|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-1054 |
4.46e-177 |
|
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: 570.80 E-value: 4.46e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 12 SQVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY 91
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 92 KQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCGSSVFLKRLYGVGSHIVMVK------------EPVC---------- 149
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRkmkniqsqrggcEGTCsctskgfstr 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 150 ----------------DVDEISKLIHYYIPTATLKTNVGNELSFILP-KEYTHK-FEALLTALEENQENLGISSFGMSIT 211
Cdd:TIGR01257 1188 cparvdeitpeqvldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPnKNFKQRaYASLFRELEETLADLGLSSFGISDT 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 212 TMEEVFLRVSKMEDS----------------------KPDMEATQSPSAGSKGNRNRDVESSmRAGFPTQSEDQTIVFNT 269
Cdd:TIGR01257 1268 PLEEIFLKVTEDADSgslfaggaqqkrenanlrhpcsGPTEKAGQTPQASHTCSPGQPAAHP-EGQPPPEPEDPGVPLNT 1346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 270 GCPLYLQQFHAMFMKRLMYNWRNWRVLSVQILGLVISTFLLLKSH----EFRHKRIRQMNLDDYGQTIVPFSILGKSNLT 345
Cdd:TIGR01257 1347 GARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSiiipPFGEYPALTLHPWMYGQQYTFFSMDEPNSEH 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 346 TSLLIH-LENMLKPGNHQLKE------------------VQGDLLKYLEGNE----------------------EC---- 380
Cdd:TIGR01257 1427 LEVLADvLLNKPGFGNRCLKEewlpeypcgnstpwktpsVSPNITHLFQKQKwtaahpspscrcstrekltmlpECpega 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 381 ------------------------------IHLCIVALSIK--------------------------------------- 391
Cdd:TIGR01257 1507 gglpppqrtqrsteilqdltdrnisdflvkTYPALIRSSLKskfwvneqryggisiggklpaipitgealvgflsdlgqm 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 392 --VAAG-------------------RAKLTVLFNNEAYHSPSLSLAVLDN-ILFMSL----SGANASITVFhkPQPRPTS 445
Cdd:TIGR01257 1587 mnVSGGpvtreaskempdflkhletEDNIKVWFNNKGWHALVSFLNVAHNaILRASLpkdrDPEEYGITVI--SQPLNLT 1664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 446 KEWPR------STYGKIVAFKIQLGMALLVSGFCILTVTERITKAKHMQFLSGASVLVYWLSALVFDFIIFFISCCFLLV 519
Cdd:TIGR01257 1665 KEQLSeitvltTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVG 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 520 MFKYYKIDIYVTDYHILETMLILILFGWSAIPLTYLMSFLFSKSIPAYIQLLVFYYLSGTSGLLIDTIIEAGLSTIISNS 599
Cdd:TIGR01257 1745 IFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLR 1824
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 600 TQTFLLSSLLFFPTYNLGKCISEytviyqrkiLCIQQKNVLKYLNCSKEYTKKniySLKKPMIGKYLIAMSIAGFVYLLf 679
Cdd:TIGR01257 1825 FNAMLRKLLIVFPHFCLGRGLID---------LALSQAVTDVYAQFGEEHSAN---PFQWDLIGKNLVAMAVEGVVYFL- 1891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 680 iffweniswkLRMLIHQHIYFG--VCKKYKSDIisnelsgTSEDNDVENERREILYQPEKflnCPVL-IKQLTKIY--FK 754
Cdd:TIGR01257 1892 ----------LTLLIQHHFFLSrwIAEPAKEPI-------FDEDDDVAEERQRIISGGNK---TDILrLNELTKVYsgTS 1951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 755 SPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQFDALLEYLT 834
Cdd:TIGR01257 1952 SP---AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLT 2028
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 835 GWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRL 914
Cdd:TIGR01257 2029 GREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 915 LWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNKFGDIYILKTKVKSGE-----TLKEFKNF 989
Cdd:TIGR01257 2109 LWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllpDLNPVEQF 2188
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 990 ITLTFPGSELKQENQGILNYYIPSkdNSWGKVFGILEKAKEQYDLEDYSISQITLDQVFLAFADQ 1054
Cdd:TIGR01257 2189 FQGNFPGSVQRERHYNMLQFQVSS--SSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQ 2251
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
743-964 |
5.81e-101 |
|
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: 316.37 E-value: 5.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYfKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGY 822
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 903 PSTGMDPRARRLLWDAVIKIReSGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLK 964
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
745-972 |
7.34e-82 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 265.77 E-value: 7.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKsplILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCP 824
Cdd:COG1131 3 VRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 905 TGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNKF-GDIYI 972
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLlEDVFL 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
743-964 |
1.45e-60 |
|
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: 206.07 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKsplILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGY 822
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 903 PSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLK 964
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
745-954 |
1.91e-59 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 201.09 E-value: 1.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCP 824
Cdd:cd03230 3 VRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMvmyariwgiserqirpyvntylnslelephanslisTYSEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 905 TGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
745-969 |
8.20e-59 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 202.01 E-value: 8.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCP 824
Cdd:COG4555 4 VENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 905 TGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNKFGD 969
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-132 |
2.51e-52 |
|
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: 182.70 E-value: 2.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 12 SQVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY 91
Cdd:cd03263 100 ARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV 179
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958644180 92 KQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCGSSVFLK 132
Cdd:cd03263 180 RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
477-968 |
2.00e-47 |
|
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: 185.99 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 477 VTERITKAKHMQFLSGASVLVYWLSALVFDFIIFFISCCFLLVMFKYYKIdIYVTDYHILetMLILILFGWSAIPLTYLM 556
Cdd:TIGR01257 675 VLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRI-LHYSDPFIL--FLFLLAFSTATIMQCFLL 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 557 SFLFSK-SIPAYIQLLVFY--YLSGTSGLLIDTIIEAGLSTIISnstqtfLLSSLLF-FPTynlgkcisEYTVIYQRKIL 632
Cdd:TIGR01257 752 STFFSKaSLAAACSGVIYFtlYLPHILCFAWQDRMTADLKTAVS------LLSPVAFgFGT--------EYLVRFEEQGL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 633 CIQQKNVLKYLNCSKEYTkkniYSLKKPMIgkyLIAMSIAGFV--YLLFIF---FWENISWklrmlihqhiYFGVCKKYk 707
Cdd:TIGR01257 818 GLQWSNIGNSPLEGDEFS----FLLSMKMM---LLDAALYGLLawYLDQVFpgdYGTPLPW----------YFLLQESY- 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 708 sdIISNELSGTSEDNDVE-----NERREILYQPEKFLNC-----------PVLIKQLTKIY--FKSPlilAVKNISLAIQ 769
Cdd:TIGR01257 880 --WLGGEGCSTREERALEkteplTEEMEDPEHPEGINDSfferelpglvpGVCVKNLVKIFepSGRP---AVDRLNITFY 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 770 ERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQFDALLEYLTGWEIMVMYARIWGIS 849
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRS 1034
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 850 ERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIReSGKAI 929
Cdd:TIGR01257 1035 WEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTI 1113
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958644180 930 IITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNKFG 968
Cdd:TIGR01257 1114 IMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFG 1152
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
759-963 |
3.70e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 171.14 E-value: 3.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQFDALLEYLTGWEI 838
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDA 918
Cdd:PRK13537 101 LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958644180 919 VIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PRK13537 181 LRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
743-954 |
4.72e-46 |
|
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: 164.85 E-value: 4.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIY-FKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIG 821
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 902 EPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
761-963 |
5.92e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 168.86 E-value: 5.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQFDALLEYLTGWEIMV 840
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 841 MYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVI 920
Cdd:PRK13536 137 VFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLR 216
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958644180 921 KIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PRK13536 217 SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
745-1048 |
2.28e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 165.67 E-value: 2.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKiYFKSplILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDvlkVRSKIGYCP 824
Cdd:COG4152 4 LKGLTK-RFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 qfdallE----Y--LTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:COG4152 78 ------EerglYpkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNKFGDIYIlktKVK 978
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL---RLE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 979 SGETLKEFKNfitltFPGSELKQENQGILNYYIPSKDNSWgkvfGILEKAKEQYDLEDYSISQITLDQVF 1048
Cdd:COG4152 229 ADGDAGWLRA-----LPGVTVVEEDGDGAELKLEDGADAQ----ELLRALLARGPVREFEEVRPSLNEIF 289
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
760-953 |
4.41e-45 |
|
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: 161.68 E-value: 4.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVlkvRSKIGYCPQFDALLEYLTGWEIM 839
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA---RNRIGYLPEERGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 840 VMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAV 919
Cdd:cd03269 92 VYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190
....*....|....*....|....*....|....
gi 1958644180 920 IKIRESGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:cd03269 172 RELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
745-961 |
7.09e-44 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 159.03 E-value: 7.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYC 823
Cdd:COG1122 3 LENLSFSYPGGTPAL--DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLReLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 824 PQF-DALLeyltgweIM------VMYA-RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLS--TAIAMmg 893
Cdd:COG1122 81 FQNpDDQL-------FAptveedVAFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAiaGVLAM-- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 894 KPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
745-955 |
3.32e-43 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 156.20 E-value: 3.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSpliLAVKNISLAIQErECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCP 824
Cdd:cd03264 3 LENLTKRYGKK---RALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 905 TGMDPRARrllwdavIKIRE------SGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:cd03264 159 AGLDPEER-------IRFRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
745-954 |
1.76e-41 |
|
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: 151.22 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKsplILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVlKVRSKIGYCP 824
Cdd:cd03268 3 TNDLTKTYGK---KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVMYARIWGISERQIrpyvNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 905 TGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
760-953 |
2.04e-40 |
|
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: 148.38 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQF-DALLEYLTGWE 837
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLVFQNpDDQFFGPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWD 917
Cdd:cd03225 96 EVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958644180 918 AVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:cd03225 176 LLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
15-127 |
2.09e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.36 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 15 KGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-Q 93
Cdd:COG1131 101 YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAaE 180
|
90 100 110
....*....|....*....|....*....|....
gi 1958644180 94 NRTILLTTHYMDEADMLGDRIAIMVQGTLRCCGS 127
Cdd:COG1131 181 GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
745-934 |
9.48e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 143.39 E-value: 9.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLilaVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCP 824
Cdd:COG4133 5 AENLSCRRGERLL---FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVMYARIWGISERQIRpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|
gi 1958644180 905 TGMDPRARRLLWDAVIKIRESGKAIIITSH 934
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
758-961 |
3.01e-37 |
|
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: 140.26 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT--KDVLKVRSKIGYCPQFDALLEYLTG 835
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglPPHEIARLGIGRTFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WE-IMV---------MYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPST 905
Cdd:cd03219 93 LEnVMVaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 906 GMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:cd03219 173 GLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
745-953 |
6.51e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.22 E-value: 6.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYC 823
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 824 PQFdalleyltgweimvmyariwgiserqirpyvntylnslelephanslistySEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 904 STGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
745-961 |
2.36e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.77 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSK--IGY 822
Cdd:COG1137 6 AENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWE-IMvMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:COG1137 83 LPQEASIFRKLTVEDnIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 902 EPSTGMDPRA----RRLlwdaVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:COG1137 162 EPFAGVDPIAvadiQKI----IRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
759-961 |
2.38e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.83 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitKDVLKVRSKIGYCPQ---FDALLeYLTG 835
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGYVPQraeVDWDF-PITV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WEIMVM--YARI--WGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRA 911
Cdd:COG1121 95 RDVVLMgrYGRRglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 912 RRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLsIMVHGKLTCLGSPQ 961
Cdd:COG1121 175 EEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPE 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
747-965 |
6.11e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 130.36 E-value: 6.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 747 QLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSK--IGYCP 824
Cdd:cd03218 5 NLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 905 TGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKN 965
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
760-961 |
7.35e-34 |
|
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: 130.93 E-value: 7.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKdvLK----VRSKIGYCPQ----FDAL-- 829
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPphriARLGIARTFQnprlFPELtv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 830 LEYL---------TGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:COG0411 97 LENVlvaaharlgRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
16-220 |
2.18e-33 |
|
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: 130.97 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ-N 94
Cdd:TIGR01188 95 GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEeG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 95 RTILLTTHYMDEADMLGDRIAIMVQGTLRCCGSSVFLKRLYGvGSHIVMVKEPVCDVD-EISKLIHYYIPT--ATLKTNV 171
Cdd:TIGR01188 175 VTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKvEVSMLIAELGETglGLLAVTV 253
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958644180 172 GNELSFILPKEYTHKFEALLTALEENqeNLGISSFGMSITTMEEVFLRV 220
Cdd:TIGR01188 254 DSDRIKILVPDGDETVPEIVEAAIRN--GIRIRSISTERPSLDDVFLKL 300
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
745-965 |
4.43e-33 |
|
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: 128.16 E-value: 4.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSK--IGY 822
Cdd:TIGR04406 4 AENLIKSYKKRK---VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWE-IMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:TIGR04406 81 LPQEASIFRKLTVEEnIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 902 EPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKN 965
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-132 |
4.96e-33 |
|
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: 127.49 E-value: 4.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK--Q 93
Cdd:cd03265 102 GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeF 181
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958644180 94 NRTILLTTHYMDEADMLGDRIAIMVQGTLRCCGSSVFLK 132
Cdd:cd03265 182 GMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
743-954 |
5.41e-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: 127.25 E-value: 5.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITkDVLKVRSKIGY 822
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 903 PSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
745-960 |
3.03e-32 |
|
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: 125.88 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYC 823
Cdd:cd03295 3 FENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 824 PQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPH--ANSLISTYSEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 902 EPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSP 960
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
760-958 |
3.90e-32 |
|
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: 124.57 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitKDVLKVRSKIGYCPQ-FDALLEY-LTGWE 837
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIGYVPQrRSIDRDFpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVM--YARIWGI-----SERQIrpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPR 910
Cdd:cd03235 90 VVLMglYGHKGLFrrlskADKAK---VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958644180 911 ARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLsIMVHGKLTCLG 958
Cdd:cd03235 167 TQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
743-949 |
3.89e-31 |
|
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: 121.81 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYF-KSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITkdvlKVRSKIG 821
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQFDALLEYLTGWEiMVMYA-RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:cd03293 77 YVFQQDALLPWLTVLD-NVALGlELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIM 949
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
761-905 |
6.76e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 118.90 E-value: 6.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQFDALLEYLTGWEIM 839
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 840 VMYARIWGISERQIRPYVNTYLNSLELEPHANSLI----STYSEGNKRRLSTAIAMMGKPSVIFLDEPST 905
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
758-1047 |
9.94e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 124.04 E-value: 9.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKI----GycpQFDALLEYL 833
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIgvvfG---QRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARR 913
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 914 LLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNKFGDIYILKTkvksgeTLKEFKNFITL 992
Cdd:COG4586 192 AIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVL------ELAEPVPPLEL 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 993 TFPGSELKQENqGILNYYIPSKDNswgkVFGILEKAKEQYDLEDYSISQITLDQV 1047
Cdd:COG4586 266 PRGGEVIEREG-NRVRLEVDPRES----LAEVLARLLARYPVRDLTIEEPPIEEV 315
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
760-968 |
1.60e-30 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 130.24 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQFDALLEYLTGWEIM 839
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 840 VMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAV 919
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 920 IKI-RESGKAIIITSHSMEECEaLCTRLSIMVHGKLTCLGSPQYLKNKFG 968
Cdd:NF033858 441 IELsREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
757-955 |
8.75e-30 |
|
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: 118.59 E-value: 8.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 757 LILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYC-PQFDALLEYLTG 835
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRA---- 911
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAqeni 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644180 912 RRLLWDAVikiRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:cd03267 193 RNFLKEYN---RERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
46-122 |
1.99e-29 |
|
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: 115.57 E-value: 1.99e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-230 |
3.20e-29 |
|
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: 127.05 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 12 SQVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD-VVQT 90
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtIVSI 2116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 91 YKQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCGSSVFLKRLYGVGSHIVM-VKEP----VCDVDEISKLIHYYIPTA 165
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPkddlLPDLNPVEQFFQGNFPGS 2196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 166 TLKTNVGNELSFILPKEYTHKFEALLTAleeNQENLGISSFGMSITTMEEVFLRVSKMEDSKPDM 230
Cdd:TIGR01257 2197 VQRERHYNMLQFQVSSSSLARIFQLLIS---HKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYDL 2258
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
745-954 |
4.96e-29 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 115.66 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPL-ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-----DVLKVRS 818
Cdd:cd03255 3 LKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekeLAAFRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 819 KIGYCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEEcEALCTRLSIMVHGKL 954
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
745-959 |
6.81e-29 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 115.76 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYF-KSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKVRSK 819
Cdd:cd03258 4 LKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 IGYCPQFDALLEYLTGWEiMVMYA-RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFE-NVALPlEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGS 959
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
742-961 |
8.32e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 121.93 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 742 PVL-IKQLTKIY--FKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVL 814
Cdd:COG1123 259 PLLeVRNLSKRYpvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 815 KVRSKIGYCPQ--FDALLEYLTGWEIMVMYARIWGI-SERQIRPYVNTYLNSLELEP-HANSLISTYSEGNKRRLSTAIA 890
Cdd:COG1123 339 ELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 891 MMGKPSVIFLDEPSTGMDPRAR----RLLWDAVikiRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQaqilNLLRDLQ---RELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
762-965 |
2.76e-28 |
|
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: 114.14 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKVRSKIGYCPQFDALLEYLTGWE 837
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMYARIWGI-SERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLW 916
Cdd:cd03261 97 NVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 917 DAVIKIRES-GKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKN 965
Cdd:cd03261 177 DLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
742-960 |
5.69e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 742 PVLIKQLTKIYFK-SPL-ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK---V 816
Cdd:PRK13637 2 SIKIENLTHIYMEgTPFeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 817 RSKIGYCPQFDallEYLTGWEimVMYARI------WGISERQIRPYVNTYLN--SLELEPHANSLISTYSEGNKRRLSTA 888
Cdd:PRK13637 82 RKKVGLVFQYP---EYQLFEE--TIEKDIafgpinLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 889 --IAMmgKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGK-AIIITSHSMEECEALCTRLSIMVHGKLTCLGSP 960
Cdd:PRK13637 157 gvVAM--EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
742-961 |
1.26e-27 |
|
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: 118.47 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 742 PVL-IKQLTkIYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTA---GDVFIDGISITKDVLKVR 817
Cdd:COG1123 3 PLLeVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 818 SK-IGYCPQ-FDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKP 895
Cdd:COG1123 82 GRrIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 896 SVIFLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
745-953 |
1.37e-27 |
|
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: 110.35 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKsplILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT---KDVLKVRSKIG 821
Cdd:cd03229 3 LKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdleDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQFDALLEYLTGWEImVMYAriwgiserqirpyvntylnslelephanslistYSEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:cd03229 80 MVFQDFALFPHLTVLEN-IALG---------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 902 EPSTGMDPRARRLLWDAVIKIRE-SGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
743-971 |
2.79e-27 |
|
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: 111.17 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSpliLAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITkDVLKVRSKIGY 822
Cdd:cd03300 1 IELENVSKFYGGF---VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 903 PSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQylknkfgDIY 971
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE-------EIY 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
761-961 |
3.02e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.52 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSK--IGYCPQFDALLEYLTGWEI 838
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMYARIW-GISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWD 917
Cdd:PRK10895 99 LMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644180 918 AVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK10895 179 IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPT 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
760-960 |
7.44e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 7.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitkdvlkvrsKIGycpqfdALLEY------- 832
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVS------ALLELgagfhpe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 833 LTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEP-STGmDPRA 911
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DAAF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958644180 912 RRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSP 960
Cdd:COG1134 182 QKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
761-961 |
1.25e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 110.13 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKdvLKVRS---KIGYCPQFDALLEYLTGWE 837
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS--LSRRElarRIAYVPQEPPAPFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 iMVMYARI--------WGISERQIrpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDP 909
Cdd:COG1120 95 -LVALGRYphlglfgrPSAEDREA---VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 910 RARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:COG1120 171 AHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
758-958 |
1.27e-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: 109.16 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitkdvlKVRSKIGYCPQFDallEYLTGWE 837
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSSLLGLGGGFN---PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEP-STGmDPRARRLLW 916
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958644180 917 DAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLG 958
Cdd:cd03220 183 RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
761-953 |
1.71e-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: 109.40 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAG-DVFIDGISITK-DVLKVRSKIGYC-PQF-DALLEYLTGW 836
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGeDVWELRKRIGLVsPALqLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 837 EiMVM---YARI--WG-ISERQIRpYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPR 910
Cdd:COG1119 99 D-VVLsgfFDSIglYRePTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644180 911 ARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:COG1119 177 ARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
733-972 |
4.43e-26 |
|
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: 108.88 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 733 YQPEKFLNCPVLIKQLTKIYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-- 810
Cdd:cd03294 12 KNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAam 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 811 --KDVLKVRSK-IGYCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLST 887
Cdd:cd03294 92 srKELRELRRKkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 888 AIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNK 966
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
....*.
