|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
505-1315 |
3.38e-158 |
|
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: 531.13 E-value: 3.38e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 505 LGTYYNRSCILVPFE--DEGFTTAATGNDSFTEGDFYFGVAFyldddgakgePGLDLSTNK----VHYELRMTRDTLVDE 578
Cdd:TIGR01257 512 LANQYLECLVLDKFEsyDDEVQLTQRALSLLEENRFWAGVVF----------PDMYPWTSSlpphVKYKIRMDIDVVEKT 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 579 DEDGFQTSDLFPQwitLGPDMNSAYYDSGFTVMQALFDSLILMEVSGSDvPPVSYHLKPMPWPSYSDDNFIYVIRSTLPL 658
Cdd:TIGR01257 582 NKIKDRYWDSGPR---ADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAE-PPVGIYLQQMPYPCFVDDSFMIILNRCFPI 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 659 ILIFAFIYSASSITRELVFEKEQRLKEMMKMMGLSTWVHWLAWFTKCFLFLFISVVIIMIIFavgdcsrsataMGAEFAR 738
Cdd:TIGR01257 658 FMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFI-----------MHGRILH 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 739 YSDGGPVFLLFLLFAVNTICLCFMFSTFFSKSNVASAAGAILFFLFYMPYLFISEGLDEMPQSDKAGACLLGPTCVSIGM 818
Cdd:TIGR01257 727 YSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGT 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 819 DILSRWEASGQGLTSSTVNKSPYDGDsaKFSMAAVYGMLFLDSLIYLLVTWYMENVFPGEYGVPRPWYFFADPKYWTG-- 896
Cdd:TIGR01257 807 EYLVRFEEQGLGLQWSNIGNSPLEGD--EFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGge 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 897 -------KADEETP-----SNAPTVPHGTgpRSEFVEDFAGNNAVGIQIEGLRKVFYPQtggAKVALEHLDLNMYRDQIT 964
Cdd:TIGR01257 885 gcstreeRALEKTEplteeMEDPEHPEGI--NDSFFERELPGLVPGVCVKNLVKIFEPS---GRPAVDRLNITFYENQIT 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 965 ALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAE 1044
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQ 1039
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1045 AEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHF 1124
Cdd:TIGR01257 1040 LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHH 1119
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1125 MEEADILGDRIAILADGELRTVGSSMFLKNTFGVGYHMTVVK-----------------------GSNC----------- 1170
Cdd:TIGR01257 1120 MDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRkmkniqsqrggcegtcsctskgfSTRCparvdeitpeq 1199
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1171 ----DVVGLLNLVQRYAPEAQMTSNVGSELTVVVP-KSASSR-FPDMFAELETAQRKLDIASFGMGVTTMEEVFLKVAE- 1243
Cdd:TIGR01257 1200 vldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPnKNFKQRaYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEd 1279
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1244 --GRHLQSESEQKEAEHSALIMP-----------------------------------ETRQSRVETGMALRLHQFRAML 1286
Cdd:TIGR01257 1280 adSGSLFAGGAQQKRENANLRHPcsgptekagqtpqashtcspgqpaahpegqpppepEDPGVPLNTGARLILQHVQALL 1359
|
890 900
....*....|....*....|....*....
