461 FDEFSLEAVEDGRSSYRLKRNGEN-DAKPAKTLSEGEKTAIALayflaeleGDENDLKKKIVVIDDPVSSLDSNHRFAVA 539
|
90
....*....|....*..
gi 27436953 655 SLLRER--RADHVILFS 669
Cdd:COG4694 540 SLLKELskKAKQVIVLT 556
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
467-540 |
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 27436953 467 PVAPEFqGKEAIRIRNVKKEYKGKSgkveALKGLLFDIYEGQITAILGHSGAGKSSLLNILNGLSVPTEGSVTI 540
Cdd:PRK11819 315 PPGPRL-GDKVIEAENLSKSFGDRL----LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| |