gi 1958644180 967 FGDIYI 972
Cdd:cd03294 252 PANDYV 257
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
745-955 |
1.15e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 104.43 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYfksPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDG--ISITKDVLKVRSKIGY 822
Cdd:cd03216 3 LRGITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFdalleyltgweimvmyariwGISERQirpyvntylnslelephanslistysegnkrRLSTAIAMMGKPSVIFLDE 902
Cdd:cd03216 80 VYQL--------------------SVGERQ-------------------------------MVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 903 PSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
744-954 |
1.64e-25 |
|
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: 104.94 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 744 LIKQLTKIYFKSPLILaVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTA--GDVFIDGISITKDVLkvRSKIG 821
Cdd:cd03213 9 LTVTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF--RKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQFDALLEYLTGWEIMVMYARIWGIserqirpyvntylnslelephanslistySEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 902 EPSTGMDPRARRLLWDAVIKIRESGKAIIITSHS-MEECEALCTRLSIMVHGKL 954
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
745-937 |
2.31e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.52 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLILavKNISLAIQERE-CFgLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK----DVLKVRSK 819
Cdd:COG2884 4 FENVSKRYPGGREAL--SDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 IGYCPQfDA-LLEYLTGWEiMVMYA-RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSV 897
Cdd:COG2884 81 IGVVFQ-DFrLLPDRTVYE-NVALPlRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958644180 898 IFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSME 937
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
745-954 |
2.34e-25 |
|
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: 105.67 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIY-FKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKVRSK 819
Cdd:cd03257 4 VKNLSVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 IGYCPQ--FDALLEYLTGWEIMVMYARIWGI--SERQIRPYVNTYLNSLELEP-HANSLISTYSEGNKRRLSTAIAMMGK 894
Cdd:cd03257 84 IQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 895 PSVIFLDEPSTGMDPRARRLLWDAVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
745-955 |
4.08e-25 |
|
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: 104.26 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLkvRSKIGYCP 824
Cdd:cd03226 2 IENISFSYKKGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 Q-------FDALLEYLtgweimvmYARIWGISERQIRpyVNTYLNSLEL----EPHANSListySEGNKRRLSTAIAMMG 893
Cdd:cd03226 78 QdvdyqlfTDSVREEL--------LLGLKELDAGNEQ--AETVLKDLDLyalkERHPLSL----SGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 894 KPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
760-953 |
5.97e-25 |
|
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: 104.05 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK--DVLKVRSKIGYCPQFDALLEYLTGWE 837
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlpPHERARAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMYARIWGISERQIRP-YVntylnsLELEP----HANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRAR 912
Cdd:cd03224 95 NLLLGAYARRRAKRKARLeRV------YELFPrlkeRRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958644180 913 RLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:cd03224 169 EEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-121 |
3.39e-24 |
|
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: 101.77 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 18 PQNMCLEE------TNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY 91
Cdd:cd03225 101 LENLGLPEeeieerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKL 180
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 92 K-QNRTILLTTHYMDEADMLGDRIAIMVQGT 121
Cdd:cd03225 181 KaEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
758-965 |
5.34e-24 |
|
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: 101.98 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKdvLK----VRSKIGYCPQFDALLEYL 833
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG--LPphriARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWE--IMVMYARIWGISERQIRPYVntylnsLE----LEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGM 907
Cdd:COG0410 94 TVEEnlLLGAYARRDRAEVRADLERV------YElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 908 DPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKN 965
Cdd:COG0410 168 APLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
717-961 |
5.65e-24 |
|
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: 107.20 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 717 GTSEDndVENERREILYQPEKFLNC----PVL-IKQLTKIYF--KSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQ 789
Cdd:TIGR03269 251 GTPDE--VVAVFMEGVSEVEKECEVevgePIIkVRNVSKRYIsvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 790 ILTGEITPTAGDVFI----DGISITK--DVLKVRSK--IGYCPQFDAL------LEYLTG-------WEIMVMYA----R 844
Cdd:TIGR03269 329 IIAGVLEPTSGEVNVrvgdEWVDMTKpgPDGRGRAKryIGILHQEYDLyphrtvLDNLTEaiglelpDELARMKAvitlK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 845 IWGISERQIRPYVNTYlnslelePHanslisTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRE 924
Cdd:TIGR03269 409 MVGFDEEKAEEILDKY-------PD------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKARE 475
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958644180 925 S-GKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:TIGR03269 476 EmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
745-954 |
6.15e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.39 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIY-FKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKVRSK 819
Cdd:COG1135 4 LENLSKTFpTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalseRELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 IGYCPQFDALLEYLTGWEiMVMYA-RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAE-NVALPlEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 899 FLDEPSTGMDPRA-RRLLwdAVIK-I-RESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:COG1135 163 LCDEATSALDPETtRSIL--DLLKdInRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
746-972 |
7.39e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.50 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 746 KQLTK--IYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK----DVLKV-RS 818
Cdd:PRK10070 27 QGLSKeqILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVrRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 819 KIGYCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNKFGDIYI 972
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
745-981 |
8.48e-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: 104.02 E-value: 8.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitKDVLKV---RSKIG 821
Cdd:COG3842 8 LENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLppeKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQFDALLEYLTGWEImVMYA-RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRR--LSTAIAMmgKPSVI 898
Cdd:COG3842 81 MVFQDYALFPHLTVAEN-VAFGlRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRvaLARALAP--EPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL----KNKF-----G 968
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIyerpATRFvadfiG 237
|
250
....*....|...
gi 1958644180 969 DIYILKTKVKSGE 981
Cdd:COG3842 238 EANLLPGTVLGDE 250
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
743-958 |
2.61e-23 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 99.25 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitKDVLKVRSK--- 819
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG----RDVTDLPPKdrd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 IGYCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIF 899
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 900 LDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLG 958
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-127 |
3.79e-23 |
|
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: 99.33 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 18 PQNMCLEE------TNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY 91
Cdd:COG1122 101 PENLGLPReeirerVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL 180
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958644180 92 -KQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCGS 127
Cdd:COG1122 181 nKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-220 |
4.57e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.95 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK 92
Cdd:COG4152 97 RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 93 QN-RTILLTTHYMDEADMLGDRIAIMVQGTLRCCGSSVFLKRLYGVGSHIVMVKEpvcDVDEISKLihyyiPTATLKTNV 171
Cdd:COG4152 177 AKgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADG---DAGWLRAL-----PGVTVVEED 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958644180 172 GNELSFILPKEYTHkfEALLTALeenQENLGISSFGMSITTMEEVFLRV 220
Cdd:COG4152 249 GDGAELKLEDGADA--QELLRAL---LARGPVREFEEVRPSLNEIFIEV 292
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
758-1054 |
5.92e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 101.74 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLLGFNGAGKTTTfqILTGEIT-PTAGDVFIDGISITKDVLKVRSKIG-YCPQFDALLEYLTG 835
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RG--ALPAHV*gPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLL 915
Cdd:NF000106 104 RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 916 WDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNKFGDiYILKTKVKSGETLKEFKNFITLT-- 993
Cdd:NF000106 184 WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGG-RTLQIRPAHAAELDRMVGAIAQAgl 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 994 --FPGSELKQENqGILNYYIPSkDNSWGKVFGILekAKEQYDLEDYSISQITLDQVFLAFADQ 1054
Cdd:NF000106 263 dgIAGATADHED-GVVNVPIVS-DEQLSAVVGML--GERGFTISGHQHPSAQL*EVFLAITGQ 321
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
745-958 |
6.64e-23 |
|
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: 96.74 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSK-IGYC 823
Cdd:cd03214 2 VENLSVGYGGRTVL---DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 824 PQfdaLLEYLtgweimvmyaRIWGISERQIrpyvntylNSLelephanslistySEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:cd03214 79 PQ---ALELL----------GLAHLADRPF--------NEL-------------SGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 904 STGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLG 958
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
743-961 |
1.50e-22 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 97.80 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRsKIGY 822
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEIMVMYARIWGISER----QIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 899 FLDEPSTGMDPRARRLL--WdavikIRESGKAIIITS----HSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:cd03296 159 LLDEPFGALDAKVRKELrrW-----LRRLHDELHVTTvfvtHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
746-954 |
2.31e-22 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 96.32 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 746 KQLTKIYfkSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKVRSKIG 821
Cdd:cd03292 4 INVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 902 EPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
758-954 |
2.56e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 96.50 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQfDALLEYLTGW 836
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQ-DVTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 837 EIMVMYA------RIWGISERQ-IRPYVNTYLNSLELE--PHANSListySEGNKRRLSTAIAMMGKPSVIFLDEPSTGM 907
Cdd:cd03245 96 DNITLGApladdeRILRAAELAgVTDFVNKHPNGLDLQigERGRGL----SGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958644180 908 DPRARRLLWDAvIKIRESGKAIIITSH--SMEEceaLCTRLSIMVHGKL 954
Cdd:cd03245 172 DMNSEERLKER-LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGRI 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
24-123 |
3.55e-22 |
|
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: 96.85 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTH 102
Cdd:COG4555 111 KRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSH 190
|
90 100
....*....|....*....|.
gi 1958644180 103 YMDEADMLGDRIAIMVQGTLR 123
Cdd:COG4555 191 IMQEVEALCDRVVILHKGKVV 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
754-934 |
3.75e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 96.19 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 754 KSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITP---TAGDVFIDGISITKDvlKVRSKIGYCPQFDALL 830
Cdd:cd03234 18 KYARIL--NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 831 EYLTGWEIMVMYARIWG---ISERQIRPYVNTY-LNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTG 906
Cdd:cd03234 94 PGLTVRETLTYTAILRLprkSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180
....*....|....*....|....*...
gi 1958644180 907 MDPRARRLLWDAVIKIRESGKAIIITSH 934
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
15-126 |
4.31e-22 |
|
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: 95.72 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 15 KGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQN 94
Cdd:cd03264 100 KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED 179
|
90 100 110
....*....|....*....|....*....|..
gi 1958644180 95 RTILLTTHYMDEADMLGDRIAIMVQGTLRCCG 126
Cdd:cd03264 180 RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
758-965 |
4.67e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.60 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQFD--ALLEYLTG 835
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQhvRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WE-IMVMYAR------IWGI--------SERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:PRK11300 98 IEnLLVAQHQqlktglFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKN 965
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
46-121 |
1.70e-21 |
|
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: 92.31 E-value: 1.70e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAIMVQGT 121
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
760-974 |
1.74e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.53 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT---KDVLKVRSKIGYCPQ------FDALL 830
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVFQnpddqlFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 831 EYLTGWEIMVMyariwGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTA--IAMmgKPSVIFLDEPSTGMD 908
Cdd:PRK13639 97 EEDVAFGPLNL-----GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAgiLAM--KPEIIVLDEPTSGLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 909 PRA----RRLLWDavikIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPqylKNKFGDIYILK 974
Cdd:PRK13639 170 PMGasqiMKLLYD----LNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP---KEVFSDIETIR 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
760-971 |
2.81e-21 |
|
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: 94.17 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKVRSKIGYCPQFDALLEYLTG 835
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQLRRQIGMIFQQFNLIERLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WEiMVMYAR------IWGIS------ERQIRPYvntYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:cd03256 96 LE-NVLSGRlgrrstWRSLFglfpkeEKQRALA---ALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 904 STGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNK-FGDIY 971
Cdd:cd03256 172 VASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEvLDEIY 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
760-954 |
9.74e-21 |
|
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: 92.24 E-value: 9.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTG-----EITPTAGDVFIDGISITK---DVLKVRSKIGYCPQFDALLE 831
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldvDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 832 yLTGWEIMVMYARIWGISERQIR--------------PYVNTYLNSLELephanslistySEGNKRRLSTAIAMMGKPSV 897
Cdd:cd03260 95 -GSIYDNVAYGLRLHGIKLKEELderveealrkaalwDEVKDRLHALGL-----------SGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 898 IFLDEPSTGMDPRARRLLWDAVIKIRESgKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03260 163 LLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
760-953 |
1.54e-20 |
|
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: 89.75 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQfDALLEYLTgwei 838
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQ-DPFLFSGT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 mvmyariwgiserqIRpyvntylnslelephANSListySEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDA 918
Cdd:cd03228 92 --------------IR---------------ENIL----SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1958644180 919 VIKIREsGKAIIITSHSMEECEaLCTRLSIMVHGK 953
Cdd:cd03228 139 LRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
761-954 |
2.14e-20 |
|
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: 89.58 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQFDALLEyltgweim 839
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFS-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 840 vmyariwG-ISErqirpyvntylNSLelephanslistySEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDA 918
Cdd:cd03246 90 -------GsIAE-----------NIL-------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958644180 919 VIKIRESGKAIIITSHSMEECEAlCTRLSIMVHGKL 954
Cdd:cd03246 139 IAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
742-954 |
7.60e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 7.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 742 PVL-IKQLTKIYfksPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDG----ISITKDVLkv 816
Cdd:COG1129 3 PLLeMRGISKSF---GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrFRSPRDAQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 817 RSKIGYCPQFDALLEYLTGWE-IMV--MYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMG 893
Cdd:COG1129 78 AAGIAIIHQELNLVPNLSVAEnIFLgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 894 KPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
755-973 |
7.66e-20 |
|
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: 7.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 755 SPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQ----FDA- 828
Cdd:COG2274 487 SPPVL--DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQdvflFSGt 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 829 LLEYLTGWEIMVMYARIWGISER-QIRPYVNTYLNSLE--LEPHANSListySEGNKRRLSTAIAMMGKPSVIFLDEPST 905
Cdd:COG2274 565 IRENITLGDPDATDEEIIEAARLaGLHDFIEALPMGYDtvVGEGGSNL----SGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 906 GMDPRARRLLWDAVIKIREsGKAIIITSHSMeECEALCTRLSIMVHGKLTCLGSPQYLKNKFGDIYIL 973
Cdd:COG2274 641 ALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
745-954 |
9.12e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.17 E-value: 9.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIY-FKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKVRSK 819
Cdd:PRK11153 4 LKNISKVFpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 IGYCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIF 899
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 900 LDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
743-966 |
9.86e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.44 E-value: 9.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKqLTKIYFKSPLI--LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSK 819
Cdd:PRK13632 6 VMIK-VENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 IGYC---P--QF--------------DALLEYLTGWEIMVMYARIWGIserqirpyvntyLNSLELEPHanSListySEG 880
Cdd:PRK13632 85 IGIIfqnPdnQFigatveddiafgleNKKVPPKKMKDIIDDLAKKVGM------------EDYLDKEPQ--NL----SGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 881 NKRRLSTAIAMMGKPSVIFLDEpSTGM-DPRARRLLWDAVIKIRESG-KAIIITSHSMEECeALCTRLSIMVHGKLTCLG 958
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDE-STSMlDPKGKREIKKIMVDLRKTRkKTLISITHDMDEA-ILADKVIVFSEGKLIAQG 224
|
....*....
gi 1958644180 959 SPQ-YLKNK 966
Cdd:PRK13632 225 KPKeILNNK 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
745-936 |
1.46e-19 |
|
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: 88.36 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKiYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT---KDVLKVRSKIG 821
Cdd:cd03262 3 IKNLHK-SFGDFHVL--KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQFDALLEYLTGWEiMVMYARIW--GISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIF 899
Cdd:cd03262 80 MVFQQFNLFPHLTVLE-NITLAPIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958644180 900 LDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSM 936
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEM 195
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
760-976 |
1.50e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.19 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-----KDVLKVRSKIGYCPQF-DALLEYL 833
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIKQIRKKVGLVFQFpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWEIMVMYARIWGISERQIrpyVNTYLNSLELEPHANSLIST----YSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDP 909
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEA---EALAREKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 910 RARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPqylKNKFGDIYILKTK 976
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP---KDIFQDVDFLEEK 242
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
743-963 |
4.47e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSkIGY 822
Cdd:PRK11432 7 VVLKNITKRFGSNTVI---DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD-ICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEiMVMYA-RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:PRK11432 83 VFQSYALFPHMSLGE-NVGYGlKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 902 EPSTGMDPRARRLLWDaviKIRESGKAIIITS----HSMEECEALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PRK11432 162 EPLSNLDANLRRSMRE---KIRELQQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
743-967 |
5.88e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.75 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitKDVLKVRSK--- 819
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTDLPPKdrn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 IGYCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIF 899
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 900 LDEPSTGMDPRARrllWDAVIKI----RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL----KNKF 967
Cdd:COG3839 157 LDEPLSNLDAKLR---VEMRAEIkrlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELydrpANLF 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
742-961 |
6.83e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.89 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 742 PVL-IKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITkDVLKVRSKI 820
Cdd:PRK11607 18 PLLeIRNLTKSFDGQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 821 GYCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKIRES-GKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
742-955 |
7.37e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 742 PVL-IKQLTKIYfksPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDG----ISITKDVLkv 816
Cdd:COG3845 4 PALeLRGITKRF---GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrIRSPRDAI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 817 RSKIGYCPQ-FdALLEYLTGWE-IMVMYARIWGIS------ERQIRPYVNTYlnSLELEPHAnsLISTYSEGNKRRLSTA 888
Cdd:COG3845 79 ALGIGMVHQhF-MLVPNLTVAEnIVLGLEPTKGGRldrkaaRARIRELSERY--GLDVDPDA--KVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 889 IAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
776-934 |
7.76e-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: 85.76 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 776 LLGFNGAGKTTTFQIL-----TGEITptaGDVFIDGISITKDVLKVrskIGYCPQFDALLEYLTGWEIMVMYARIWGISE 850
Cdd:cd03232 38 LMGESGAGKTTLLDVLagrktAGVIT---GEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALLRGLSV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 851 RQirpyvntylnslelephanslistysegnKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAII 930
Cdd:cd03232 112 EQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAIL 162
|
....
gi 1958644180 931 ITSH 934
Cdd:cd03232 163 CTIH 166
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
759-974 |
8.40e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGI--SITKDVLKVRSKIGYCPQ------FDALL 830
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtSDEENLWDIRNKAGMVFQnpdnqiVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 831 EyltgwEIMVMYARIWGISERQIRPYVNTYL---NSLELEPHANSLISTyseGNKRRLSTA--IAMmgKPSVIFLDEPST 905
Cdd:PRK13633 104 E-----EDVAFGPENLGIPPEEIRERVDESLkkvGMYEYRRHAPHLLSG---GQKQRVAIAgiLAM--RPECIIFDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 906 GMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECeALCTRLSIMVHGKLTCLGSPqylKNKFGDIYILK 974
Cdd:PRK13633 174 MLDPSGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP---KEIFKEVEMMK 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-154 |
8.56e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQT-YKQN 94
Cdd:PRK13537 109 GLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARG 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 95 RTILLTTHYMDEADMLGDRIAIMVQGtlrccgssvflKRLYGVGSHIVMVKEPVCDVDEI 154
Cdd:PRK13537 189 KTILLTTHFMEEAERLCDRLCVIEEG-----------RKIAEGAPHALIESEIGCDVIEI 237
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
760-954 |
1.12e-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: 84.79 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK--VRSKIGYCPQfDALLEYLtgwe 837
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAYVPE-DRKREGL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMyariwGISErqirpyvNTYLNSLelephanslistYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWD 917
Cdd:cd03215 90 VLDL-----SVAE-------NIALSSL------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958644180 918 AVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03215 146 LIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
763-961 |
1.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.58 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 763 NISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-----KDVLKVRSKIGYCPQF-DALLEYLTGW 836
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKKLRKKVSLVFQFpEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 837 EIMVMYARIWGISERQIRPYVNTYLNSLEL-EPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLL 915
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958644180 916 WDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK13641 185 MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPK 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
760-961 |
2.01e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI---TKDVLKVRSKIGYCPQ------FDALL 830
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQdpdnqlFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 831 EYLTGWEIMVMyariwGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPR 910
Cdd:PRK13636 101 YQDVSFGAVNL-----KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 911 ARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK13636 176 GVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-120 |
2.04e-18 |
|
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: 85.02 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK 92
Cdd:cd03269 96 QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELA 175
|
90 100
....*....|....*....|....*....