gi 167517209 1287 TKRFVYSLRNKNAIITQILLPLTFTFIAL 1315
Cdd:TIGR01257 1360 VKRFQHTIRSHKDFLAQIVLPATFVFLAL 1388
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
931-1153 |
7.45e-99 |
|
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: 315.98 E-value: 7.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:cd03263 1 LQIRNLTKTY---KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSSMFLK 1153
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
931-1148 |
1.50e-72 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 241.89 E-value: 1.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHK-QDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
931-1153 |
1.41e-55 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 192.58 E-value: 1.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:cd03265 1 IEVENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1091 DEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSSMFLK 1153
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
931-1148 |
3.73e-54 |
|
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: 189.68 E-value: 3.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:COG4555 2 IEVENLSKKY-----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHK-QDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
931-1143 |
1.24e-53 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 185.29 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:cd03230 1 IEVRNLSKRY-----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIvfysrlkglsvaeaeaevpvyikdidlenkadarvnSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHKQD-RTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
931-1141 |
7.68e-49 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 176.53 E-value: 7.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:PRK13537 8 IDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADG 1141
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
652-1243 |
1.45e-46 |
|
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: 184.83 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 652 IRSTLPLILIFAFIYSASSITRELVFEKEQRLKEMMKMMGLSTWVHWLAWFTKCFLFLFISVVIIMIIFaVGDCSRSAT- 730
Cdd:TIGR01257 1678 VDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIF-IGFQKKAYTs 1756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 731 -----AMGAEFARYSDG-----GPVFLLF--------------LLFAVNTICLCFMFSTFFSKSNVASAAGAILFFLFYM 786
Cdd:TIGR01257 1757 penlpALVALLMLYGWAvipmmYPASFLFdvpstayvalscanLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVF 1836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 787 PYLFISEGLDEMPQSDKAgacllgptcvsigMDILSRWeasGQGLTSStvnksPYDGDSAKFSMAAvygmLFLDSLIYLL 866
Cdd:TIGR01257 1837 PHFCLGRGLIDLALSQAV-------------TDVYAQF---GEEHSAN-----PFQWDLIGKNLVA----MAVEGVVYFL 1891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 867 VTWYMENVFpgeygvprpwyFFADpkyWTGKadeetPSNAPTVPHGTGPRSEFVEDFAGNNAVGI-QIEGLRKVFypqTG 945
Cdd:TIGR01257 1892 LTLLIQHHF-----------FLSR---WIAE-----PAKEPIFDEDDDVAEERQRIISGGNKTDIlRLNELTKVY---SG 1949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGICPQFDTLFPTLTV 1025
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTG 2029
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1026 SEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHT 1105
Cdd:TIGR01257 2030 REHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1106 WDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSSMFLKNTFGVGYHMTV-VKGSNCDVVGLLNLVQRY- 1182
Cdd:TIGR01257 2110 WNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKDDLLPDLNPVEQFf 2189
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1183 ---APEAQMTSNVGSELTVVVPKSASSRfpdMFAELETAQRKLDIASFGMGVTTMEEVFLKVAE 1243
Cdd:TIGR01257 2190 qgnFPGSVQRERHYNMLQFQVSSSSLAR---IFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAK 2250
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1246 |
5.57e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 167.98 E-value: 5.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDidgVRDSL 1010
Cdd:COG4152 2 LELKGLTKRF-----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:COG4152 74 GYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHK-QDRTIILTTHFMEEADILGDRIAILADGELRTVGSSMFLKNTFgvGYHMTVVKGSN 1169
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQF--GRNTLRLEADG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1170 cDVVGLLNLvqryaPEAQMTSNVGSELTVVVPKSASSRfpdmfAELETAQRKLDIASFGMGVTTMEEVFLKVAEGRH 1246
Cdd:COG4152 232 -DAGWLRAL-----PGVTVVEEDGDGAELKLEDGADAQ-----ELLRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
929-1141 |
7.46e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 169.24 E-value: 7.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 929 VGIQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRD 1008
Cdd:PRK13536 40 VAIDLAGVSKSY-----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFV 1088
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1089 ALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADG 1141
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
931-1147 |
2.39e-45 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 163.13 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMyRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:cd03264 1 LQLENLTKRY-----GKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1091 DEPTSGMDPFKR---RHtwdMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:cd03264 155 DEPTAGLDPEERirfRN---LLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
931-1147 |
7.31e-44 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 158.60 E-value: 7.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIdgvRDSL 1010
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA---RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHK-QDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
931-1148 |
1.22e-41 |
|
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: 152.87 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkVFYPqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDS 1009
Cdd:COG1122 1 IELENLS-FSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LGICPQF--DTLFpTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRR--AVSCALALcgGS 1085
Cdd:COG1122 77 VGLVFQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQrvAIAGVLAM--EP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1086 TFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
931-1147 |
3.90e-41 |
|
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: 151.37 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAkVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:cd03266 2 ITADALTKRFRDVKKTV-QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHK-QDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
931-1138 |
6.39e-41 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 150.70 E-value: 6.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVfYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGhninDDIDGVRDSL 1010
Cdd:cd03293 1 LEVRNVSKT-YGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAIL 1138
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
951-1095 |
1.87e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.86 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN-DDIDGVRDSLGICPQFDTLFPTLTVSEHI 1029
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1030 VFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARV----NSLSGGQRRAVSCALALCGGSTFVALDEPTS 1095
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
932-1142 |
3.37e-38 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 142.61 E-value: 3.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 932 QIEGLRkVFYPqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSL 1010
Cdd:cd03225 1 ELKNLS-FSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQF-DTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVA 1089
Cdd:cd03225 78 GLVFQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1090 LDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGE 1142
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
931-1143 |
2.05e-37 |
|
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: 140.32 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVfYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDG----- 1005
Cdd:cd03255 1 IELKNLSKT-YGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 VRDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGS 1085
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1086 TFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADiLGDRIAILADGEL 1143
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLreLNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
931-1147 |
2.71e-37 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 139.96 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDsL 1010
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:cd03259 155 DEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
931-1144 |
6.09e-37 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 138.89 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRdSL 1010
Cdd:cd03268 1 LKTNDLTKTY-----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSvaeaEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKH-KQDRTIILTTHFMEEADILGDRIAILADGELR 1144
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
931-1148 |
2.51e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 2.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGhninDDIDGV---- 1006
Cdd:COG3842 6 LELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLppek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDsLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVscALA------ 1080
Cdd:COG3842 77 RN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRV--ALAralape 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1081 ----LcggstfvaLDEPTSGMDPFKRRHTWDmLLKHKQDR---TIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG3842 154 prvlL--------LDEPLSALDAKLREEMRE-ELRRLQRElgiTFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
931-1140 |
5.17e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.07 E-value: 5.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:COG4133 3 LEAENLSCRR-----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPvyIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEA--LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHKQD-RTIILTTHfmEEADILGDRIAILAD 1140
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARgGAVLLTTH--QPLELAAARVLDLGD 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
931-1148 |
9.95e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 136.66 E-value: 9.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdIDGV--RD 1008
Cdd:cd03295 1 IEFENVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPVelRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENK--ADARVNSLSGGQRRAVSCALALCGGST 1086
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1087 FVALDEPTSGMDPFKRRHTWDMLLKHKQD--RTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
931-1148 |
1.25e-33 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 130.48 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN----DDIDGV 1006
Cdd:COG1127 6 IEVRNLTKSF-----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHIVFYSR-LKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGS 1085
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1086 TFVALDEPTSGMDPFKRRHTWDMLLKHKQDR--TIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
932-1142 |
1.74e-33 |
|
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: 126.98 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 932 QIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSL 1010
Cdd:cd00267 1 EIENLSFRY-----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQfdtlfptltvsehivfysrlkglsvaeaeaevpvyikdidlenkadarvnsLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKH-KQDRTIILTTHFMEEADILGDRIAILADGE 1142
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
931-1147 |
3.19e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 130.07 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTG-------------------GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGT 991
Cdd:cd03294 1 IKIKGLYKIFGKNPQkafkllakgkskeeilkktGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 992 AKVNGHNIN----DDIDGVR-DSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNS 1066
Cdd:cd03294 81 VLIDGQDIAamsrKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1067 LSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAILADGELR 1144
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
...
gi 167517209 1145 TVG 1147
Cdd:cd03294 241 QVG 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
931-1148 |
3.50e-33 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 128.89 E-value: 3.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdIDGVRDSL 1010
Cdd:cd03300 1 IELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-LPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1091 DEPTSGMDpFKRRHTWDMLLKHKQDR---TIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:cd03300 155 DEPLGALD-LKLRKDMQLELKRLQKElgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
931-1143 |
1.18e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 127.08 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypQTGGAKV-ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI----NDDIDG 1005
Cdd:COG1136 5 LELRNLTKSY--GTGEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 VR-DSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGG 1084
Cdd:COG1136 83 LRrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1085 STFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADIlGDRIAILADGEL 1143
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLreLNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
932-1143 |
3.31e-32 |
|
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: 126.69 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 932 QIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHnindDIDGVRDS-- 1009
Cdd:COG0411 6 EVRGLTKRF-----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR----DITGLPPHri 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 --LGIC-----PQfdtLFPTLTVSEHI-----------VFYSRLKGLSVAEAEAEVPVYIKDI----DLENKADARVNSL 1067
Cdd:COG0411 77 arLGIArtfqnPR---LFPELTVLENVlvaaharlgrgLLAALLRLPRARREEREARERAEELlervGLADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1068 SGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMeeaDI---LGDRIAILADGE 1142
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIrrLRDERGITILLIEHDM---DLvmgLADRIVVLDFGR 230
|
.