gi 1958644180 93 -QNRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:cd03269 176 rAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
35-120 |
2.24e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 35 LTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQT-YKQNRTILLTTHYMDEADMLGDR 113
Cdd:PRK13536 162 LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDR 241
|
....*..
gi 1958644180 114 IAIMVQG 120
Cdd:PRK13536 242 LCVLEAG 248
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
775-954 |
2.25e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 85.04 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 775 GLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKV-----RSKIGYCPQFDALLEYLTGWEIMVMYARIWGIS 849
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFGLKRKRNR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 850 ERQIRpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRES-GKA 928
Cdd:cd03297 107 EDRIS--VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIP 184
|
170 180
....*....|....*....|....*.
gi 1958644180 929 IIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:cd03297 185 VIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
745-903 |
2.83e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVfidgiSITKDVlkvrsKIGYCP 824
Cdd:COG0488 1 LENLSKSFGGRPLL---DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----SIPKGL-----RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVM-YARIWGISER-------------------------------QIRPYVNTYLNSLELEPH-AN 871
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDgDAELRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEdLD 147
|
170 180 190
....*....|....*....|....*....|..
gi 1958644180 872 SLISTYSEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
760-966 |
6.00e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.17 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQF-DALLEYLTGWE 837
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGLVFQDpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWD 917
Cdd:PRK13647 100 DVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958644180 918 AVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNK 966
Cdd:PRK13647 180 ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
760-972 |
2.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-----KDVLKVRSKIGYCPQF--DALLEY 832
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRPVRKRIGMVFQFpeSQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 833 LTGWEImVMYARIWGISERQIRPYVNTYLNSLELEPHANSLiSTY--SEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPR 910
Cdd:PRK13646 102 TVEREI-IFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQ-SPFqmSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 911 ARRLLWDAVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL---KNKFGDIYI 972
Cdd:PRK13646 180 SKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfkdKKKLADWHI 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
745-970 |
2.56e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKD-VLKVRSKIGYC 823
Cdd:PRK13650 7 VKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 824 ---P--QF-DALLE--YLTGWEIMvmyariwGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKP 895
Cdd:PRK13650 87 fqnPdnQFvGATVEddVAFGLENK-------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 896 SVIFLDEPSTGMDPRARRLLWDAVIKIRES-GKAIIITSHSMEECeALCTRLSIMVHGKLTCLGSPQYLKNKFGDI 970
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
24-122 |
3.08e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 81.40 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTE---KRDAfsKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY--KQNRTIL 98
Cdd:COG4619 108 ERALELLERLGLPPdilDKPV--ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVL 185
|
90 100
....*....|....*....|....
gi 1958644180 99 LTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:COG4619 186 WVSHDPEQIERVADRVLTLEAGRL 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
740-947 |
5.15e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.40 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 740 NCPVLI-KQLTKIYFKSPLILAV-KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVR 817
Cdd:PRK11629 2 NKILLQcDNLCKRYQEGSVQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 818 S-----KIGYCPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMM 892
Cdd:PRK11629 82 AelrnqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 893 GKPSVIFLDEPSTGMDPRARrllwDAVIKI-----RESGKAIIITSHSMEeceaLCTRLS 947
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNA----DSIFQLlgelnRLQGTAFLVVTHDLQ----LAKRMS 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
46-121 |
5.16e-17 |
|
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: 79.92 E-value: 5.16e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQN--RTILLTTHYMDEADMLGDRIAIMVQGT 121
Cdd:cd03229 101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
746-963 |
6.31e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.29 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 746 KQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT---KDVLKVRSKIGY 822
Cdd:PRK09493 5 KNVSKHFGPTQVL---HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEiMVMYA--RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:PRK09493 82 VFQQFYLFPHLTALE-NVMFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
747-966 |
7.40e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 747 QLTKIYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSK--IGYCP 824
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlgIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVM----YARIWGIS---ERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSV 897
Cdd:PRK09700 87 QELSVIDELTVLENLYIgrhlTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 898 IFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKNK 966
Cdd:PRK09700 167 IIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
742-946 |
8.19e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 8.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 742 PVL-IKQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIdGISItkdvlkvrsKI 820
Cdd:COG0488 314 KVLeLEGLSKSYGDKTLL---DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 821 GYCPQ-FDALLEYLTGWEIMVMYARiwGISERQIRpyvnTYLNSLELEP-HANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:COG0488 381 GYFDQhQEELDPDKTVLDELRDGAP--GGTEQEVR----GYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKIreSGkAIIITSHSMEECEALCTRL 946
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRI 499
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-117 |
1.09e-16 |
|
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: 80.21 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD-VVQTYKQNR-TILLTT 101
Cdd:cd03293 110 ERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEeLLDIWRETGkTVLLVT 189
|
90
....*....|....*.
gi 1958644180 102 HYMDEADMLGDRIAIM 117
Cdd:cd03293 190 HDIDEAVFLADRVVVL 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
761-960 |
1.37e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI---TKDVLKVRSKIGYCPQFDALLEYLTGWE 837
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVFQDPEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMYA-RIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLW 916
Cdd:PRK13638 97 SDIAFSlRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644180 917 DAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSP 960
Cdd:PRK13638 177 AIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
746-961 |
1.38e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.39 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 746 KQLTKIYFKSplILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCP 824
Cdd:PRK13652 7 RDLCYSYSGS--KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIReVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMVMYARI-WGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:PRK13652 85 QNPDDQIFSPTVEQDIAFGPInLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 904 STGMDPRARRLLWDAVIKIRES-GKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
760-963 |
1.76e-16 |
|
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: 84.05 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQ----FDA-LLEYL 833
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdLRRRIAVVPQrphlFDTtLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 tgweimvMYAR-------IWGISER-QIRPYVNTYLNSLE--LEPHANSListySEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:COG4987 430 -------RLARpdatdeeLWAALERvGLGDWLAALPDGLDtwLGEGGRRL----SGGERRRLALARALLRDAPILLLDEP 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 904 STGMDPRARRLLWDAVIKIREsGKAIIITSHSMEECEAlCTRLSIMVHGKLTCLGSPQYL 963
Cdd:COG4987 499 TEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
762-970 |
3.36e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITP---TAGDVFIDGISITKDVLKVRSkiGYCPQFDALLEYLTGWEI 838
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMYA-----RIWGISERQIRpyVNTYLNSLELEPHANSLIST------YSEGNKRRLSTAIAMMGKPSVIFLDEPSTGM 907
Cdd:TIGR00955 120 LMFQAhlrmpRRVTKKEKRER--VDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 908 DPRARRLLWDAVIKIRESGKAIIITSH--SMEECEaLCTRLSIMVHGKLTCLGSPQYLKNKFGDI 970
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDL 261
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
743-979 |
3.82e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITkDVLKVRSKIGY 822
Cdd:PRK09452 15 VELRGISKSFDGKEVI---SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 903 PSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL----KNKF-----GDIYI 972
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLFvarfiGEINI 250
|
....*..
gi 1958644180 973 LKTKVKS 979
Cdd:PRK09452 251 FDATVIE 257
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-117 |
6.28e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.98 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY- 91
Cdd:COG1116 106 ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLw 185
|
90 100
....*....|....*....|....*..
gi 1958644180 92 -KQNRTILLTTHYMDEADMLGDRIAIM 117
Cdd:COG1116 186 qETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
760-960 |
7.29e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-----KDVLKVRSKIGYCPQF-DALLEYL 833
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqKEIKPVRKKVGVVFQFpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHA-NSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRAR 912
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958644180 913 RLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSP 960
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
27-120 |
7.59e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.55 E-value: 7.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 27 NNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMD 105
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYME 205
|
90
....*....|....*
gi 1958644180 106 EADMLGDRIAIMVQG 120
Cdd:NF000106 206 EAEQLAHELTVIDRG 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
759-934 |
1.00e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.63 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGF-------------NGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQ 825
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFtlnagealqvtgpNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 826 FDALLEYLTGWEIMVMYARIWGISERQIrpyvntyLNSLE---LEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTI-------EDALAavgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 1958644180 903 PSTGMDPRARRLLWDAVIKIRESGKAIIITSH 934
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
745-934 |
1.06e-15 |
|
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: 75.18 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitkdvlkvRSKIGYCP 824
Cdd:cd03221 3 LENLSKTYGGKLLL---KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFdalleyltgweimvmyariwgiserqirpyvntylnslelephanslistySEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:cd03221 70 QL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|
gi 1958644180 905 TGMDPRARRLLWDAvikIRESGKAIIITSH 934
Cdd:cd03221 99 NHLDLESIEALEEA---LKEYPGTVILVSH 125
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
760-955 |
1.33e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-KDVLK-VRSKIGYCP---QFDALLEYLT 834
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDaIRAGIAYVPedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 835 GWE-----IMVMYARIWGISERQIRPYVNTYLNSLELE-PHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:COG1129 347 IREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958644180 909 PRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:COG1129 427 VGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
760-959 |
2.12e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 77.08 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKdvLK----VRSKIGYCPQFDALLEYLTG 835
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTG--LDeheiARLGIGRKFQKPTVFEELTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WE-IMVMYAR---IWGI----SERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLstAIAM--MGKPSVIFLDEPST 905
Cdd:COG4674 103 FEnLELALKGdrgVFASlfarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWL--EIGMllAQDPKLLLLDEPVA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 906 GMDPRARRLLWDAVIKIRESgKAIIITSHSMEECEALCTRLSIMVHGKLTCLGS 959
Cdd:COG4674 181 GMTDAETERTAELLKSLAGK-HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
761-961 |
2.37e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.12 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKVRskiGYCPQFDALLEYLTGW 836
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspAELARRR---AVLPQHSSLSFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 837 EIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMM------GKPSVIFLDEPSTGMDPR 910
Cdd:PRK13548 95 EVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 911 --------ARRLlwdavikIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK13548 175 hqhhvlrlARQL-------AHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-114 |
2.42e-15 |
|
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: 75.98 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 12 SQVKGVPQNMclEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY 91
Cdd:COG4133 100 AALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
90 100
....*....|....*....|....
gi 1958644180 92 KQN-RTILLTTHymDEADMLGDRI 114
Cdd:COG4133 178 LARgGAVLLTTH--QPLELAAARV 199
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
14-123 |
2.42e-15 |
|
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: 76.25 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 14 VKGVPQNMCLEETNNMLSAFNLTEKRdafSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK- 92
Cdd:cd03266 108 LKGDELTARLEELADRLGMEELLDRR---VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRa 184
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 93 QNRTILLTTHYMDEADMLGDRIAIMVQGTLR 123
Cdd:cd03266 185 LGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
760-963 |
2.62e-15 |
|
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: 76.50 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQfDALLeyLTGwEI 838
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLRSMIGVVLQ-DTFL--FSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 M--VMYAR------IWGISERQIRpyVNTYLNSLE--LEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:cd03254 94 MenIRLGRpnatdeEVIEAAKEAG--AHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 909 PRARRLLWDAVIKIREsGKAIIITSHsmeecealctRLS-------IMV--HGKLTCLGSPQYL 963
Cdd:cd03254 172 TETEKLIQEALEKLMK-GRTSIIIAH----------RLStiknadkILVldDGKIIEEGTHDEL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
756-954 |
2.70e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 756 PLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI----TKDVLKVRSKIGYcpQFDALLE 831
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAAGVAIIY--QELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 832 YLTGWE-IMV--MYARIWGISERQIRPYVNTYLNSL--ELEPHANslISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTG 906
Cdd:PRK11288 93 EMTVAEnLYLgqLPHKGGIVNRRLLNYEAREQLEHLgvDIDPDTP--LKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958644180 907 MDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:PRK11288 171 LSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
754-1003 |
3.78e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.36 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 754 KSPL-ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFID------GISITKDVLKVRSKIGYCPQF 826
Cdd:PRK13645 19 KTPFeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 827 DALLEYLTGWEIMVMYARI-WGISERQIRPYVNTYLNSLEL-EPHANSLISTYSEGNKRRLSTA--IAMMGKPSVifLDE 902
Cdd:PRK13645 99 PEYQLFQETIEKDIAFGPVnLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAgiIAMDGNTLV--LDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 903 PSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLknkFGDIYILkTKVKSgE 981
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI---FSNQELL-TKIEI-D 251
|
250 260
....*....|....*....|..
gi 1958644180 982 TLKEFKNFITLTFPGSELKQEN 1003
Cdd:PRK13645 252 PPKLYQLMYKLKNKGIDLLNKN 273
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
761-960 |
4.73e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.87 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTG--EITPTAGDVFIDGISITKDVLKVRSKIGycpqfdalleyltgweI 838
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLG----------------I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMY---ARIWGISerqirpyVNTYLNSLELephanslisTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLL 915
Cdd:cd03217 80 FLAFqypPEIPGVK-------NADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958644180 916 WDAVIKIRESGKAIIITSHSMEECEAL-CTRLSIMVHGKLTCLGSP 960
Cdd:cd03217 144 AEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
745-951 |
5.88e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.28 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFK-SPL-ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSK--- 819
Cdd:COG1101 4 LKNLSKTFNPgTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKyig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 820 -------IGYCPQfdalleyLTGWEIMVM-YAR------IWGISERQiRPYVNTYLNSLE--LEPHANSLISTYSEGNKR 883
Cdd:COG1101 84 rvfqdpmMGTAPS-------MTIEENLALaYRRgkrrglRRGLTKKR-RELFRELLATLGlgLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 884 RLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGK--AIIITsHSMEECEALCTRLsIMVH 951
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNltTLMVT-HNMEQALDYGNRL-IMMH 223
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
396-584 |
6.79e-15 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 77.43 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 396 RAKLTVLFNNEAYHSPSLSLAVLDNILFMSLsGANASITVFHKPQPRPTSKEW-----PRSTYGKIVAFKIqLGMALLVS 470
Cdd:pfam12698 98 SATVTVYINSSNLLVSKLILNALQSLLQQLN-ASALVLLLEALSTSAPIPVEStplfnPQSGYAYYLVGLI-LMIIILIG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 471 GFCILT--VTERITKAKHMQFLSGASVLVYWLSALVFDFIIFFISCCFLLVMFkyykIDIYVTDYHILETMLILILFGWS 548
Cdd:pfam12698 176 AAIIAVsiVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL----FGIGIPFGNLGLLLLLFLLYGLA 251
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958644180 549 AIPLTYLMSFLFSKSIPAY-IQLLVFYYLSGTSGLLI 584
Cdd:pfam12698 252 YIALGYLLGSLFKNSEDAQsIIGIVILLLSGFFGGLF 288
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-126 |
7.09e-15 |
|
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: 76.14 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVV---Q 89
Cdd:cd03294 128 EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELlrlQ 207
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958644180 90 TyKQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCG 126
Cdd:cd03294 208 A-ELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-122 |
7.11e-15 |
|
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: 75.17 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ-NRTILLTTH 102
Cdd:cd03219 122 ERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEH 201
|
90 100
....*....|....*....|
gi 1958644180 103 YMDEADMLGDRIAIMVQGTL 122
Cdd:cd03219 202 DMDVVMSLADRVTVLDQGRV 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
759-961 |
7.27e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.21 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKD-VLKVRSKIGYC---P--QF------ 826
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRRQVGMVfqnPdnQFvgatvq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 827 DAL---LEYLtgweimvmyariwGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:PRK13635 101 DDVafgLENI-------------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 904 STGMDPRARRLLWDAVIKIRESGKAIIIT-SHSMEECeALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPE 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
745-954 |
8.90e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 8.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKsplILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT--KDVLKVRSKIGY 822
Cdd:PRK11614 8 FDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALLEYLTGWEIMVM---YARIWGISERQIRPYvntylnslELEP----HANSLISTYSEGNKRRLSTAIAMMGKP 895
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMggfFAERDQFQERIKWVY--------ELFPrlheRRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 896 SVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
759-955 |
8.95e-15 |
|
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: 73.50 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQfdalleyltgwei 838
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 mvmyariwgiserqiRPYV-NTYLnslelephANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWD 917
Cdd:cd03247 83 ---------------RPYLfDTTL--------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958644180 918 AVIKIREsGKAIIITSHSMEECEALcTRLSIMVHGKLT 955
Cdd:cd03247 140 LIFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-186 |
9.69e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.97 E-value: 9.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 20 NMCLEETNNmlSAFNLTEK----RDAFSKS---LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY- 91
Cdd:PRK13646 115 KMNLDEVKN--YAHRLLMDlgfsRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLq 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 92 -KQNRTILLTTHYMDEADMLGDRIAIMVQGTL--RCCGSSVFLKRLYGVGSHIvmvkepvcDVDEISKL-------IHYY 161
Cdd:PRK13646 193 tDENKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKKLADWHI--------GLPEIVQLqydfeqkYQTK 264
|
170 180
....*....|....*....|....*.
gi 1958644180 162 IPTATLktnvgNELSFI-LPKEYTHK 186
Cdd:PRK13646 265 LKDIAL-----TEEEFVsLYKEWQHE 285
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
30-127 |
1.15e-14 |
|
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: 74.46 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 30 LSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMDEA 107
Cdd:cd03261 121 LEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTA 200
|
90 100
....*....|....*....|
gi 1958644180 108 DMLGDRIAIMVQGTLRCCGS 127
Cdd:cd03261 201 FAIADRIAVLYDGKIVAEGT 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
760-970 |
1.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISiTKDVLK---VRSKIGYCPQfDALLEYL--T 834
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKlqgIRKLVGIVFQ-NPETQFVgrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 835 GWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRL 914
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 915 LWDAVIKIRESGKAIIITSHSMEECEAlCTRLSIMVHGKLTCLGSPQylkNKFGDI 970
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE---NVLSDV 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-120 |
1.41e-14 |
|
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: 74.15 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK 92
Cdd:cd03258 108 EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDIN 187
|
90 100 110
....*....|....*....|....*....|
gi 1958644180 93 QNR--TILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:cd03258 188 RELglTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-122 |
1.56e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 17 VPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR- 95
Cdd:PRK13648 114 VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHn 193
|
90 100
....*....|....*....|....*...
gi 1958644180 96 -TILLTTHYMDEAdMLGDRIAIMVQGTL 122
Cdd:PRK13648 194 iTIISITHDLSEA-MEADHVIVMNKGTV 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
761-961 |
3.63e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI-TKDVLKVRSKIGYCPQFDALLEYLTGWEIM 839
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 840 VM-----YARIWGISERQiRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD-PRARR 913
Cdd:PRK09536 99 EMgrtphRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958644180 914 LLwDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK09536 178 TL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-122 |
3.71e-14 |
|
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: 76.48 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 8 LCPSS---QVKGVPQNMCL------EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDP 78
Cdd:COG1123 96 LNPVTvgdQIAEALENLGLsraearARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958644180 79 ASRRSTWDVVQTYKQNR--TILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:COG1123 176 TTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
745-961 |
4.00e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 74.29 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIY-FKSPLI-LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-----KDVLKVR 817
Cdd:PRK13634 5 FQKVEHRYqYKTPFErRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 818 SKIGYCPQF--DALLEYLTGWEIMvmYARI-WGISERQIRPYVNTYLNSLELEPhanSLIS----TYSEGNKRRLSTA-- 888
Cdd:PRK13634 85 KKVGIVFQFpeHQLFEETVEKDIC--FGPMnFGVSEEDAKQKAREMIELVGLPE---ELLArspfELSGGQMRRVAIAgv 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 889 IAMmgKPSVIFLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK13634 160 LAM--EPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
758-960 |
4.44e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI-----------------TKDVLKVRSKI 820
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitnpyskkIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 821 GYCPQFDALLEYLTGWEIMVMYARI-WGISERQIRPYVNTYLNSLEL-EPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:PRK13631 119 SMVFQFPEYQLFKDTIEKDIMFGPVaLGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSP 960
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
739-988 |
5.24e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 73.31 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 739 LNCPVLIKQLTKIY---------FKSPLI--------LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGD 801
Cdd:PRK13546 1 MNVSVNIKNVTKEYriyrtnkerMKDALIpkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 802 VFIDGisitkDVLKVRSKIGYCPQfdalleyLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGN 881
Cdd:PRK13546 81 VDRNG-----EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 882 KRRLSTAIAMMGKPSVIFLDEP-STGMDPRARRLLwDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGS- 959
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCL-DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEl 227
|
250 260 270
....*....|....*....|....*....|...