gi 167517209 1143 L 1143
Cdd:COG0411 231 V 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
931-1143 |
1.36e-31 |
|
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: 124.23 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFyPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI----NDDIDGV 1006
Cdd:cd03258 2 IELKNVSKVF-GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGST 1086
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1087 FVALDEPTSGMDPFKRRHTWDMLLKHKQDR--TIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
931-1143 |
2.11e-31 |
|
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: 123.70 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHnindDIDGV---- 1006
Cdd:cd03219 1 LEVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE----DITGLpphe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDT--LFPTLTV------------SEHIVFYSRLKGLSVAEAEAEvpVYIKDIDLENKADARVNSLSGGQR 1072
Cdd:cd03219 72 IARLGIGRTFQIprLFPELTVlenvmvaaqartGSGLLLARARREEREARERAE--ELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1073 RAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMeeaDI---LGDRIAILADGEL 1143
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDM---DVvmsLADRVTVLDQGRV 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
931-1149 |
3.74e-31 |
|
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: 122.67 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYP-----PTAGTAKVNGHNINDDIDG 1005
Cdd:cd03260 1 IELRDLNVYY-----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 V---RDSLGICPQFDTLFPtLTVSEHIVFYSRLKG-LSVAEAEAEVPVYIKDIDLENKADARVN--SLSGGQRRAVSCAL 1079
Cdd:cd03260 76 VlelRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1080 ALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
894-1143 |
3.76e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.02 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 894 WTGKADE--ETPSNAPTVPHGTGPRSEFVEDFAGNNAVgIQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNG 971
Cdd:COG1123 223 EDGPPEEilAAPQALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESG 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 972 AGKTTTISMLVGMYPPTAGTAKVNGHNIND----DIDGVRDSLGICPQ--FDTLFPTLTVSEHIVF-YSRLKGLSVAEAE 1044
Cdd:COG1123 302 SGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEpLRLHGLLSRAERR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1045 AEVPVYIKDIDL-ENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDR--TIILT 1121
Cdd:COG1123 382 ERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFI 461
|
250 260
....*....|....*....|..
gi 167517209 1122 THFMEEADILGDRIAILADGEL 1143
Cdd:COG1123 462 SHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
941-1142 |
7.73e-31 |
|
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: 119.80 E-value: 7.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 941 YPqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTL 1019
Cdd:cd03228 10 YP--GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1020 FPTltvsehivfysrlkglSVAEaeaevpvyikdidlenkadarvNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDP 1099
Cdd:cd03228 88 FSG----------------TIRE----------------------NILSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 167517209 1100 FKRRHTWDMLLKHKQDRTIILTTHFMEEADiLGDRIAILADGE 1142
Cdd:cd03228 130 ETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
939-1146 |
1.04e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 122.66 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 939 VFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHnindDIDGVRDSLGICPQFDT 1018
Cdd:COG4525 11 VRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV----PVTGPGADRGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1019 LFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:COG4525 87 LLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 167517209 1099 PFKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAILADGELRTV 1146
Cdd:COG4525 167 ALTREQMQELLLDvwQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIV 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
931-1157 |
1.82e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDidgvRDSL 1010
Cdd:COG1121 7 IELENLT-VSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQ---FDTLFPtLTVSEhIV---FYSR---LKGLS------VAEAeaevpvyIKDIDLENKADARVNSLSGGQRRAV 1075
Cdd:COG1121 78 GYVPQraeVDWDFP-ITVRD-VVlmgRYGRrglFRRPSradreaVDEA-------LERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1076 SCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAIL-----ADGELRTVGSS 1149
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLnrglvAHGPPEEVLTP 228
|
....*...