gi 1958644180 960 ----PQYLKnkfgdiYILKTKVKSGETLKEFKN 988
Cdd:PRK13546 228 ddvlPKYEA------FLNDFKKKSKAEQKEFRN 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
743-971 |
5.25e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSPLILAVkniSLAIQERECFGLLGFNGAGKTTTFQ----ILTGEITPTA-----GDVFIDGISITKDV 813
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAV---DLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 814 LKVRSKIGYCPQFDALLEYLTGWEIMVMYA----RIWGISERQIRPYVNTY----LNSLELEPHANSLISTYSEGNKRRL 885
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGAlgstPFWRTCFSWFTREQKQRalqaLTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 886 STAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRES-GKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLK 964
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFD 241
|
....*...
gi 1958644180 965 N-KFGDIY 971
Cdd:PRK09984 242 NeRFDHLY 249
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
38-122 |
5.79e-14 |
|
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: 72.21 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 38 KRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLGDRIAIM 117
Cdd:cd03260 134 KDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFL 213
|
....*
gi 1958644180 118 VQGTL 122
Cdd:cd03260 214 LNGRL 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
46-108 |
7.18e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 7.18e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR---TILLTTHYMDEAD 108
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAE 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-160 |
7.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.20 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRstwDVVQTYKQ-- 93
Cdd:PRK13633 115 GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR---EVVNTIKEln 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 94 ---NRTILLTTHYMDEAdMLGDRIAIMVQGTLRCCGS--SVFlkrlygvgSHIVMVKEPVCDVDEISKLIHY 160
Cdd:PRK13633 192 kkyGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTpkEIF--------KEVEMMKKIGLDVPQVTELAYE 254
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-120 |
8.02e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD--VVQTYKQNRTILLTTHYMDE 106
Cdd:NF033858 381 MLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRllIELSREDGVTIFISTHFMNE 460
|
90
....*....|....
gi 1958644180 107 AdMLGDRIAIMVQG 120
Cdd:NF033858 461 A-ERCDRISLMHAG 473
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
30-127 |
1.10e-13 |
|
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: 71.93 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 30 LSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEA 107
Cdd:COG1127 126 LELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSA 205
|
90 100
....*....|....*....|
gi 1958644180 108 DMLGDRIAIMVQGTLRCCGS 127
Cdd:COG1127 206 FAIADRVAVLADGKIIAEGT 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
46-122 |
1.32e-13 |
|
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: 69.76 E-value: 1.32e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVV-QTYKQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-126 |
1.63e-13 |
|
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: 69.77 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 17 VPQnmcleetnnMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--N 94
Cdd:cd03214 78 VPQ---------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARerG 148
|
90 100 110
....*....|....*....|....*....|..
gi 1958644180 95 RTILLTTHYMDEADMLGDRIAIMVQGTLRCCG 126
Cdd:cd03214 149 KTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
745-961 |
2.13e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLilaVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSK-IGYC 823
Cdd:PRK11231 5 TENLTVGYGTKRI---LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARrLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 824 PQFDALLEYLTGWEiMVMYAR-----IWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:PRK11231 82 PQHHLTPEGITVRE-LVAYGRspwlsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
760-963 |
2.23e-13 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 74.02 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQ----FDALLEylt 834
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQIAWVPQnpylFAGTIR--- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 835 gwEIMVMYARiwGISERQIRP-----YVNTYLNSLE------LEPHANSListySEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:COG4988 429 --ENLRLGRP--DASDEELEAaleaaGLDEFVAALPdgldtpLGEGGRGL----SGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 904 STGMDPRARRLLWDAVIKIREsGKAIIITSHSMEECeALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
30-142 |
2.40e-13 |
|
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: 71.23 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 30 LSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY--KQNRTILLTTHYMDEA 107
Cdd:COG1120 122 LERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLA 201
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958644180 108 DMLGDRIAIMVQGTLRCCGS--SVF----LKRLYGVGSHIV 142
Cdd:COG1120 202 ARYADRLVLLKDGRIVAQGPpeEVLtpelLEEVYGVEARVI 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
760-935 |
2.68e-13 |
|
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: 73.93 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQ----FDA-LLEYL 833
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQdahlFDTtVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 -------TGWEIMVMYARIwGISErqirpyvntYLNSLE------LEPHANSListySEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:TIGR02868 430 rlarpdaTDEELWAALERV-GLAD---------WLRALPdgldtvLGEGGARL----SGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958644180 901 DEPSTGMDPRAR----RLLWDAvikirESGKAIIITSHS 935
Cdd:TIGR02868 496 DEPTEHLDAETAdellEDLLAA-----LSGRTVVLITHH 529
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
760-959 |
4.21e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKvrSKIGYCPQ-------FDALLEy 832
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAYVPQseevdwsFPVLVE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 833 ltgwEIMVM-------YARIWGISERQIrpyVNTYLNSLELEPHANSLISTYSEGNKRR--LSTAIAMMGkpSVIFLDEP 903
Cdd:PRK15056 99 ----DVVMMgryghmgWLRRAKKRDRQI---VTAALARVDMVEFRHRQIGELSGGQKKRvfLARAIAQQG--QVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 904 STGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTrLSIMVHGklTCLGS 959
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG--TVLAS 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
760-960 |
4.53e-13 |
|
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: 69.36 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQ----FDALLEylT 834
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQdptlFSGTIR--S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 835 GWEIMVMYariwgiSERQIRpyvntylNSLELEPHANSListySEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRArrl 914
Cdd:cd03369 101 NLDPFDEY------SDEEIY-------GALRVSEGGLNL----SQGQRQLLCLARALLKRPRVLVLDEATASIDYAT--- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 915 lwDAVIK--IRE--SGKAIIITSHSMEECeALCTRLSIMVHGKLTCLGSP 960
Cdd:cd03369 161 --DALIQktIREefTNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
759-955 |
4.91e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-KDVLKVR-SKIGYCP---QFDALLEYL 833
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITgLSPRERRrLGVAYIPedrLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWEIMVM-------YARIWGISERQIRPY---------VNTylnslelePHANSLISTYSEGNKRRLSTAIAMMGKPSV 897
Cdd:COG3845 352 SVAENLILgryrrppFSRGGFLDRKAIRAFaeelieefdVRT--------PGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 898 IFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
34-123 |
5.29e-13 |
|
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: 69.17 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 34 NLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGD 112
Cdd:cd03268 115 GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVAD 194
|
90
....*....|.
gi 1958644180 113 RIAIMVQGTLR 123
Cdd:cd03268 195 RIGIINKGKLI 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
30-126 |
6.47e-13 |
|
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: 69.22 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 30 LSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPasrRSTWDVVQTYKQ----NRTILLTTHyMD 105
Cdd:cd03234 128 LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS---FTALNLVSTLSQlarrNRIVILTIH-QP 203
|
90 100
....*....|....*....|...
gi 1958644180 106 EADM--LGDRIAIMVQGTLRCCG 126
Cdd:cd03234 204 RSDLfrLFDRILLLSSGEIVYSG 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-117 |
6.84e-13 |
|
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: 68.82 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQT-YKQNRTILLTTH 102
Cdd:cd03226 105 EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
90
....*....|....*
gi 1958644180 103 YMDEADMLGDRIAIM 117
Cdd:cd03226 185 DYEFLAKVCDRVLLL 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
776-934 |
6.88e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.22 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 776 LLGFNGAGKTTTFQILTGEITP---TAGDVFIDGISItkDVLKVRSkIGYCPQFDALLEYLTGWEIMVMYARIW---GIS 849
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL--DSSFQRS-IGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVS 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 850 ERQIRPYVNTYLNSLELEPHANSLISTYSEG----NKRRLSTAIAMMGKP-SVIFLDEPSTGMDPRARRLLWDAVIKIRE 924
Cdd:TIGR00956 871 KSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLAD 950
|
170
....*....|
gi 1958644180 925 SGKAIIITSH 934
Cdd:TIGR00956 951 HGQAILCTIH 960
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-122 |
7.81e-13 |
|
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: 68.67 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQ--T 90
Cdd:cd03255 108 LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelN 187
|
90 100 110
....*....|....*....|....*....|..
gi 1958644180 91 YKQNRTILLTTHYMDEADMlGDRIAIMVQGTL 122
Cdd:cd03255 188 KEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
745-961 |
8.94e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.88 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKiYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitKDVLKVRSK---IG 821
Cdd:PRK10851 5 IANIKK-SFGRTQVL--NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLHARdrkVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQFDALLEYLTGWEIMVMYARIWGISER----QIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSV 897
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTVLPRRERpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 898 IFLDEPSTGMDPRARRLL--WdavikIRESGKAIIITS----HSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELrrW-----LRQLHEELKFTSvfvtHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
762-955 |
9.54e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIG--YCP---QFDAL-LEYLTG 835
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLyLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WEIM-VMYAR--IWgISERQIRPYVNTYLNSLELE-PHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRA 911
Cdd:PRK15439 360 WNVCaLTHNRrgFW-IKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644180 912 RRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
39-122 |
9.66e-13 |
|
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: 69.25 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 39 RDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMDEADMLGDRIAI 116
Cdd:cd03295 129 ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAI 208
|
....*.
gi 1958644180 117 MVQGTL 122
Cdd:cd03295 209 MKNGEI 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
30-122 |
9.87e-13 |
|
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: 68.69 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 30 LSAFNLTEKR-DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMDE 106
Cdd:cd03257 129 LVGVGLPEEVlNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGV 208
|
90
....*....|....*.
gi 1958644180 107 ADMLGDRIAIMVQGTL 122
Cdd:cd03257 209 VAKIADRVAVMYAGKI 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-133 |
9.88e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEkrDAFSKS---LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY- 91
Cdd:PRK13634 115 GVSEEDAKQKAREMIELVGLPE--ELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLh 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958644180 92 -KQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCGS--SVFLKR 133
Cdd:PRK13634 193 kEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADP 237
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
764-954 |
9.98e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 764 ISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK----DVLKVRSK-IGYCPQFDALLEYLTGWEI 838
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRAKhVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDA 918
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958644180 919 VIKI-RESGKAIIITSHSmEECEALCTRLSIMVHGKL 954
Cdd:PRK10584 189 LFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
759-960 |
1.00e-12 |
|
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: 68.67 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQ----F------- 826
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQdpvlFsgtirsn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 827 -DALLEYlTGWEimvmyarIWGISER-QIRPYVNTYLNSLELEPHANSliSTYSEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:cd03244 98 lDPFGEY-SDEE-------LWQALERvGLKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 905 TGMDPRArrllwDAVIK--IRE--SGKAIIITSHsmeecealctRLS-------IMV--HGKLTCLGSP 960
Cdd:cd03244 168 ASVDPET-----DALIQktIREafKDCTVLTIAH----------RLDtiidsdrILVldKGRVVEFDSP 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
747-949 |
1.17e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.96 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 747 QLTKIYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDvlkvRSKIGYCPQF 826
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP----GAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 827 DALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTG 906
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644180 907 MDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIM 949
Cdd:PRK11248 159 LDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
761-973 |
1.88e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDG--ISITKDV-----LKVRSKIGYCPQFDALLEYL 833
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvLYFGKDIfqidaIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWEIMVMYARIWGISE-RQIRPYVNTYLNSL----ELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEkREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 909 PRARRLLWDAVIKIRESgKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL----KNKFGDIYIL 973
Cdd:PRK14246 186 IVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
760-961 |
1.90e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 71.35 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI---TKDVLkvRSKIGYCPQfDALLEYLTgw 836
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdlTLESL--RRQIGVVPQ-DTFLFSGT-- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 837 eIM--VMYARIwGISERQIRP-----YVNTYLNSLE------LEPHANSListySEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:COG1132 430 -IRenIRYGRP-DATDEEVEEaakaaQAHEFIEALPdgydtvVGERGVNL----SGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 904 STGMDPRARRLLWDAVIKIREsGKAIIITSHsmeecealctRLS-------IMV--HGKLTCLGSPQ 961
Cdd:COG1132 504 TSALDTETEALIQEALERLMK-GRTTIVIAH----------RLStirnadrILVldDGRIVEQGTHE 559
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
25-123 |
2.25e-12 |
|
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: 67.81 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 25 ETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHY 103
Cdd:TIGR03740 104 RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELRELIRSFpEQGITVILSSHI 183
|
90 100
....*....|....*....|
gi 1958644180 104 MDEADMLGDRIAIMVQGTLR 123
Cdd:TIGR03740 184 LSEVQQLADHIGIISEGVLG 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
745-937 |
2.72e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.96 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIY-FKSPLIL-AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDV---FID----------GISI 809
Cdd:PRK13651 5 VKNIVKIFnKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDeknkkktkekEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 810 TKDVLK------------VRSKIGYCPQFD--ALLEYLTGWEIMvMYARIWGISERQIRPYVNTYL-------NSLELEP 868
Cdd:PRK13651 85 EKLVIQktrfkkikkikeIRRRVGVVFQFAeyQLFEQTIEKDII-FGPVSMGVSKEEAKKRAAKYIelvgldeSYLQRSP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 869 HAnslistYSEGNKRRLSTA--IAMmgKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSME 937
Cdd:PRK13651 164 FE------LSGGQKRRVALAgiLAM--EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
46-120 |
3.12e-12 |
|
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: 65.87 E-value: 3.12e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMlGDRIAIMVQG 120
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
760-945 |
3.46e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.30 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisiTKDVLKVRSkigycpqfdALLEYLTGWEIM 839
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---SAALIAISS---------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 840 VMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAV 919
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180
....*....|....*....|....*.
gi 1958644180 920 IKIRESGKAIIITSHSMEECEALCTR 945
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTK 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-122 |
3.76e-12 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 67.52 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEK-RDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLT 100
Cdd:COG1124 116 ERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFV 195
|
90 100
....*....|....*....|..
gi 1958644180 101 THYMDEADMLGDRIAIMVQGTL 122
Cdd:COG1124 196 SHDLAVVAHLCDRVAVMQNGRI 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-130 |
4.73e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.77 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 18 PQNMCLEE---TNNMLSAFNLT--EKRDAFSKS---LSGGMKRKLAI--IIALigGSKVVILDEPTSGMDPASRRSTWDV 87
Cdd:PRK13637 109 PINLGLSEeeiENRVKRAMNIVglDYEDYKDKSpfeLSGGQKRRVAIagVVAM--EPKILILDEPTAGLDPKGRDEILNK 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958644180 88 VQTY--KQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCG--SSVF 130
Cdd:PRK13637 187 IKELhkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGtpREVF 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
45-136 |
5.00e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 67.04 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIaIMVQGTLR 123
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRV-LLLNRGLV 217
|
90
....*....|....*....
gi 1958644180 124 CCGS--SVF----LKRLYG 136
Cdd:COG1121 218 AHGPpeEVLtpenLSRAYG 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-158 |
5.59e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.52 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 15 KGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ- 93
Cdd:PRK13640 113 RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKk 192
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 94 -NRTILLTTHYMDEADMlGDRIAIMVQGTLRCCGSSVflkrlyGVGSHIVMVKEPVCDVDEISKLI 158
Cdd:PRK13640 193 nNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPV------EIFSKVEMLKEIGLDIPFVYKLK 251
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-122 |
5.72e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 66.01 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDV-VQTY 91
Cdd:cd03262 103 KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVmKDLA 182
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 92 KQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:cd03262 183 EEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
761-963 |
5.78e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDG--ISITKDV---LKV---------RSKIGYCPQF 826
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtINLVRDKdgqLKVadknqlrllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 827 DALLEYLTGWE-IMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTY-SEGNKRRLSTAIAMMGKPSVIFLDEPS 904
Cdd:PRK10619 101 FNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHlSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 905 TGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
768-921 |
6.69e-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: 66.66 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 768 IQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDgisitkdvlkvRSKIGYCPQfdalleYLTGWEIMVMYARIWG 847
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-----------LDTVSYKPQ------YIKADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 848 ISERQ-IRPYVNT-YLNSLELEPHANSLISTYSEGNKRRlsTAIAM-MGKPSVIFL-DEPSTGMDPRaRRLLWDAVIK 921
Cdd:cd03237 85 ITKDFyTHPYFKTeIAKPLQIEQILDREVPELSGGELQR--VAIAAcLSKDADIYLlDEPSAYLDVE-QRLMASKVIR 159
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-120 |
7.00e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.70 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 14 VKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPasrRSTWDVVQTYKQ 93
Cdd:PRK11264 113 VKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQ 189
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 94 ----NRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK11264 190 laqeKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
761-955 |
7.37e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK----DVLK--------VRSKIGYCPQFD- 827
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrsplDAVKkgmayiteSRRDNGFFPNFSi 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 828 ----ALLEYLTgweiMVMYARIWGI-SERQIRPYVNTYLNSLELEPHA-NSLISTYSEGNKRRLSTAIAMMGKPSVIFLD 901
Cdd:PRK09700 359 aqnmAISRSLK----DGGYKGAMGLfHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 902 EPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
760-961 |
7.47e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.58 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI-------TKDVLKVRSKIGYCPQFDALLEY 832
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 833 LTgweimVMY------ARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTG 906
Cdd:PRK11124 97 LT-----VQQnlieapCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 907 MDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRL------SIMVHGKLTCLGSPQ 961
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVvymengHIVEQGDASCFTQPQ 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
46-127 |
7.49e-12 |
|
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: 69.41 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADmLGDRIAIMVQGTLRCC 125
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQ 550
|
..
gi 1958644180 126 GS 127
Cdd:COG4987 551 GT 552
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-122 |
9.38e-12 |
|
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: 66.20 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 23 LEETNNMLsafNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLT 100
Cdd:cd03267 134 LDELSELL---DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLT 210
|
90 100
....*....|....*....|..
gi 1958644180 101 THYMDEADMLGDRIAIMVQGTL 122
Cdd:cd03267 211 SHYMKDIEALARRVLVIDKGRL 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
760-967 |
9.93e-12 |
|
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: 68.68 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTG--EITPTAGDVfIDGISITKDVLKVR--SKIGY-CPQFDALLEYLT 834
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRI-IYHVALCEKCGYVErpSKVGEpCPVCGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 835 G--WE------------IMVMYARIWGISERQiRPYVNTyLNSLE---------------------LEPHANSLISTYSE 879
Cdd:TIGR03269 94 VdfWNlsdklrrrirkrIAIMLQRTFALYGDD-TVLDNV-LEALEeigyegkeavgravdliemvqLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 880 GNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIK-IRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLG 958
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEG 251
|
....*....
gi 1958644180 959 SPQYLKNKF 967
Cdd:TIGR03269 252 TPDEVVAVF 260
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
29-122 |
1.14e-11 |
|
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: 68.39 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAFNLTEK-RDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMD 105
Cdd:COG1123 387 LLERVGLPPDlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLA 466
|
90
....*....|....*..
gi 1958644180 106 EADMLGDRIAIMVQGTL 122
Cdd:COG1123 467 VVRYIADRVAVMYDGRI 483
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
762-935 |
1.36e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDvlKVRSKIGYCPQFDALLEYLTGWEIMVM 841
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP--DVAEACHYLGHRNAMKPALTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 842 YARIWGISERQIRPyvntYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIK 921
Cdd:PRK13539 97 WAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
170
....*....|....