gi 167517209 1150 MFLKNTFG 1157
Cdd:COG1121 229 ENLSRAYG 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
931-1148 |
5.17e-30 |
|
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: 120.15 E-value: 5.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNInDDIDgVRD-- 1008
Cdd:COG1120 2 LEAENLS-VGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLS-RREla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 -SLGICPQFDTLFPTLTVSEhIVFYSR------LKGLSvAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALAL 1081
Cdd:COG1120 75 rRIAYVPQEPPAPFGLTVRE-LVALGRyphlglFGRPS-AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1082 CGGSTFVALDEPTSGMDPfkrRHTWDML-----LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDL---AHQLEVLellrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
931-1148 |
5.34e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.56 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkVFYPqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTA---GTAKVNGHNINDDIDGVR 1007
Cdd:COG1123 5 LEVRDLS-VRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1008 -DSLGICPQ-FDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGS 1085
Cdd:COG1123 82 gRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1086 TFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
931-1148 |
6.18e-30 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 120.61 E-value: 6.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLrkVF-YPqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDD--IDGVR 1007
Cdd:TIGR04520 1 IEVENV--SFsYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEenLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1008 DSLGICPQF-DTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGG--QRRAVSCALAL--- 1081
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGqkQRVAIAGVLAMrpd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1082 CggstfVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEAdILGDRIAILADGELRTVGS 1148
Cdd:TIGR04520 157 I-----IILDEATSMLDPKGRKEVLETIrkLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGT 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
931-1143 |
7.74e-30 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 118.40 E-value: 7.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND---DIDGVR 1007
Cdd:cd03262 1 IEIKNLHKSF-----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1008 DSLGICPQFDTLFPTLTVSEHIVFYSR-LKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGST 1086
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1087 FVALDEPTSGMDPFKRRHTWDMLLKHKQD-RTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
931-1142 |
4.28e-29 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 114.98 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGV---R 1007
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1008 DSLGICPQFDTLFPTLTVSEHIVFysrlkglsvaeaeaevpvyikdidlenkadarvnSLSGGQRRAVSCALALCGGSTF 1087
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1088 VALDEPTSGMDPFKRRhTWDMLLKHKQDR---TIILTTHFMEEADILGDRIAILADGE 1142
Cdd:cd03229 122 LLLDEPTSALDPITRR-EVRALLKSLQAQlgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
931-1147 |
6.07e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 115.81 E-value: 6.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDsL 1010
Cdd:cd03301 1 VELENVTKRF-----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1091 DEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
931-1148 |
1.13e-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: 116.06 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI----NDDIDGV 1006
Cdd:cd03261 1 IELRGLTKSF-----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHIVFYSRLKG-LSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGS 1085
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1086 TFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIrsLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
931-1149 |
4.23e-28 |
|
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: 114.18 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:cd03218 1 LRAENLSKRY-----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GIC--PQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFV 1088
Cdd:cd03218 76 GIGylPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1089 ALDEPTSGMDP-----FKRrhtwdmLLKHKQDRTI-ILTT-HFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:cd03218 156 LLDEPFAGVDPiavqdIQK------IIKILKDRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
946-1143 |
8.27e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 111.37 E-value: 8.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNInddidgvrdslgicpqfdtlfptltv 1025
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1026 sehivfySRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHT 1105
Cdd:cd03214 64 -------ASLSPKELARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 167517209 1106 WDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:cd03214 137 LELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
931-1143 |
9.93e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 112.98 E-value: 9.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFyPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:cd03257 2 LEVKNLSVSF-PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 G----ICPQ--FDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENK---ADARVNSLSGGQRRAVSCALAL 1081
Cdd:cd03257 81 RkeiqMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1082 CGGSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
946-1139 |
1.42e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.86 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDidgvRDSLGICPQ---FDTLFPt 1022
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQrrsIDRDFP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 LTVSE--------HIVFYSRLKglsvAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPT 1094
Cdd:cd03235 85 ISVRDvvlmglygHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 167517209 1095 SGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILA 1139
Cdd:cd03235 161 AGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
931-1148 |
5.20e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 5.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIndDIDGVRDS- 1009
Cdd:COG1129 5 LEMRGISKSF----GGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV--RFRSPRDAq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 -LGIC--PQFDTLFPTLTVSEHIVF---YSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCG 1083
Cdd:COG1129 78 aAGIAiiHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1084 GSTFVALDEPTSGMDP------FK--RRhtwdmlLKhKQDRTIILTTHFMEEADILGDRIAILADGelRTVGS 1148
Cdd:COG1129 158 DARVLILDEPTASLTEreverlFRiiRR------LK-AQGVAIIYISHRLDEVFEIADRVTVLRDG--RLVGT 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
931-1149 |
6.37e-27 |
|
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: 110.83 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:TIGR04406 2 LVAENLIKSY-----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GI--CPQFDTLFPTLTVSEHI-VFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTF 1087
Cdd:TIGR04406 77 GIgyLPQEASIFRKLTVEENImAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1088 VALDEPTSGMDPF-----KRrhtwdmLLKHKQDRTI--ILTTHFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:TIGR04406 157 ILLDEPFAGVDPIavgdiKK------IIKHLKERGIgvLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
926-1148 |
7.19e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.62 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 926 NNAVGIQIEglrKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDD-ID 1004
Cdd:PRK13632 3 NKSVMIKVE---NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1005 GVRDSLGICPQF-DTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCG 1083
Cdd:PRK13632 80 EIRKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1084 GSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEAdILGDRIAILADGELRTVGS 1148
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
933-1143 |
7.34e-27 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.80 E-value: 7.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 933 IEgLRKVfYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND----DIDGVRD 1008
Cdd:cd03292 1 IE-FINV-TKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFV 1088
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1089 ALDEPTSGMDPfkrRHTWDM--LLK--HKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:cd03292 159 IADEPTGNLDP---DTTWEImnLLKkiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
931-1148 |
1.14e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 107.51 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINddIDGVRDS- 1009
Cdd:cd03216 1 LELRGITKRF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--FASPRDAr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 -LGIcpqfdtlfptltvsehivfysrlkglsvaeaeaevpvyikdidlenkadARVNSLSGGQRRAVSCALALCGGSTFV 1088
Cdd:cd03216 74 rAGI-------------------------------------------------AMVYQLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1089 ALDEPTSGMDPfkrrHTWDMLLKH-----KQDRTIILTTHFMEEADILGDRIAILADGelRTVGS 1148
Cdd:cd03216 105 ILDEPTAALTP----AEVERLFKVirrlrAQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
926-1148 |
2.62e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.12 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 926 NNAVGIQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIndDIDG 1005
Cdd:COG3845 1 MMPPALELRGITKRF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV--RIRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 VRD--SLGI--CPQ-FdTLFPTLTVSEHIVFY---SRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSC 1077
Cdd:COG3845 74 PRDaiALGIgmVHQhF-MLVPNLTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1078 ALALCGGSTFVALDEPTSGMDP------FK--RRhtwdmlLKhKQDRTIILTTHFMEEADILGDRIAILADGelRTVGS 1148
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPqeadelFEilRR------LA-AEGKSIIFITHKLREVMAIADRVTVLRRG--KVVGT 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
931-1156 |
4.29e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 111.70 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDsL 1010
Cdd:COG3839 4 LELENVSKSY-----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVpvyiKDI----DLENKADARVNSLSGGQRRAVSCALALcggst 1086
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRV----REAaellGLEDLLDRKPKQLSGGQRQRVALGRAL----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1087 fVA------LDEPTSGMDPFKRrhtWDM--LLK--HKQ-DRTIILTTHFMEEADILGDRIAILADGELRTVGSSMFL--- 1152
Cdd:COG3839 149 -VRepkvflLDEPLSNLDAKLR---VEMraEIKrlHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELydr 224
|
....*
gi 167517209 1153 -KNTF 1156
Cdd:COG3839 225 pANLF 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
930-1148 |
4.57e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.39 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 930 GIQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDgVRDS 1009
Cdd:COG1118 2 SIEVRNISKRF-----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP-PRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 -LGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALcggstfv 1088
Cdd:COG1118 76 rVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1089 A-------LDEPTSGMDPFKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG1118 149 AvepevllLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
931-1152 |
6.14e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 108.71 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLrKVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTT---TISMLVGMYP--PTAGTAKVNGHNI---NDD 1002
Cdd:PRK14239 6 LQVSDL-SVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1003 IDGVRDSLGICPQFDTLFPtLTVSEHIVFYSRLKGLSVAEA-EAEVPVYIKDIDLENKADARVN----SLSGGQRRAVSC 1077
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRLHdsalGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1078 ALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS--SMFL 1152
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDtkQMFM 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
915-1136 |
8.49e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.61 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 915 PRSEFVEDfagnnAVGIQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKV 994
Cdd:NF033858 256 PRPADDDD-----EPAIEARGLTMRF-----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 995 NGHNIN-DDIDgVRDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRR 1073
Cdd:NF033858 326 FGQPVDaGDIA-TRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQ 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1074 AVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDR-TIILTTHFMEEADiLGDRIA 1136
Cdd:NF033858 405 RLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIElSREDGvTIFISTHFMNEAE-RCDRIS 468
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
906-1162 |
1.15e-25 |
|
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: 113.71 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 906 APTVPHGTGPRsefvedfAGNNAVGIQIEGLRkvF-YPqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGM 984
Cdd:COG4987 316 PPAVTEPAEPA-------PAPGGPSLELEDVS--FrYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 985 YPPTAGTAKVNGHNIND-DIDGVRDSLGICPQ----FDTlfptlTVSEHIvfysRLKGLSVAEAEAEVP---VYIKDI-- 1054
Cdd:COG4987 385 LDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQrphlFDT-----TLRENL----RLARPDATDEELWAAlerVGLGDWla 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1055 DLENKADARV----NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADi 1130
Cdd:COG4987 456 ALPDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE- 534
|
250 260 270
....*....|....*....|....*....|..