gi 1958644180 922 IRESGKAIIITSHS 935
Cdd:PRK13539 173 HLAQGGIVIAATHI 186
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
46-158 |
1.39e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.80 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDEADMLGDRIAIMVQGTLRC 124
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958644180 125 CGS--SVFL-KRLYgvgSHIVMVKEPVCDVdeISKLI 158
Cdd:PRK13631 257 TGTpyEIFTdQHII---NSTSIQVPRVIQV--INDLI 288
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
35-122 |
1.47e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.13 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 35 LTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRStwdVVQTYKQ-NR----TILLTTHYMDEADM 109
Cdd:PRK11153 130 LSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS---ILELLKDiNRelglTIVLITHEMDVVKR 206
|
90
....*....|...
gi 1958644180 110 LGDRIAIMVQGTL 122
Cdd:PRK11153 207 ICDRVAVIDAGRL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
29-126 |
1.51e-11 |
|
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: 64.85 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDE 106
Cdd:cd03259 114 LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEE 193
|
90 100
....*....|....*....|
gi 1958644180 107 ADMLGDRIAIMVQGTLRCCG 126
Cdd:cd03259 194 ALALADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
743-966 |
1.63e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.36 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 743 VLIKQLTKIYFKSPlILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGD---VFIDGISIT-KDVLKVRS 818
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTaKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 819 KIGYCpqFDALLEYLTGWEIMVMYAriWGISERQI-RP----YVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMG 893
Cdd:PRK13640 85 KVGIV--FQNPDNQFVGATVGDDVA--FGLENRAVpRPemikIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 894 KPSVIFLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEaLCTRLSIMVHGKLTCLGSPQYLKNK 966
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
46-127 |
2.33e-11 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 67.48 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHymDEADM-LGDRIAIMVQGTLRC 124
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVE 551
|
...
gi 1958644180 125 CGS 127
Cdd:COG4988 552 QGT 554
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
760-937 |
2.42e-11 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 67.70 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQFDALLEYLTGWEI 838
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAGTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MV--MYARIWGISERQIRPYVNTYLNSL------ELEPHANSListySEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPR 910
Cdd:TIGR02857 417 RLarPDASDAEIREALERAGLDEFVAALpqgldtPIGEGGAGL----SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180
....*....|....*....|....*..
gi 1958644180 911 ARRLLWDAVIKIREsGKAIIITSHSME 937
Cdd:TIGR02857 493 TEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
776-934 |
2.69e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 68.33 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 776 LLGFNGAGKTTTFQILTGEITP--TAGDVFIDGISITKDVLKVRSkiGYCPQFDALLEYLTGWEIMVMYARIW---GISE 850
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQETFARIS--GYCEQNDIHSPQVTVRESLIYSAFLRlpkEVSK 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 851 RQIRPYVNTYLNSLELEPHANSL-----ISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRES 925
Cdd:PLN03140 989 EEKMMFVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT 1068
|
....*....
gi 1958644180 926 GKAIIITSH 934
Cdd:PLN03140 1069 GRTVVCTIH 1077
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
34-120 |
3.29e-11 |
|
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: 64.41 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 34 NLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD-VVQTYKQNR-TILLTTHYMDEADMLG 111
Cdd:TIGR01184 103 GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEeLMQIWEEHRvTVLMVTHDVDEALLLS 182
|
....*....
gi 1958644180 112 DRIAIMVQG 120
Cdd:TIGR01184 183 DRVVMLTNG 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
760-955 |
3.32e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK----DVLKVRSKIGYCPQFDALLEYLTG 835
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPFLRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRarrlL 915
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA----L 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958644180 916 WDAVIKIRES----GKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:PRK10908 173 SEGILRLFEEfnrvGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-123 |
3.44e-11 |
|
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: 63.85 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 27 NNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTI--LLTTHYM 104
Cdd:cd03297 113 DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIpvIFVTHDL 192
|
90
....*....|....*....
gi 1958644180 105 DEADMLGDRIAIMVQGTLR 123
Cdd:cd03297 193 SEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-120 |
5.69e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 64.65 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAI--IIALigGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ 93
Cdd:PRK13635 111 GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIagVLAL--QPDIIILDEATSMLDPRGRREVLETVRQLKE 188
|
90 100
....*....|....*....|....*....
gi 1958644180 94 NR--TILLTTHYMDEAdMLGDRIAIMVQG 120
Cdd:PRK13635 189 QKgiTVLSITHDLDEA-AQADRVIVMNKG 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
761-958 |
5.77e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.09 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTT---TFQILT--GEITPTAGDVFIDGISITK---DVLKVRSKIGYCPQFDALLEY 832
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 833 LTGWEIMVMYARIWGI--SERQIRPYVNTYLNSL----ELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTG 906
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 907 MDPRARRLLWDAVIKIRESgKAIIITSHSMEECEALCTRLSIMVHGKLTCLG 958
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
745-934 |
9.83e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIY------FKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-------- 810
Cdd:PRK15112 7 VRNLSKTFryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysyrs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 811 ----------KDVLKVRSKIGYCpqFDALLEYLTGWEimvmyariwgISERQIRpyVNTYLNSLELEP-HANSLISTYSE 879
Cdd:PRK15112 87 qrirmifqdpSTSLNPRQRISQI--LDFPLRLNTDLE----------PEQREKQ--IIETLRQVGLLPdHASYYPHMLAP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 880 GNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRES-GKAII-ITSH 934
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIyVTQH 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-128 |
1.78e-10 |
|
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: 62.18 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ-NRTILLTTH 102
Cdd:cd03218 112 EKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDH 191
|
90 100
....*....|....*....|....*.
gi 1958644180 103 YMDEADMLGDRIAIMVQGTLRCCGSS 128
Cdd:cd03218 192 NVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
29-120 |
2.04e-10 |
|
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: 61.68 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAF-NLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDE 106
Cdd:cd03224 115 VYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRdEGVTILLVEQNARF 194
|
90
....*....|....
gi 1958644180 107 ADMLGDRIAIMVQG 120
Cdd:cd03224 195 ALEIADRAYVLERG 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
759-934 |
2.51e-10 |
|
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: 60.97 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGF-------------NGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQ 825
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFtlaagealqvtgpNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 826 FDALLEYLTGWEIMVMYARIWGISErqirpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPST 905
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 1958644180 906 GMDPRARRLLWDAVIKIRESGKAIIITSH 934
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
760-934 |
3.36e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKvrskiGYCPQFDA------LLEYL 833
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-----DYRKLFSAvftdfhLFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWEimvmyariWGISERQIrpyVNTYLNSLELE---PHANSLIST--YSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:PRK10522 413 LGPE--------GKPANPAL---VEKWLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180
....*....|....*....|....*..
gi 1958644180 909 PRARRLLWDAVI-KIRESGKAIIITSH 934
Cdd:PRK10522 482 PHFRREFYQVLLpLLQEMGKTIFAISH 508
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
724-934 |
3.64e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 724 VENERREILYQPEKFLNcPVLIKQLTKIYFKSPLILAVKNISLAIQERecFGLLGFNGAGKTTTFQILTGEITPTAGDvf 803
Cdd:PRK10636 294 VDNPFHFSFRAPESLPN-PLLKMEKVSAGYGDRIILDSIKLNLVPGSR--IGLLGRNGAGKSTLIKLLAGELAPVSGE-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 804 idgISITKDVlkvrsKIGYCPQFDalLEYLTGWEIMVMY-ARIW-GISERQIRpyvnTYLNSLELEPHANSLIST-YSEG 880
Cdd:PRK10636 369 ---IGLAKGI-----KLGYFAQHQ--LEFLRADESPLQHlARLApQELEQKLR----DYLGGFGFQGDKVTEETRrFSGG 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 881 NKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIResgKAIIITSH 934
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE---GALVVVSH 485
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
763-965 |
3.65e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.09 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 763 NISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK----DVLKVRSKIGYCPQFDALLEYLTGWEI 838
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMYARIWG-ISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLwd 917
Cdd:PRK11831 105 VAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL-- 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 918 aVIKIRESGKAI----IITSHSMEECEALCTRLSIMVHGKLTCLGSPQYLKN 965
Cdd:PRK11831 183 -VKLISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
772-934 |
3.86e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 772 ECFGLLGFNGAGKTTTFQILTGEITPT--AGDVFIDGISITKDVLKvrsKIGYCPQFDALLEYLTGWEIMVMYA--RIWG 847
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILK---RTGFVTQDDILYPHLTVRETLVFCSllRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 848 ISERQIRPYV-NTYLNSLELEPH-----ANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIK 921
Cdd:PLN03211 172 SLTKQEKILVaESVISELGLTKCentiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170
....*....|...
gi 1958644180 922 IRESGKAIIITSH 934
Cdd:PLN03211 252 LAQKGKTIVTSMH 264
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
761-961 |
4.73e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitkdvlkvRSKIGYCPQ---FDALLEyLTGWE 837
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------KLRIGYVPQklyLDTTLP-LTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMYAriwGISERQIRPyvntYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWD 917
Cdd:PRK09544 89 FLRLRP---GTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 918 AVIKIR-ESGKAIIITSHSM-----EECEALCtrlsimVHGKLTCLGSPQ 961
Cdd:PRK09544 162 LIDQLRrELDCAVLMVSHDLhlvmaKTDEVLC------LNHHICCSGTPE 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
44-122 |
4.95e-10 |
|
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: 60.26 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRstwDVVQTYK----QNRTILLTTHyMDEADMLG--DRIAIM 117
Cdd:cd03213 110 RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL---QVMSLLRrladTGRTIICSIH-QPSSEIFElfDKLLLL 185
|
....*
gi 1958644180 118 VQGTL 122
Cdd:cd03213 186 SQGRV 190
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
762-934 |
5.41e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK---DVLKV--RSKIGYCPQFDALLEYLTGW 836
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldaDALAQlrREHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 837 ---EIMVMYAriwGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARR 913
Cdd:PRK10535 105 qnvEVPAVYA---GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180
....*....|....*....|.
gi 1958644180 914 LLWDAVIKIRESGKAIIITSH 934
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
755-946 |
5.47e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.63 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 755 SPLILAVKNISLAIQERECFGLLGF-------------NGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKI 820
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFhvdageallvqgdNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 821 GYCPQFDALLEYLTGWEIMVmyariwGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFLC------GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRL 946
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
35-117 |
5.59e-10 |
|
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: 60.24 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 35 LTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ-NRTILLTTHYMDEADMLGDR 113
Cdd:cd03235 122 LSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDR 201
|
....
gi 1958644180 114 IAIM 117
Cdd:cd03235 202 VLLL 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
752-934 |
5.78e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 752 YFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYCPQFDALLE 831
Cdd:PRK13540 11 YHDQPLL---QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 832 YLTGWEiMVMYARIWGISERQIRPYVNTYlnslELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRA 911
Cdd:PRK13540 88 YLTLRE-NCLYDIHFSPGAVGITELCRLF----SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|...
gi 1958644180 912 RRLLWDAVIKIRESGKAIIITSH 934
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
45-122 |
6.12e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.94 E-value: 6.12e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-122 |
6.22e-10 |
|
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: 59.37 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 32 AFNLtekrdAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDEADML 110
Cdd:cd03215 96 AENI-----ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGL 170
|
90
....*....|..
gi 1958644180 111 GDRIAIMVQGTL 122
Cdd:cd03215 171 CDRILVMYEGRI 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
745-963 |
7.89e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.26 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT-KDVLKVRSKIGYC 823
Cdd:PRK13642 7 VENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 824 PQF-DALLEYLTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:PRK13642 87 FQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 903 PSTGMDPRARRLLWDAVIKIRESGKAIIIT-SHSMEECeALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
44-122 |
8.43e-10 |
|
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: 62.93 E-value: 8.43e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLgDRIAIMVQGTL 122
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
734-908 |
8.60e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 734 QPEKFLNCPVLIKQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVfidgisitkdv 813
Cdd:PRK15064 311 QDKKLHRNALEVENLTKGFDNGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 814 lK--VRSKIGYCPQ-----FD---ALLEYLTGWeimvmyaRIWGISERQIRPYVNTYLNSlelEPHANSLISTYSEGNKR 883
Cdd:PRK15064 377 -KwsENANIGYYAQdhaydFEndlTLFDWMSQW-------RQEGDDEQAVRGTLGRLLFS---QDDIKKSVKVLSGGEKG 445
|
170 180
....*....|....*....|....*
gi 1958644180 884 RLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
761-955 |
9.92e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISIT----KDVLKvrSKIGYCPQ---FDALLEYL 833
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspQDGLA--NGIVYISEdrkRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWEIMVMYA-----RIWG-ISERQIRPYVNTYLNSLELE-PHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTG 906
Cdd:PRK10762 346 SVKENMSLTAlryfsRAGGsLKHADEQQAVSDFIRLFNIKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958644180 907 MDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:PRK10762 426 VDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-122 |
1.13e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 59.67 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY--KQ 93
Cdd:COG1136 115 GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrEL 194
|
90 100
....*....|....*....|....*....
gi 1958644180 94 NRTILLTTHYMDEADMlGDRIAIMVQGTL 122
Cdd:COG1136 195 GTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
775-934 |
1.13e-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: 60.07 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 775 GLLGFNGAGKTTTFQILTGEITPTAGdvfidgisitkdvlkvrsKIGYCPQFDALLEYLTGWEIMVMYARIwgiSERQIR 854
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLG------------------KFDDPPDWDEILDEFRGSELQNYFTKL---LEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 855 P-----YV------------------------NTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPST 905
Cdd:cd03236 89 VivkpqYVdlipkavkgkvgellkkkdergklDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|..
gi 1958644180 906 GMDPRARrllWDAVIKIRE---SGKAIIITSH 934
Cdd:cd03236 169 YLDIKQR---LNAARLIRElaeDDNYVLVVEH 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
40-130 |
1.15e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 60.53 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 40 DAFSKS---LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQN-RTILLTTHYMDEADMLGDRIA 115
Cdd:PRK13649 137 SLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVY 216
|
90
....*....|....*..
gi 1958644180 116 IMVQGTLRCCG--SSVF 130
Cdd:PRK13649 217 VLEKGKLVLSGkpKDIF 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-127 |
1.19e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRT-ILLTTH 102
Cdd:PRK10895 116 DRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDH 195
|
90 100
....*....|....*....|....*
gi 1958644180 103 YMDEADMLGDRIAIMVQGTLRCCGS 127
Cdd:PRK10895 196 NVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
759-961 |
1.37e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.15 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCpqFDALLEYLTGwe 837
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIV--FQNPDNQFVG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 IMVMYARIWGIsERQIRPY------VNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRA 911
Cdd:PRK13648 99 SIVKYDVAFGL-ENHAVPYdemhrrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 912 RRLLWDAVIKIRESGKAIIIT-SHSMEECeALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISiTHDLSEA-MEADHVIVMNKGTVYKEGTPT 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
765-958 |
1.43e-09 |
|
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: 59.04 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 765 SLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSkIGYCPQFDALLEYLTgWEIMVMYAR 844
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQENNLFAHLT-VEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 845 IWGISER-QIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKI- 922
Cdd:cd03298 96 SPGLKLTaEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLh 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958644180 923 RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLG 958
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
13-127 |
1.53e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD--VVQT 90
Cdd:PRK10070 132 ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDelVKLQ 211
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958644180 91 YKQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCGS 127
Cdd:PRK10070 212 AKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
46-130 |
1.65e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQN-RTILLTTHYMDEADMLGDRIAIMVQGTLRC 124
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
....*...
gi 1958644180 125 CG--SSVF 130
Cdd:PRK13643 225 CGtpSDVF 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
29-106 |
2.07e-09 |
|
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: 59.33 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY--KQNRTILLTTHYMDE 106
Cdd:COG1119 126 LLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEE 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
750-934 |
2.19e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.16 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 750 KIYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTG--EITPTA---GDVFIDGISITK-DVLKVRSKIGYC 823
Cdd:PRK14247 10 KVSFGQVEVL--DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKmDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 824 PQFDALLEYLTGWEIMVMYARIWGI--SERQIRPYVNTYLNSLEL----EPHANSLISTYSEGNKRRLSTAIAMMGKPSV 897
Cdd:PRK14247 88 FQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958644180 898 IFLDEPSTGMDPRARRLLWDAVIKIRESgKAIIITSH 934
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
764-955 |
2.34e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 764 ISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDG--ISITKDVLKVRSKIGYCPQ---FDALLEYLTGWEI 838
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMYAR----IWG--ISERQIRPYVNTYLNSLELE-PHANSLISTYSEGNK------RRLSTAIammgkpSVIFLDEPST 905
Cdd:PRK11288 352 INISARrhhlRAGclINNRWEAENADRFIRSLNIKtPSREQLIMNLSGGNQqkailgRWLSEDM------KVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 906 GMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
35-122 |
2.65e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.09 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 35 LTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQtyKQNR----TILLTTHYMDEADML 110
Cdd:COG1135 130 LSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLK--DINRelglTIVLITHEMDVVRRI 207
|
90
....*....|..
gi 1958644180 111 GDRIAIMVQGTL 122
Cdd:COG1135 208 CDRVAVLENGRI 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
746-961 |
2.80e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 746 KQLTKIYFKSPLilaVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCP 824
Cdd:PRK10253 11 EQLTLGYGKYTV---AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 825 QFDALLEYLTGWEIMV--------MYARiWgisERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPS 896
Cdd:PRK10253 88 QNATTPGDITVQELVArgryphqpLFTR-W---RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 897 VIFLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQ 961
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPK 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
38-127 |
3.06e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 38 KRDAFSksLSGGMKRKLAI--IIALIGgsKVVILDEPTSGMDPASRRSTWDVVQTYKQN--RTILLTTHYMDEADMLGDR 113
Cdd:PRK13645 145 KRSPFE--LSGGQKRRVALagIIAMDG--NTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADE 220
|
90
....*....|....
gi 1958644180 114 IAIMVQGTLRCCGS 127
Cdd:PRK13645 221 VIVMHEGKVISIGS 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
760-931 |
3.20e-09 |
|
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: 58.40 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQfDALLEYLTGWEi 838
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAsLRRQIGLVSQ-DVFLFNDTVAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMYARIwGISERQIRPYVNTylnslelePHANSLI---------------STYSEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:cd03251 95 NIAYGRP-GATREEVEEAARA--------ANAHEFImelpegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180
....*....|....*....|....*...
gi 1958644180 904 STGMDPRARRLLWDAVIKIRESGKAIII 931
Cdd:cd03251 166 TSALDTESERLVQAALERLMKNRTTFVI 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
46-122 |
3.30e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.72 E-value: 3.30e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
745-954 |
3.59e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.61 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKiYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAG-----DVFIDG-ISITKD---VLK 815
Cdd:PRK11264 6 VKNLVK-KFHGQTVL--HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLSQQkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 816 VRSKIGYCPQFDALLEYLTGWE-IMVMYARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGK 894
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 895 PSVIFLDEPSTGMDPrarRLLWDAVIKIR---ESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:PRK11264 163 PEVILFDEPTSALDP---ELVGEVLNTIRqlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
44-122 |
3.67e-09 |
|
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: 58.50 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEADMLGDRIAIMVQGT 121
Cdd:cd03299 128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGK 207
|
.
gi 1958644180 122 L 122
Cdd:cd03299 208 L 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
760-953 |
3.96e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGeITPTA---GDVFIDG-------ISIT--KDVLKVRSKIGYCPQFD 827
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGsplkasnIRDTerAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 828 ALLEYLTGWEIM---------VMYARiwgiserqirpyVNTYLNSLELEPHANSL-ISTYSEGNKRRLSTAIAMMGKPSV 897
Cdd:TIGR02633 95 VAENIFLGNEITlpggrmaynAMYLR------------AKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 898 IFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-127 |
3.99e-09 |
|
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: 58.02 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK 92
Cdd:cd03300 98 RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQ 177
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958644180 93 QNR--TILLTTHYMDEADMLGDRIAIMVQGTLRCCGS 127
Cdd:cd03300 178 KELgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
37-122 |
4.43e-09 |
|
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: 57.89 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 37 EKRDAfsKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEADMLGDRI 114
Cdd:cd03298 122 EKRLP--GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRV 199
|
....*...
gi 1958644180 115 AIMVQGTL 122
Cdd:cd03298 200 VFLDNGRI 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
751-973 |
4.83e-09 |
|
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: 57.88 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 751 IYFK----SPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI-TKDVLKVRSKIGYCPQ 825
Cdd:cd03252 6 VRFRykpdGPVIL--DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 826 FDALLEYLTGWEI-----------MVMYARIWGISE--RQIRPYVNTYLNSlelepHANSListySEGNKRRLSTAIAMM 892
Cdd:cd03252 84 ENVLFNRSIRDNIaladpgmsmerVIEAAKLAGAHDfiSELPEGYDTIVGE-----QGAGL----SGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 893 GKPSVIFLDEPSTGMDPRARRLLWDAVIKIReSGKAIIITSHSMEECEAlCTRLSIMVHGKLTCLGSPQYLKNKFGDIYI 972
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
.
gi 1958644180 973 L 973
Cdd:cd03252 233 L 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
45-120 |
6.02e-09 |
|
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: 57.60 E-value: 6.02e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADmLGDRIAIMVQG 120
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSG 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-120 |
6.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 18 PQNMCL------EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVV-QT 90
Cdd:PRK13647 105 PVNMGLdkdeveRRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRL 184
|
90 100 110
....*....|....*....|....*....|
gi 1958644180 91 YKQNRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK13647 185 HNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
742-968 |
6.28e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 742 PVL-IKQLTKIYFKSPlilAVKNISLAIQERECFGLLGFNGAGKTTTFQILT--GEITP---TAGDVFIDGISI---TKD 812
Cdd:PRK14239 4 PILqVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIyspRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 813 VLKVRSKIGYCPQ----FDalleyLTGWEIMVMYARIWGISERQI-RPYVNTYL------NSLELEPHANSLisTYSEGN 881
Cdd:PRK14239 81 TVDLRKEIGMVFQqpnpFP-----MSIYENVVYGLRLKGIKDKQVlDEAVEKSLkgasiwDEVKDRLHDSAL--GLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 882 KRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITsHSMEECEALCTRLSIMVHGKLTCLGS-- 959
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDRTGFFLDGDLIEYNDtk 232
|
250 260
....*....|....*....|
gi 1958644180 960 -----PQ------YLKNKFG 968
Cdd:PRK14239 233 qmfmnPKhketedYISGKFG 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
745-954 |
6.72e-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: 59.45 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPT-AGDVFIDG--ISITKDVLKVRSKIG 821
Cdd:TIGR02633 260 ARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQAIRAGIA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQ---FDALLEYL-TGWEIMVM----YARIWGISERQIRPYVNTYLNSLELEPHANSL-ISTYSEGNKRRLSTAIAMM 892
Cdd:TIGR02633 340 MVPEdrkRHGIVPILgVGKNITLSvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 893 GKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:TIGR02633 420 TNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-122 |
9.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.80 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 15 KGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAI--IIALigGSKVVILDEPTSGMDPASRRSTWDVVQTYK 92
Cdd:PRK13642 110 QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVagIIAL--RPEIIILDESTSMLDPTGRQEIMRVIHEIK 187
|
90 100 110
....*....|....*....|....*....|..
gi 1958644180 93 Q--NRTILLTTHYMDEADMlGDRIAIMVQGTL 122
Cdd:PRK13642 188 EkyQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
760-953 |
9.72e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGeITPTA---GDVFIDGisitkDVLKVRS-------KIGYCPQFDAL 829
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEG-----EELQASNirdteraGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 830 LEYLT-------GWEIM--------VMYARiwgiserqirpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGK 894
Cdd:PRK13549 94 VKELSvleniflGNEITpggimdydAMYLR------------AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 895 PSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-122 |
1.01e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 56.98 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPAsrrSTWDVVQTYK 92
Cdd:COG2884 105 RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE---TSWEIMELLE 181
|
90 100 110
....*....|....*....|....*....|....
gi 1958644180 93 Q-NR---TILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:COG2884 182 EiNRrgtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
768-934 |
1.04e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 768 IQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDgisitkdvlkvrSKIGYCPQfdalleYLTGWEIMVMYARIWG 847
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------LKISYKPQ------YIKPDYDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 848 ISERQIRPYVNTYL-NSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRaRRLLWDAVIK--IRE 924
Cdd:PRK13409 424 ITDDLGSSYYKSEIiKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRLAVAKAIRriAEE 502
|
170
....*....|
gi 1958644180 925 SGKAIIITSH 934
Cdd:PRK13409 503 REATALVVDH 512
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-183 |
1.12e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.43 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 15 KGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRstwDVVQTYKQN 94
Cdd:PRK13650 110 KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL---ELIKTIKGI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 95 R-----TILLTTHYMDEAdMLGDRIAIMVQGTLRccgSSVFLKRLYGVGSHIVMVkepvcDVDeisklihyyIPTATLKT 169
Cdd:PRK13650 187 RddyqmTVISITHDLDEV-ALSDRVLVMKNGQVE---STSTPRELFSRGNDLLQL-----GLD---------IPFTTSLV 248
|
170
....*....|....
gi 1958644180 170 NVGNELSFILPKEY 183
Cdd:PRK13650 249 QSLRQNGYDLPEGY 262
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
45-128 |
1.14e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHV 231
|
....*.
gi 1958644180 123 RCCGSS 128
Cdd:PRK09984 232 FYDGSS 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
46-127 |
1.17e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.07 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLgDRIAIMVQGTLRCC 125
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
..
gi 1958644180 126 GS 127
Cdd:PRK11160 555 GT 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
719-934 |
1.24e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.79 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 719 SEDNDVENERREILYQPEKFLNCPVL-IKQLTKIYFKSPLIlavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITP 797
Cdd:TIGR03719 298 SQEFQKRNETAEIYIPPGPRLGDKVIeAENLTKAFGDKLLI---DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 798 TAGDvfidgISITKDVlkvrsKIGYCPQF-DALLEYLTGWEIMVMYARIWGISERQI--RPYVNTYlnslelephaN--- 871
Cdd:TIGR03719 375 DSGT-----IEIGETV-----KLAYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIpsRAYVGRF----------Nfkg 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 872 ----SLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIreSGKAIIItSH 934
Cdd:TIGR03719 435 sdqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVI-SH 498
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-122 |
1.41e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 32 AFNL-TEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQN-RTILLTTHYMDEADM 109
Cdd:PRK10762 381 LFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLG 460
|
90
....*....|...
gi 1958644180 110 LGDRIAIMVQGTL 122
Cdd:PRK10762 461 MSDRILVMHEGRI 473
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-122 |
1.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.15 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 38 KRDAFSKS---LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDR 113
Cdd:PRK13641 135 SEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADD 214
|
....*....
gi 1958644180 114 IAIMVQGTL 122
Cdd:PRK13641 215 VLVLEHGKL 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
747-963 |
1.90e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 747 QLTKIYFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQ 825
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 826 FDALLEYLTGWEIMVMYARIW-------GISERQirpYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVI 898
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPWhgalgrfGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 899 FLDEPSTGMDPrARRLLWDAVIK--IRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PRK10575 170 LLDEPTSALDI-AHQVDVLALVHrlSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-121 |
2.17e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 55.92 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY--KQNRTILLTTHYMDE 106
Cdd:COG3840 113 ALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELcrERGLTVLMVTHDPED 192
|
90
....*....|....*
gi 1958644180 107 ADMLGDRIAIMVQGT 121
Cdd:COG3840 193 AARIADRVLLVADGR 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
752-908 |
2.40e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 752 YFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGisitkdvlKVRSKIGYCPQFDALle 831
Cdd:PLN03073 518 YPGGPLLF--KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA--------KVRMAVFSQHHVDGL-- 585
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 832 YLTGWEIMVMYARIWGISERQIRPYVNTY--LNSLELEPhanslISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:PLN03073 586 DLSSNPLLYMMRCFPGVPEQKLRAHLGSFgvTGNLALQP-----MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
44-122 |
2.47e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-127 |
3.58e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.96 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 18 PQNMCLEE------TNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTW----DV 87
Cdd:PRK13652 104 PINLGLDEetvahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIdflnDL 183
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958644180 88 VQTYkqNRTILLTTHYMDEADMLGDRIAIMVQGtlRCCGS 127
Cdd:PRK13652 184 PETY--GMTVIFSTHQLDLVPEMADYIYVMDKG--RIVAY 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
44-123 |
3.92e-08 |
|
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: 54.95 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASR---RSTWDVVQTyKQNRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:cd03301 129 KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRvqmRAELKRLQQ-RLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
...
gi 1958644180 121 TLR 123
Cdd:cd03301 208 QIQ 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
45-115 |
4.03e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.56 E-value: 4.03e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLGDRIA 115
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
754-954 |
4.13e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.85 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 754 KSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-----------DVLKV-RSKIG 821
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrDIQMVfQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 -YCPQFDalleylTGWEIMVMYARIWGISERQIRPYVNTYLNSLELEP-HANSLISTYSEGNKRRLSTAIAMMGKPSVIF 899
Cdd:PRK10419 101 aVNPRKT------VREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 900 LDEPSTGMDprarRLLWDAVIKI-----RESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:PRK10419 175 LDEAVSNLD----LVLQAGVIRLlkklqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-122 |
4.15e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 40 DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLGDRIAIMVQ 119
Cdd:PRK14247 141 DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYK 220
|
...
gi 1958644180 120 GTL 122
Cdd:PRK14247 221 GQI 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-74 |
4.23e-08 |
|
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: 53.42 E-value: 4.23e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958644180 30 LSAFNLTEKRD----AFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTS 74
Cdd:pfam00005 102 LEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
46-138 |
4.37e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.46 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDEADML-GDRIAIMVQGTLR 123
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIV 184
|
90
....*....|....*
gi 1958644180 124 CCGSSVFLKRLYGVG 138
Cdd:cd03217 185 KSGDKELALEIEKKG 199
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
39-120 |
5.67e-08 |
|
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: 53.86 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 39 RDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTH------YMDEADMLgD 112
Cdd:cd03247 92 RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHhltgieHMDKILFL-E 170
|
....*...
gi 1958644180 113 RIAIMVQG 120
Cdd:cd03247 171 NGKIIMQG 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
40-122 |
5.73e-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: 56.73 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 40 DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMDEADMLGDRIAIM 117
Cdd:TIGR03269 422 DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALM 501
|
....*
gi 1958644180 118 VQGTL 122
Cdd:TIGR03269 502 RDGKI 506
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
761-908 |
7.29e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.81 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTA---GDVFIDGISITKDVLKVRSKIGYCPQFDALLEYLTGWE 837
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 838 IMVMYARIWGiserqirpyvntylnslelephaNSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:cd03233 103 TLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
752-934 |
7.57e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 54.47 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 752 YFKSPLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQFDALL 830
Cdd:cd03249 10 YPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 831 EYLTGWEImvMYARIWGISERQIR----PYVNTYLNSL------ELEPHANSListySEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:cd03249 90 DGTIAENI--RYGKPDATDEEVEEaakkANIHDFIMSLpdgydtLVGERGSQL----SGGQKQRIAIARALLRNPKILLL 163
|
170 180 190
....*....|....*....|....*....|....
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKIREsGKAIIITSH 934
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
763-934 |
8.26e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 763 NISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDvlkvrskigyCPQFDALLEY---------- 832
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ----------RDEYHQDLLYlghqpgikte 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 833 LTGWEIMVMYARIWG-ISERQIRpyvnTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRA 911
Cdd:PRK13538 89 LTALENLRFYQRLHGpGDDEALW----EALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|...
gi 1958644180 912 RRLLWDAVIKIRESGKAIIITSH 934
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-107 |
8.84e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTE---KRDAFSksLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQT-Y 91
Cdd:PRK13651 135 GVSKEEAKKRAAKYIELVGLDEsylQRSPFE--LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlN 212
|
90
....*....|....*.
gi 1958644180 92 KQNRTILLTTHYMDEA 107
Cdd:PRK13651 213 KQGKTIILVTHDLDNV 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
761-986 |
9.05e-08 |
|
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: 54.86 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTgEITPTAGDVFIDGISITKDVL-KVRSKIGYCPQ--------FDALLE 831
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSWNSVPLqKWRKAFGVIPQkvfifsgtFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 832 YLTGWEimvmYARIWGISER-QIRPYVNTYLNSLELEPHANSLIstYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPR 910
Cdd:cd03289 99 PYGKWS----DEEIWKVAEEvGLKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 911 ARRLLwDAVIKIRESGKAIIITSHSMeecEAL--CTRLSIMVHGKLTCLGSPQYLKNkfgDIYILKTKVKSGETLKEF 986
Cdd:cd03289 173 TYQVI-RKTLKQAFADCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLLN---EKSHFKQAISPSDRLKLF 243
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-133 |
9.99e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.85 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD-VVQTYKQ- 93
Cdd:PRK13636 112 KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKlLVEMQKEl 191
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958644180 94 NRTILLTTHYMDEADMLGDRIAIMVQGTLRCCG--SSVFLKR 133
Cdd:PRK13636 192 GLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEK 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
46-122 |
1.01e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 55.88 E-value: 1.01e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMlGDRIAIMVQGTL 122
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
30-120 |
1.10e-07 |
|
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: 54.11 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 30 LSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQ--TYKQNRTILLTTHYMDEA 107
Cdd:cd03256 129 LERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLA 208
|
90
....*....|...
gi 1958644180 108 DMLGDRIAIMVQG 120
Cdd:cd03256 209 REYADRIVGLKDG 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
747-938 |
1.13e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 747 QLTKIYFKSPLILAVKNISLAIQEREcFGLL-GFNGAGKTTTFQILTGEITPTAGDVFIDGISITkdVLK---VRSKIGY 822
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS--TLKpeiYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 823 CPQFDALL------EYLTGWEImvmyariwgiseRQIRPYVNTYLNSL---ELEPHA-NSLISTYSEGNKRRLSTAIAMM 892
Cdd:PRK10247 86 CAQTPTLFgdtvydNLIFPWQI------------RNQQPDPAIFLDDLerfALPDTIlTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958644180 893 GKPSVIFLDEPSTGMDPRARRLLWDAVIK-IRESGKAIIITSHSMEE 938
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLWVTHDKDE 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-122 |
1.21e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.94 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY- 91
Cdd:PRK09493 104 RVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLa 183
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 92 KQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK09493 184 EEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
46-117 |
1.36e-07 |
|
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: 55.37 E-value: 1.36e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHymDEADM-LGDRIAIM 117
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--RLALAaLADRIVVL 529
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
762-967 |
1.41e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.04 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITkDVLKVRSKIGYCPQFDALLEYLTGWEIMVM 841
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 842 YARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIK 921
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 922 I-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSP----QYLKNKF 967
Cdd:PRK11000 179 LhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPlelyHYPANRF 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-128 |
1.52e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 43 SKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK14246 151 ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
....*.
gi 1958644180 123 RCCGSS 128
Cdd:PRK14246 231 VEWGSS 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
45-127 |
1.61e-07 |
|
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: 53.64 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMdEADMLGDRIAIMVQGTLRC 124
Cdd:cd03252 138 GLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVE 216
|
...
gi 1958644180 125 CGS 127
Cdd:cd03252 217 QGS 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
46-117 |
1.67e-07 |
|
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: 54.29 E-value: 1.67e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHymdeaDM-----LGDRIAIM 117
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITH-----DLgvvaeIADRVAVM 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-127 |
2.42e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQ-TYKQN 94
Cdd:PRK13638 107 GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRrIVAQG 186
|
90 100 110
....*....|....*....|....*....|...
gi 1958644180 95 RTILLTTHYMDEADMLGDRIAIMVQGTLRCCGS 127
Cdd:PRK13638 187 NHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
763-955 |
2.62e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 763 NISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDgisitkdvlkVRSKIGYC--PQFdALLEYLTGWEIMV 840
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD----------PNERLGKLrqDQF-AFEEFTVLDTVIM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 841 MYARIWGISERQIRPYVNT------YLNSLELEP---------------------------HaNSLISTYSEGNKRRLST 887
Cdd:PRK15064 88 GHTELWEVKQERDRIYALPemseedGMKVADLEVkfaemdgytaearagelllgvgipeeqH-YGLMSEVAPGWKLRVLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 888 AIAMMGKPSVIFLDEPSTGMDPRARRLLWDaVIKIRESgkAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRWLED-VLNERNS--TMIIISHDRHFLNSVCTHMADLDYGELR 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
762-954 |
3.03e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIG-Y-CPQFDALLEYLTGWE-I 838
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYlVPQEPLLFPNLSVKEnI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 839 MVMYARIWGISER--QIRPYVNTYLNsleLEPHANSListysEGNKRRLSTAI-AMMGKPSVIFLDEPSTGMDPRARRLL 915
Cdd:PRK15439 108 LFGLPKRQASMQKmkQLLAALGCQLD---LDSSAGSL-----EVADRQIVEILrGLMRDSRILILDEPTASLTPAETERL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958644180 916 WDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKL 954
Cdd:PRK15439 180 FSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
43-122 |
3.17e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.07 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 43 SKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRstwDVVQTYKQ-----NRTILLTTHYMDEAdMLGDRIAIM 117
Cdd:PRK13632 140 PQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR---EIKKIMVDlrktrKKTLISITHDMDEA-ILADKVIVF 215
|
....*
gi 1958644180 118 VQGTL 122
Cdd:PRK13632 216 SEGKL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-117 |
3.35e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.94 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRStwdvVQTY- 91
Cdd:COG4525 102 RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQ----MQELl 177
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 92 -----KQNRTILLTTHYMDEADMLGDRIAIM 117
Cdd:COG4525 178 ldvwqRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
40-120 |
3.47e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 40 DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDEADMLGDRIAIMV 118
Cdd:COG3845 136 DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLR 215
|
..
gi 1958644180 119 QG 120
Cdd:COG3845 216 RG 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
42-122 |
3.81e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.54 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 42 FSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLGDRIAIMVQGT 121
Cdd:PRK14267 146 YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGK 225
|
.
gi 1958644180 122 L 122
Cdd:PRK14267 226 L 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
761-955 |
4.35e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGeITPTA--GDVFIDG----ISITKDVLKV--------RSKIGYCPQF 826
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpvkIRNPQQAIAQgiamvpedRKRDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 827 D-------ALLEYLTGWEIMVMYARIWGISERQIRPYVNTylNSLELEphanslISTYSEGNKRRLSTAIAMMGKPSVIF 899
Cdd:PRK13549 357 GvgknitlAALDRFTGGSRIDDAAELKTILESIQRLKVKT--ASPELA------IARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 900 LDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLT 955
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-127 |
4.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.68 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 18 PQNMCLEET------NNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQT- 90
Cdd:PRK13644 103 PENLCLPPIeirkrvDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKl 182
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958644180 91 YKQNRTILLTTHYMDEADMlGDRIAIMVQGTLRCCGS 127
Cdd:PRK13644 183 HEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
46-122 |
4.52e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.77 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVqtYKQNR---TILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLL--YDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
760-958 |
5.62e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.71 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISItkDVLK------VRSKIGYCPQ--FDALLE 831
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI--DTLSpgklqaLRRDIQFIFQdpYASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 832 YLT-GWEIMVMYaRIWGISE-RQIRPYVNTYLNSLELEP-HANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:PRK10261 417 RQTvGDSIMEPL-RVHGLLPgKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 909 PRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLG 958
Cdd:PRK10261 496 VSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-122 |
6.72e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 8 LCPSSQVKGVPQNMCLEetnnmLSAFNLTEKRDAFSK-SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD 86
Cdd:PRK14271 130 LVPRKEFRGVAQARLTE-----VGLWDAVKDRLSDSPfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958644180 87 VVQTYKQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK14271 205 FIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-122 |
7.52e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK 92
Cdd:COG4161 109 KVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS 188
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 93 QNR-TILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:COG4161 189 QTGiTQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
46-102 |
7.57e-07 |
|
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: 49.75 E-value: 7.57e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKqnRTILLTTH 102
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP--GTVILVSH 125
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
775-934 |
8.38e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 775 GLLGFNGAGKTTTFQILTGEITPTAGDVfiDGISITKDVL-------------KVRS---KIGYCPQF-DALLEYLTG-- 835
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDY--EEEPSWDEVLkrfrgtelqnyfkKLYNgeiKVVHKPQYvDLIPKVFKGkv 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WEImvmyarIWGISERQIRPYVntyLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARrll 915
Cdd:PRK13409 181 REL------LKKVDERGKLDEV---VERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR--- 248
|
170 180
....*....|....*....|.
gi 1958644180 916 WDAVIKIRE--SGKAIIITSH 934
Cdd:PRK13409 249 LNVARLIRElaEGKYVLVVEH 269
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
46-122 |
8.45e-07 |
|
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: 51.32 E-value: 8.45e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMlGDRIAIMVQGTL 122
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
46-130 |
8.73e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.62 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRT--ILLTTHYMDEADMLGDRIAIMVQGTLR 123
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
....*....
gi 1958644180 124 CCGS--SVF 130
Cdd:PRK10418 221 EQGDveTLF 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
775-934 |
9.62e-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: 52.86 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 775 GLLGFNGAGKTTTFQILTGEITPTAGDvfIDGISITKDVL-------------KVRS---KIGYCPQF-DALLEYLTG-- 835
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGD--YDEEPSWDEVLkrfrgtelqdyfkKLANgeiKVAHKPQYvDLIPKVFKGtv 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 836 WEIMVmyariwGISERQIrpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLL 915
Cdd:COG1245 181 RELLE------KVDERGK---LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNV 251
|
170
....*....|....*....
gi 1958644180 916 WDAVIKIRESGKAIIITSH 934
Cdd:COG1245 252 ARLIRELAEEGKYVLVVEH 270
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
45-122 |
1.07e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.19 E-value: 1.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-128 |
1.16e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.80 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ-NRTILLTTH 102
Cdd:COG1137 115 ERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKErGIGVLITDH 194
|
90 100
....*....|....*....|....*...
gi 1958644180 103 YMDEadMLG--DRIAIMVQGTLRCCGSS 128
Cdd:COG1137 195 NVRE--TLGicDRAYIISEGKVLAEGTP 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
34-120 |
1.21e-06 |
|
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: 50.75 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 34 NLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDEADMLGD 112
Cdd:COG0410 125 RLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIAD 204
|
....*...
gi 1958644180 113 RIAIMVQG 120
Cdd:COG0410 205 RAYVLERG 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
45-102 |
1.45e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 1.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTH 102
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
44-117 |
1.55e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.94 E-value: 1.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDEADMLGDRIAIM 117
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
764-963 |
1.68e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 764 ISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK-DVLKVRSKIGYCPQFDALLEYLTGWEIMVMY 842
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 843 ----ARIWGISER-QIRPYVNTylNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRArrllwD 917
Cdd:PLN03232 1335 ehndADLWEALERaHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-----D 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 918 AVIK--IRESGKA--IIITSHSMEECeALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PLN03232 1408 SLIQrtIREEFKSctMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
40-135 |
2.05e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.26 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 40 DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMDEADMLGDRIAIM 117
Cdd:PRK11432 131 DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVM 210
|
90
....*....|....*...
gi 1958644180 118 VQGTLRCCGSSvflKRLY 135
Cdd:PRK11432 211 NKGKIMQIGSP---QELY 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
30-120 |
2.30e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.45 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 30 LSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEA 107
Cdd:PRK11247 118 LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEA 197
|
90
....*....|...
gi 1958644180 108 DMLGDRIAIMVQG 120
Cdd:PRK11247 198 VAMADRVLLIEEG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
46-122 |
2.31e-06 |
|
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: 48.75 E-value: 2.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMdEADMLGDRIAIMVQGTL 122
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
44-102 |
2.42e-06 |
|
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: 51.59 E-value: 2.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTH 102
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
874-937 |
2.79e-06 |
|
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: 50.47 E-value: 2.79e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 874 ISTYSEGNKR--RLSTAIAM-MGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSME 937
Cdd:pfam13304 234 AFELSDGTKRllALLAALLSaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-120 |
3.00e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.08 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAFNL-TEKR-DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRS----TWDVVQtyKQNRTILLTTH 102
Cdd:COG1101 130 LLATLGLgLENRlDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALvlelTEKIVE--ENNLTTLMVTH 207
|
90
....*....|....*...
gi 1958644180 103 YMDEADMLGDRIAIMVQG 120
Cdd:COG1101 208 NMEQALDYGNRLIMMHEG 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-120 |
3.44e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 14 VKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ 93
Cdd:PRK11124 110 VLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE 189
|
90 100
....*....|....*....|....*...
gi 1958644180 94 NR-TILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK11124 190 TGiTQVIVTHEVEVARKTASRVVYMENG 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-102 |
4.28e-06 |
|
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: 48.94 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPAsrrSTWDVVQTYK 92
Cdd:cd03292 104 EVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD---TTWEIMNLLK 180
|
90
....*....|....
gi 1958644180 93 Q----NRTILLTTH 102
Cdd:cd03292 181 KinkaGTTVVVATH 194
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
761-963 |
6.11e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.32 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTT---TFQILTGEIT--PTAGDVFIDGISI--TKDVLKVRSKIGycpqfdALLEYL 833
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTflrTLNRMNDKVSgyRYSGDVLLGGRSIfnYRDVLEFRRRVG------MLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 834 TGWEIMVMYARIWGIS------ERQIRPYVNTYLNSLELEPHANSLIST----YSEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRahklvpRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 904 STGMDPRARRLLwDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSPQYL 963
Cdd:PRK14271 191 TSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
739-934 |
6.32e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 739 LNCPVL-IKQLtKIYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGE--ITPTAGDVFIDGISITKDVLK 815
Cdd:CHL00131 3 KNKPILeIKNL-HASVNENEIL--KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 816 VRSKIGYCPQFDALLEyLTGWE----IMVMY-ARIWGISERQIRP-----YVNTYLNSLELEPH--ANSLISTYSEGNKR 883
Cdd:CHL00131 80 ERAHLGIFLAFQYPIE-IPGVSnadfLRLAYnSKRKFQGLPELDPlefleIINEKLKLVGMDPSflSRNVNEGFSGGEKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 884 RlsTAIAMMG--KPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSH 934
Cdd:CHL00131 159 R--NEILQMAllDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
46-127 |
7.19e-06 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 48.52 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEADMLGDRIAIMVQGTLR 123
Cdd:TIGR02770 126 LSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARVLKLLRELRQLFgtGILLITHDLGVVARIADEVAVMDDGRIV 205
|
....
gi 1958644180 124 CCGS 127
Cdd:TIGR02770 206 ERGT 209
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
40-120 |
7.35e-06 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 48.67 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 40 DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTI--LLTTHYMDEADMLGDRIAIM 117
Cdd:TIGR02323 143 DDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLVM 222
|
...
gi 1958644180 118 VQG 120
Cdd:TIGR02323 223 QQG 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
44-102 |
8.69e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.66 E-value: 8.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRStwdVVQTYK----QNRTILLTTH 102
Cdd:TIGR00955 165 KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS---VVQVLKglaqKGKTIICTIH 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
762-951 |
1.03e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.03 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEI--TPTAGDVFIDGISITKDVLKVRSkIGYCPQFDALLEYLTgweiM 839
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLIDA-IGRKGDFKDAVELLN----A 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 840 VmyariwGISERQ--IRPYvntylnslelephansliSTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWD 917
Cdd:COG2401 122 V------GLSDAVlwLRRF------------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1958644180 918 AVIKI-RESGKAIIITSHSMEECEALCTRLSIMVH 951
Cdd:COG2401 178 NLQKLaRRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-115 |
1.17e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.11 E-value: 1.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY--KQNRTILLTTHYMDEADMLGDRIA 115
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
45-127 |
1.18e-05 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 48.95 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:TIGR02142 131 RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
....*
gi 1958644180 123 RCCGS 127
Cdd:TIGR02142 211 AAAGP 215
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
758-935 |
1.19e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 758 ILAVKNISLAIQERECFGLL------------GFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKVRSKIGYcpQ 825
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGH--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 826 FDALLEyLTGWEIMVMYARIWGISERqirpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPST 905
Cdd:PRK13541 79 LGLKLE-MTVFENLKFWSEIYNSAET-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180 190
....*....|....*....|....*....|
gi 1958644180 906 GMDPRARRLLWDAVIKIRESGKAIIITSHS 935
Cdd:PRK13541 153 NLSKENRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-117 |
1.19e-05 |
|
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: 47.81 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKR-DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQN 94
Cdd:COG4778 122 GVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR 201
|
90 100
....*....|....*....|....*.
gi 1958644180 95 RTILLT-THymDEADM--LGDRIAIM 117
Cdd:COG4778 202 GTAIIGiFH--DEEVReaVADRVVDV 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
41-129 |
1.44e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 41 AFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEADMLGDRIAIMV 118
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWADKINVLY 233
|
90
....*....|.
gi 1958644180 119 qgtlrcCGSSV 129
Cdd:PRK15093 234 ------CGQTV 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-122 |
1.53e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 47.66 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 4 ESPLlcpssQVKGVPQNMCLEETNNMLSAFNLTEK-RDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRR 82
Cdd:PRK10619 115 EAPI-----QVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG 189
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958644180 83 STWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK10619 190 EVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
42-117 |
1.54e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 42 FSKSLSGGMKRK--LAIIIAL--IGGSKVVILDEPTSGMDPASRRSTWDVV-QTYKQNRTILLTTHYMDEADMLgDRIAI 116
Cdd:cd03227 74 TRLQLSGGEKELsaLALILALasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELA-DKLIH 152
|
.
gi 1958644180 117 M 117
Cdd:cd03227 153 I 153
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-120 |
1.65e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 15 KGVPQNMCLEETNNMLSAFNLTEKRDAFSK---SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY 91
Cdd:PRK10261 135 QGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVL 214
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 92 KQNRT--ILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK10261 215 QKEMSmgVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
759-968 |
1.76e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 759 LAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVfidgisitkDVL-----------KVRSKIGYCPQfd 827
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV---------EVLggdmadarhrrAVCPRIAYMPQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 828 AL---LeY--LTGWEIMVMYARIWGIS--ERQIRpyVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:NF033858 84 GLgknL-YptLSVFENLDFFGRLFGQDaaERRRR--IDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKIRES--GKAIIITSHSMEECEAlCTRLSIMVHGKLTCLGSPQYLKNKFG 968
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
44-102 |
1.80e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 46.79 E-value: 1.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTH 102
Cdd:PRK13539 126 GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlAQGGIVIAATH 185
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
46-142 |
1.99e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.57 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRStwdvVQTYK--QNRTILLTTHYMDEADMlGDRIAIMVQGTLR 123
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL----LQESRsrASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
90
....*....|....*....
gi 1958644180 124 CCGSSVFLKRLYGVGSHIV 142
Cdd:TIGR00958 693 EMGTHKQLMEDQGCYKHLV 711
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
44-122 |
2.25e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.09 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 44 KSLSGGMKRKlaIIIA--LIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:COG1129 393 GNLSGGNQQK--VVLAkwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPELLGLSDRILVMREG 470
|
..
gi 1958644180 121 TL 122
Cdd:COG1129 471 RI 472
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
46-127 |
2.26e-05 |
|
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: 46.72 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDE-ADMlgDRIAIMVQGTLRC 124
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVE 217
|
...
gi 1958644180 125 CGS 127
Cdd:cd03244 218 FDS 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
745-966 |
2.54e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.59 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTkIYFKSP--LILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITP----TAGDVFIDGIsitkDVLK--- 815
Cdd:COG4170 6 IRNLT-IEIDTPqgRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGI----DLLKlsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 816 ------VRSKIGYCPQ------------FDALLEYLTGWEIMVMYARIWGISERQ---------IRPYvNTYLNSLeleP 868
Cdd:COG4170 81 rerrkiIGREIAMIFQepsscldpsakiGDQLIEAIPSWTFKGKWWQRFKWRKKRaiellhrvgIKDH-KDIMNSY---P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 869 HanslisTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRAR----RLLwDAVIKIResGKAIIITSHSMEECEALCT 944
Cdd:COG4170 157 H------ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQaqifRLL-ARLNQLQ--GTSILLISHDLESISQWAD 227
|
250 260
....*....|....*....|..
gi 1958644180 945 RLSIMVHGKLTCLGSPQYLKNK 966
Cdd:COG4170 228 TITVLYCGQTVESGPTEQILKS 249
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
760-934 |
2.61e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.26 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLkvrskIGYCPQFDALLE--YLtgwe 837
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR-----EAYRQLFSAVFSdfHL---- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 838 imvmYARIWGISERQIRPYVNTYLNSLELE---PHANSLIST--YSEGNKRRLSTAIAMM-GKPsVIFLDEPSTGMDPRA 911
Cdd:COG4615 418 ----FDRLLGLDGEADPARARELLERLELDhkvSVEDGRFSTtdLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPEF 492
|
170 180
....*....|....*....|....
gi 1958644180 912 RRLLWDAVI-KIRESGKAIIITSH 934
Cdd:COG4615 493 RRVFYTELLpELKARGKTVIAISH 516
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
756-953 |
2.77e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 756 PLILAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISI----TKDVLKvrSKIGYCPQFDALLE 831
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALE--NGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 832 YLTgweimVMyARIW-------GISERQIRPYVNT--YLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:PRK10982 87 QRS-----VM-DNMWlgryptkGMFVDQDKMYRDTkaIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 903 PSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLSIMVHGK 953
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
776-959 |
2.84e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 776 LLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLKV-----RSKIGYCPQfDALL--EYltgweiMVMYARIWGI 848
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQ-DARLfpHY------KVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 849 SeRQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD-PRARRLL-----WDAVIKI 922
Cdd:PRK11144 102 A-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLpylerLAREINI 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958644180 923 resgkAIIITSHSMEECEALCTRLSIMVHGKLTCLGS 959
Cdd:PRK11144 181 -----PILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
15-120 |
2.88e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.41 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 15 KGVPQNMCLEETNNMLSAFNLTEKR---DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY 91
Cdd:PRK09473 128 KGMSKAEAFEESVRMLDAVKMPEARkrmKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNEL 207
|
90 100 110
....*....|....*....|....*....|.
gi 1958644180 92 KQ--NRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK09473 208 KRefNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
28-102 |
3.88e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.37 E-value: 3.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 28 NMLSAFNLTEKrDAFSK--SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQnrTILLTTH 102
Cdd:COG0488 414 GYLGRFLFSGD-DAFKPvgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVSH 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
868-955 |
3.98e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 868 PHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHSMEECEALCTRLS 947
Cdd:PRK10982 383 PGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIL 462
|
....*...
gi 1958644180 948 IMVHGKLT 955
Cdd:PRK10982 463 VMSNGLVA 470
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
745-908 |
5.15e-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: 47.24 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQIL-------TGEITPTAG----------------D 801
Cdd:TIGR03719 7 MNRVSKVVPPKKEIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfNGEARPQPGikvgylpqepqldptkT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 802 VF---IDGISITKDVLKVRSKIG--YC---PQFDALLEYLTGWEIMVMYARIWGIsERQIrpyvNTYLNSLELePHANSL 873
Cdd:TIGR03719 85 VRenvEEGVAEIKDALDRFNEISakYAepdADFDKLAAEQAELQEIIDAADAWDL-DSQL----EIAMDALRC-PPWDAD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1958644180 874 ISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
46-122 |
5.18e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 47.15 E-value: 5.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDE-ADMlgDRIAIMVQGTL 122
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDlAQW--DQIWVMQDGQI 561
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
762-953 |
5.21e-05 |
|
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: 45.54 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 762 KNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFidgisitkdvlkVRSKIGYCPQfdalleylTGWeIMVM 841
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS------------VPGSIAYVSQ--------EPW-IQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 842 YAR---IWGiserqiRPYVNTYLNS----------LELEPHA-NSLI----STYSEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:cd03250 81 TIReniLFG------KPFDEERYEKvikacalepdLEILPDGdLTEIgekgINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 904 STGMDPRARRLLWDAVI-KIRESGKAIIITSHSMEECEAlCTRLSIMVHGK 953
Cdd:cd03250 155 LSAVDAHVGRHIFENCIlGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
772-955 |
5.59e-05 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 45.44 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 772 ECFGLLGFNGAGKTTTFQILTGEITPTAGDVfidgISITKDVLKVRSKigycpqfDALLEYLTGWEIMVMYARIWGISER 851
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEGDF----IGLRGDALPLGAN-------SFILPGLTGEENARMMASLYGLDGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 852 QIRPYVntyLNSLELEPHANSLISTYSEGNKRRLSTAIAMMgKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIII 931
Cdd:PRK15177 83 EFSHFC---YQLTQLEQCYTDRVSEYSVTMKTHLAFAINLL-LPCRLYIADGKLYTGDNATQLRMQAALACQLQQKGLIV 158
|
170 180
....*....|....*....|....
gi 1958644180 932 TSHSMEECEALCTRLSIMVHGKLT 955
Cdd:PRK15177 159 LTHNPRLIKEHCHAFGVLLHGKIT 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
745-983 |
6.02e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.02 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 745 IKQLTKIYFKSPLILavKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDG---ISITKDVLkvRSKIG 821
Cdd:PRK10790 343 IDNVSFAYRDDNLVL--QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHSVL--RQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 822 YCPQ-----FDALLEYLT-GWEImvMYARIWGISER-QIRPYVNTYLNSLE--LEPHANSListySEGNKRRLSTAIAMM 892
Cdd:PRK10790 419 MVQQdpvvlADTFLANVTlGRDI--SEEQVWQALETvQLAELARSLPDGLYtpLGEQGNNL----SVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 893 GKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIItSHsmeecealctRLS-------IMV--HGKLTCLGSPQYL 963
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI-AH----------RLStiveadtILVlhRGQAVEQGTHQQL 561
|
250 260
....*....|....*....|
gi 1958644180 964 KNKFGDIYILKTKVKSGETL 983
Cdd:PRK10790 562 LAAQGRYWQMYQLQLAGEEL 581
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
35-120 |
7.37e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 45.64 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 35 LTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQN-RTILLTTHYMDEADMLGDR 113
Cdd:PRK11614 127 LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADR 206
|
....*..
gi 1958644180 114 IAIMVQG 120
Cdd:PRK11614 207 GYVLENG 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
44-120 |
7.82e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.18 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASR---RStwDVVQTYKQ-NRTILLTTHYMDEADMLGDRIAIMVQ 119
Cdd:PRK11000 132 KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvqmRI--EISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDA 209
|
.
gi 1958644180 120 G 120
Cdd:PRK11000 210 G 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
27-120 |
7.90e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 46.37 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 27 NNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASR-RSTWDVVQTYKQ-NRTILLTTHYM 104
Cdd:PRK11607 131 NEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdRMQLEVVDILERvGVTCVMVTHDQ 210
|
90
....*....|....*.
gi 1958644180 105 DEADMLGDRIAIMVQG 120
Cdd:PRK11607 211 EEAMTMAGRIAIMNRG 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
33-120 |
9.26e-05 |
|
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: 44.56 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 33 FNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPAsrrSTWDVVQTYKQNRTILLTTHYM------DE 106
Cdd:cd03233 106 FALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS---TALEILKCIRTMADVLKTTTFVslyqasDE 182
|
90
....*....|....
gi 1958644180 107 ADMLGDRIAIMVQG 120
Cdd:cd03233 183 IYDLFDKVLVLYEG 196
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
760-931 |
1.10e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.11 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDVLK-VRSKIGYCPQfDALL-------- 830
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIAVVFQ-DAGLfnrsiedn 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 831 -----EYLTGWEIMVMYAR--IWGISERQIRPYvNTYLNSlelepHANSListySEGNKRRLSTAIAMMGKPSVIFLDEP 903
Cdd:PRK13657 429 irvgrPDATDEEMRAAAERaqAHDFIERKPDGY-DTVVGE-----RGRQL----SGGERQRLAIARALLKDPPILILDEA 498
|
170 180
....*....|....*....|....*...
gi 1958644180 904 STGMDPRARRLLWDAVIKIRESGKAIII 931
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMKGRTTFII 526
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-127 |
1.11e-04 |
|
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: 45.02 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 24 EETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRS--TWDVVQTYKQNRTILLTT 101
Cdd:cd03296 115 AKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKElrRWLRRLHDELHVTTVFVT 194
|
90 100
....*....|....*....|....*.
gi 1958644180 102 HYMDEADMLGDRIAIMVQGTLRCCGS 127
Cdd:cd03296 195 HDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
761-947 |
1.13e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.03 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILT------GEITpTAGDVFIDGISITK---DVLKVRSKIGYC---PQFDA 828
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVR-VEGRVEFFNQNIYErrvNLNRLRRQVSMVhpkPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 829 LLEY--------LTGWEIMVmyaRIWGISERQIRPyvNTYLNSLELEPHANSLisTYSEGNKRRLSTAIAMMGKPSVIFL 900
Cdd:PRK14258 102 MSVYdnvaygvkIVGWRPKL---EIDDIVESALKD--ADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958644180 901 DEPSTGMDPRARRLLWDAVIKIR-ESGKAIIITSHSMEEcealCTRLS 947
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQ----VSRLS 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-122 |
1.19e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 34 NLTEkrdafsksLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVV-QTYKQNRTILLTTHYMDEADMLGD 112
Cdd:PRK09700 406 NITE--------LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMrQLADDGKVILMVSSELPEIITVCD 477
|
90
....*....|
gi 1958644180 113 RIAIMVQGTL 122
Cdd:PRK09700 478 RIAVFCEGRL 487
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
761-933 |
1.20e-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: 46.44 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVfidgisitkdvlKVRSKIGYCPQFDalleyltgWeIMV 840
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------KHSGRISFSPQTS--------W-IMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 841 MYAR---IWGISERQIRpyVNTYLNSLELE------PHANSLI-----STYSEGNKRRLSTAIAMMGKPSVIFLDEPSTG 906
Cdd:TIGR01271 501 GTIKdniIFGLSYDEYR--YTSVIKACQLEedialfPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180
....*....|....*....|....*...
gi 1958644180 907 MDPRARRLLWDA-VIKIRESGKAIIITS 933
Cdd:TIGR01271 579 LDVVTEKEIFEScLCKLMSNKTRILVTS 606
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
760-963 |
1.55e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.59 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 760 AVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITK---DVLkvRSKIGYCPQ----FDALLEy 832
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseAAL--RQAISVVSQrvhlFSATLR- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 833 ltgwEIMVMYARiwGISERQIRpyvnTYLNSLELEPHANSL--ISTY--------SEGNKRRLSTAIAMMGKPSVIFLDE 902
Cdd:PRK11160 432 ----DNLLLAAP--NASDEALI----EVLQQVGLEKLLEDDkgLNAWlgeggrqlSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 903 PSTGMDPRARRLLWDAVIKIREsGKAIIITSH---SMEECEALCtrlsIMVHGKLTCLGSPQYL 963
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHAQ-NKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQEL 560
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-102 |
1.70e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.49 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 16 GVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVV-QTYKQN 94
Cdd:PRK10535 115 GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILhQLRDRG 194
|
....*...
gi 1958644180 95 RTILLTTH 102
Cdd:PRK10535 195 HTVIIVTH 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
46-120 |
1.83e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.19 E-value: 1.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNR--TILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-126 |
2.36e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 10 PSSQVKGVP---QNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD 86
Cdd:PRK09700 107 LTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958644180 87 VV-QTYKQNRTILLTTHYMDEADMLGDRIAIMVQGTLRCCG 126
Cdd:PRK09700 187 IMnQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
42-124 |
2.51e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 42 FSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMDEADMLGDRIAIMVQ 119
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQN 232
|
....*
gi 1958644180 120 GtlRC 124
Cdd:PRK15134 233 G--RC 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
45-140 |
2.72e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 43.99 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMK------RKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQ--TYKQNRTILLTTHYMDEADMLGDRIAI 116
Cdd:PRK13548 134 QLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARqlAHERGLAVIVVLHDLNLAARYADRIVL 213
|
90 100 110
....*....|....*....|....*....|....
gi 1958644180 117 MVQGTLRCCGS--SVF----LKRLYG----VGSH 140
Cdd:PRK13548 214 LHQGRLVADGTpaEVLtpetLRRVYGadvlVQPH 247
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-102 |
2.86e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.77 E-value: 2.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTH 102
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
47-120 |
3.06e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.76 E-value: 3.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 47 SGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY--KQNRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvrELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-107 |
3.08e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 43.53 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 13 QVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRrstwDVVQT-- 90
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR----EQMQTll 171
|
90 100
....*....|....*....|.
gi 1958644180 91 ----YKQNRTILLTTHYMDEA 107
Cdd:PRK11248 172 lklwQETGKQVLLITHDIEEA 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
42-102 |
3.13e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 3.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 42 FSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTH 102
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAH 1417
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-111 |
3.31e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 43.27 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 6 PLLcpssqVKGVPQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTW 85
Cdd:PRK11629 111 PLL-----IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
90 100
....*....|....*....|....*...
gi 1958644180 86 DVVQ--TYKQNRTILLTTHYMDEADMLG 111
Cdd:PRK11629 186 QLLGelNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
45-102 |
3.80e-04 |
|
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: 43.30 E-value: 3.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTH 102
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
45-120 |
3.95e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.18 E-value: 3.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMD---EAdmlgDRIAIMVQG 120
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNG 545
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-102 |
4.05e-04 |
|
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: 42.87 E-value: 4.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 30 LSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPAS-RRSTWDVVQTYKQNRTILLTTH 102
Cdd:cd03231 110 LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGvARFAEAMAGHCARGGMVVLTTH 183
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
44-102 |
4.07e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 44.29 E-value: 4.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRstW--DVVQTYKqnRTILLTTH 102
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYP--GTVLVVSH 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
46-120 |
4.35e-04 |
|
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: 42.99 E-value: 4.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEAdMLGDRIAIMVQG 120
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTI-ENADRIVVLEDG 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
636-936 |
5.25e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 636 QKNVLKYLNCSKEYTKKniYSLKKPMIGKYLIAMsIAGFVYLLFIF-FWENISWKLRMLIHQH------------IYFGV 702
Cdd:PTZ00265 255 EKTILKKFNLSEKLYSK--YILKANFMESLHIGM-INGFILASYAFgFWYGTRIIISDLSNQQpnndfhggsvisILLGV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 703 -CKKYKSDIISNELSGTSEDNDVENERREILYQPEKFLNCP--VLIKQLTKIYFKSPL--------ILAVKNISLAIQER 771
Cdd:PTZ00265 332 lISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDdgKKLKDIKKIQFKNVRfhydtrkdVEIYKDLNFTLTEG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 772 ECFGLLGFNGAGKTTTFQILTGEITPTAGDVFIDGISITKDV-LK-VRSKIGYCPQfDAL-------------------L 830
Cdd:PTZ00265 412 KTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDInLKwWRSKIGVVSQ-DPLlfsnsiknnikyslyslkdL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 831 EYLTGW------------------------------------EIMVMYARIWGISERQI-----RPYVNTYLNSL--ELE 867
Cdd:PTZ00265 491 EALSNYynedgndsqenknkrnscrakcagdlndmsnttdsnELIEMRKNYQTIKDSEVvdvskKVLIHDFVSALpdKYE 570
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 868 PHANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAI-IITSHSM 936
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRL 640
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-127 |
5.53e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.32 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 40 DAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ--NRTILLTTHYMDEADMLGDRIAIM 117
Cdd:PRK11144 123 DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAReiNIPILYVSHSLDEILRLADRVVVL 202
|
90
....*....|
gi 1958644180 118 VQGTLRCCGS 127
Cdd:PRK11144 203 EQGKVKAFGP 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
29-120 |
6.02e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.53 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRS--TWdVVQTYKQNR-TILLTTHYMD 105
Cdd:PRK10851 120 LLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKElrRW-LRQLHEELKfTSVFVTHDQE 198
|
90
....*....|....*
gi 1958644180 106 EADMLGDRIAIMVQG 120
Cdd:PRK10851 199 EAMEVADRVVVMSQG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
46-120 |
8.94e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.01 E-value: 8.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTW-DVVQTYKQ-NRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQnELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
868-932 |
9.65e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 9.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 868 PHANSListySEGNKRRLSTAIAMMGKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIIT 932
Cdd:PTZ00265 1354 PYGKSL----SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
761-933 |
9.74e-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: 42.54 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTAGDVfidgisitkdvlKVRSKIGYCPQFdalleyltGWeIMV 840
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KHSGRISFSSQF--------SW-IMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 841 MYAR---IWGISERQIRpyVNTYLNSLELEPHANSLIS-----------TYSEGNKRRLSTAIAMMGKPSVIFLDEPSTG 906
Cdd:cd03291 112 GTIKeniIFGVSYDEYR--YKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180
....*....|....*....|....*...
gi 1958644180 907 MDPRARRLLWDA-VIKIRESGKAIIITS 933
Cdd:cd03291 190 LDVFTEKEIFEScVCKLMANKTRILVTS 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
27-108 |
1.07e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 41.70 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 27 NNMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTI--LLTTHym 104
Cdd:COG4136 115 EQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTH-- 192
|
....
gi 1958644180 105 DEAD 108
Cdd:COG4136 193 DEED 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
45-129 |
1.09e-03 |
|
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: 42.89 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVV-QTYKQNRTILLTTHYMDEADMLGDRIAIMVQGTLr 123
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL- 481
|
....*.
gi 1958644180 124 cCGSSV 129
Cdd:TIGR02633 482 -KGDFV 486
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
45-121 |
1.12e-03 |
|
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: 41.30 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWD-VVQTY-KQNRTILLTTH---YMDEAdmlgDRIAIMVQ 119
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLlLNNKTRILVTHqlqLLPHA----DQIVVLDN 202
|
..
gi 1958644180 120 GT 121
Cdd:cd03250 203 GR 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
46-120 |
1.19e-03 |
|
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: 41.83 E-value: 1.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHYMDEAdMLGDRIAIMVQG 120
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDG 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
43-120 |
1.27e-03 |
|
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: 42.80 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 43 SKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVqTYKQNRTILLTTHYMDEADMLgDRIAIMVQG 120
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQS-DKIIVLDHG 684
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
761-960 |
1.40e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 41.74 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 761 VKNISLAIQERECFGLLGFNGAGKTTTFQILTGEITPTA--------GDVFIDGISITK-DVLKVRSKIGYCPQFDALLE 831
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAiDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 832 YLTGWEIMVM----YARIWGISERQIRPYVNTYLNSLELEPHANSLISTYSEGNKRRLSTAIAM---------MGKPSVI 898
Cdd:PRK13547 97 AFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644180 899 FLDEPSTGMDPRARRLLWDAVIKI-RESGKAIIITSHSMEECEALCTRLSIMVHGKLTCLGSP 960
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
704-908 |
1.45e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 704 KKYKSDIISNELSGTSEDNDVEnerreilYQPeKFLNCPVLI-KQLTKIYFK---SPLILAVKNISLAIQERECFGLLGF 779
Cdd:TIGR00956 24 KPYKLGVAYKNLSAYGVAADSD-------YQP-TFPNALLKIlTRGFRKLKKfrdTKTFDILKPMDGLIKPGELTVVLGR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 780 NGAGKTTTFQILTGEI----TPTAGDVFIDGISITKDVLKVRSKIGYCPQFDALLEYLTGWEIMVMYA-------RIWGI 848
Cdd:TIGR00956 96 PGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAArcktpqnRPDGV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 849 SERQIRPYV-NTYLNSLELEpH------ANSLISTYSEGNKRRLSTAIAMMGKPSVIFLDEPSTGMD 908
Cdd:TIGR00956 176 SREEYAKHIaDVYMATYGLS-HtrntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
749-820 |
2.02e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 41.98 E-value: 2.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644180 749 TKIYFKsplilAVKNISLAIQERECFGLLGFNGAGKTTTFQILTGEItPTAGDVFIDGISIT----KDVLKVRSKI 820
Cdd:COG4172 295 TVGHVK-----AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDglsrRALRPLRRRM 364
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
46-126 |
2.39e-03 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 41.66 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQ-NRTILLTTH---YMDEAdmlgDRIAIMVQGT 121
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHrpsLLAAV----DKLLVLRDGR 543
|
....*
gi 1958644180 122 LRCCG 126
Cdd:COG4618 544 VQAFG 548
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
852-935 |
2.39e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 852 QIRPYVNTYLNSLELEPHANSListySEGNKRRLSTAIAMMG--KPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAI 929
Cdd:cd03238 67 QLQFLIDVGLGYLTLGQKLSTL----SGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTV 142
|
....*.
gi 1958644180 930 IITSHS 935
Cdd:cd03238 143 ILIEHN 148
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
45-140 |
2.49e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 40.87 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRK--LAIIIALI-----GGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAI 116
Cdd:COG4559 133 TLSGGEQQRvqLARVLAQLwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILL 212
|
90 100 110
....*....|....*....|....*....|....
gi 1958644180 117 MVQGTLRCCGS--SVF----LKRLYG----VGSH 140
Cdd:COG4559 213 LHQGRLVAQGTpeEVLtdelLERVYGadlrVLAH 246
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
45-126 |
2.58e-03 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 41.37 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAIMVQGTLR 123
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLvDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
...
gi 1958644180 124 CCG 126
Cdd:PRK09536 219 AAG 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
44-116 |
2.62e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 2.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 44 KSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMdpaSRRSTWD----VVQTYKQNRTILLTTHYMDEADMLGDRIAI 116
Cdd:PRK11288 139 KYLSIGQRQMVEIAKALARNARVIAFDEPTSSL---SAREIEQlfrvIRELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
46-120 |
2.64e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 2.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644180 46 LSGGMKRKlaIIIA--LIGGSKVVILDEPTSGMDPASRRSTWDVV-QTYKQNRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK11288 397 LSGGNQQK--AILGrwLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
43-102 |
2.72e-03 |
|
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: 40.67 E-value: 2.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 43 SKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTH 102
Cdd:cd03254 137 GGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
844-934 |
3.04e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 844 RIWGISERQIRPYVntylnslelEPHANSLISTYSEGNKRRLSTAIAM----MGKPSVIFLDEPSTGMDPRARRLLWDAV 919
Cdd:cd03227 54 RRSGVKAGCIVAAV---------SAELIFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
90
....*....|....*
gi 1958644180 920 IKIRESGKAIIITSH 934
Cdd:cd03227 125 LEHLVKGAQVIVITH 139
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
45-159 |
3.12e-03 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 40.77 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQN-RTILLTTHYMDEADMLGDRIAIMVQGTLR 123
Cdd:PRK11231 138 DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958644180 124 CCGSsvflkrlygvgSHIVMVKEPVCDVDEISKLIH 159
Cdd:PRK11231 218 AQGT-----------PEEVMTPGLLRTVFDVEAEIH 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
46-80 |
3.13e-03 |
|
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: 39.44 E-value: 3.13e-03
10 20 30
....*....|....*....|....*....|....*
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPAS 80
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-102 |
3.13e-03 |
|
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: 40.03 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 19 QNMCLEetnnMLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPAS-RRSTWDVVQTYKQNRTI 97
Cdd:TIGR01189 105 QRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGvALLAGLLRAHLARGGIV 180
|
....*
gi 1958644180 98 LLTTH 102
Cdd:TIGR01189 181 LLTTH 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
46-126 |
3.37e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 40.64 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDEADMLGDrIAIMVQGTLRC 124
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLA 221
|
..
gi 1958644180 125 CG 126
Cdd:PRK15056 222 SG 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
47-134 |
3.45e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 47 SGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK-QNRTILLTTHYMDEAD-MLGDRIAIMVQGTLRC 124
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDyIKPDYVHVMQNGKIIK 232
|
90
....*....|
gi 1958644180 125 CGSSVFLKRL 134
Cdd:CHL00131 233 TGDAELAKEL 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
775-837 |
3.97e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 3.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 775 GLLGFNGAGKTTTFQILTGEITPTAGDvfidgISITKDVlkvrsKIGYCPQF-DALLEYLTGWE 837
Cdd:PRK11819 354 GIIGPNGAGKSTLFKMITGQEQPDSGT-----IKIGETV-----KLAYVDQSrDALDPNKTVWE 407
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
45-123 |
4.10e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVV-QTYKQNRTILLTTHYMDEADMLGDRIAIMVQGTLR 123
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLInQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
43-102 |
4.20e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 4.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644180 43 SKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYK--QNRTILLTTH 102
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAH 638
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-121 |
4.62e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 39.97 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 30 LSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPasrRSTWDVVQTYKQNR-----TILLTTHYM 104
Cdd:PRK11300 138 LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNP---KETKELDELIAELRnehnvTVLLIEHDM 214
|
90
....*....|....*..
gi 1958644180 105 DEADMLGDRIAIMVQGT 121
Cdd:PRK11300 215 KLVMGISDRIYVVNQGT 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
746-825 |
4.75e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 746 KQLTKIYFKSPLILavKNISLAiqerecF------GLLGFNGAGKTTTFQILTGEITPTAGDVFI-DGIsitkdvlkvrs 818
Cdd:PRK11819 10 NRVSKVVPPKKQIL--KDISLS------FfpgakiGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI----------- 70
|
....*..
gi 1958644180 819 KIGYCPQ 825
Cdd:PRK11819 71 KVGYLPQ 77
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-117 |
5.15e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 29 MLSAFNLTEKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTYKQNRTILLTTHymDEA- 107
Cdd:PRK13409 196 VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH--DLAv 273
|
90
....*....|.
gi 1958644180 108 -DMLGDRIAIM 117
Cdd:PRK13409 274 lDYLADNVHIA 284
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
37-77 |
5.49e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 5.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958644180 37 EKRDAFSKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMD 77
Cdd:PRK15134 417 ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
45-120 |
6.00e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 6.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVV-QTYKQNRTILLTTHYMDEADMLGDRIAIMVQG 120
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIaELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-122 |
6.06e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 3 QEsPLLCPSSQVKgvpQNMCLEETNNMLSAFNLTEKRDAFSKSLSGGMK--------RKLA-IIIALIGGSKVVILDEPT 73
Cdd:PRK15439 93 QE-PLLFPNLSVK---ENILFGLPKRQASMQKMKQLLAALGCQLDLDSSagslevadRQIVeILRGLMRDSRILILDEPT 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958644180 74 SGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAIMVQGTL 122
Cdd:PRK15439 169 ASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-117 |
6.95e-03 |
|
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: 39.66 E-value: 6.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644180 45 SLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRSTWDVVQTY-KQNRTILLTTHYMDEADMLGDRIAIM 117
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
863-937 |
7.24e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 863 SLELEPHANSLISTYSEGNKRRLSTAIAMM-------GKPSVIFLDEPSTGMDPRARRLLWDAVIKIRESGKAIIITSHS 935
Cdd:COG3593 149 SLRIEDGKELPLDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHS 228
|
..
gi 1958644180 936 ME 937
Cdd:COG3593 229 PH 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
776-908 |
8.99e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 776 LLGFNGAGKTTTFQILTGEITPT---AGDVFIDGISITKDVLKVRSkiGYCPQFDALLEYLTGWEIMVMYARIWGISERQ 852
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTS--AYISQNDVHVGVMTVKETLDFSARCQGVGTRY 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644180 853 --------------IRPY--VNTYLNSLELEPHANSLISTY-----------------------SEGNKRRLSTAIAMMG 893
Cdd:PLN03140 274 dllselarrekdagIFPEaeVDLFMKATAMEGVKSSLITDYtlkilgldickdtivgdemirgiSGGQKKRVTTGEMIVG 353
|
170
....*....|....*
gi 1958644180 894 KPSVIFLDEPSTGMD 908
Cdd:PLN03140 354 PTKTLFMDEISTGLD 368
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
46-102 |
9.48e-03 |
|
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: 38.38 E-value: 9.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644180 46 LSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPasrRSTWDVVQTYK----QNRTILLTTH 102
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS---QAAYNIVRFLKkladSGQAILCTIH 166
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| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
43-83 |
9.76e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 39.79 E-value: 9.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958644180 43 SKSLSGGMKRKLAIIIALIGGSKVVILDEPTSGMDPASRRS 83
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA 523
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