gi 167517209 1131 LGDRIAILADGELRTVGSSMFLKNTFGVGYHM 1162
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
930-1148 |
1.95e-25 |
|
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: 106.65 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 930 GIQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdiDGVRD- 1008
Cdd:cd03296 2 SIEVRNVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--VPVQEr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKD----IDLENKADARVNSLSGGQRRAVSCALALCGG 1084
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHEllklVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1085 STFVALDEPTSGMDPFKRRH--TWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKElrRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
931-1142 |
2.64e-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: 105.59 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN----DDIdgV 1006
Cdd:cd03224 1 LEVENLN-AGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglppHER--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHI-VFYSRLKGLSVAEAEAEV----PVyikdidLENKADARVNSLSGGQRRAVSCALAL 1081
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLlLGAYARRRAKRKARLERVyelfPR------LKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1082 CGGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGE 1142
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
951-1147 |
2.94e-25 |
|
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: 105.88 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDsLGICPQFDTLFPTLTVSEHIV 1030
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-ISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 FYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDML- 1109
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELk 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 167517209 1110 -LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:cd03299 174 kIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
962-1143 |
4.76e-25 |
|
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: 105.05 E-value: 4.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMYPP---TAGTAKVNGHNINddIDGVRDSLGICPQFDTLFPTLTVSEHIVFYSRLKG- 1037
Cdd:cd03234 34 QVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK--PDQFQKCVAYVRQDDILLPGLTVRETLTYTAILRLp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1038 --LSVAEAEAEVPVY-IKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKH-K 1113
Cdd:cd03234 112 rkSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLaR 191
|
170 180 190
....*....|....*....|....*....|..
gi 167517209 1114 QDRTIILTTHfMEEADI--LGDRIAILADGEL 1143
Cdd:cd03234 192 RNRIVILTIH-QPRSDLfrLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
931-1148 |
5.12e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.67 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND---DIDGVR 1007
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1008 DSLGICPQFD--TLFPTlTVSEHIVFYSRLKGLSVAEAEAEV--PVYIKDIDLENKADARVNSLSGGQRRAVSCALALCG 1083
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEE-TIEKDIAFGPINLGLSEEEIENRVkrAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1084 GSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
931-1164 |
6.72e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.64 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI-----NDDIDG 1005
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 VRDSLGICPQF--DTLFPTlTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVN-SLSGGQRRAVSCALALC 1082
Cdd:PRK13634 83 LRKKVGIVFQFpeHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1083 GGSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS--SMFLKNT--- 1155
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPDele 241
|
250
....*....|
gi 167517209 1156 -FGVGYHMTV 1164
Cdd:PRK13634 242 aIGLDLPETV 251
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
931-1143 |
8.56e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 104.72 E-value: 8.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVF--YPQTGG--------------AKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKV 994
Cdd:cd03267 1 IEVSNLSKSYrvYSKEPGligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 995 NGHNINDDIDGVRDSLG-ICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRR 1073
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1074 AVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDR--TIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1142 |
1.07e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.17 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVR--- 1007
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRaky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1008 ------D-SLGICpqfdtlfPTLTVSEHIVF-YSRLK--GLSVAEAEAEVPVYIK-----DIDLENKADARVNSLSGGQR 1072
Cdd:COG1101 82 igrvfqDpMMGTA-------PSMTIEENLALaYRRGKrrGLRRGLTKKRRELFREllatlGLGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1073 RAVSCALALCGGSTFVALDEPTSGMDPfkrrHTWDMLLK------HKQDRTIILTTHFMEEADILGDRIAILADGE 1142
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDP----KTAALVLEltekivEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
904-1148 |
1.12e-24 |
|
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: 110.62 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 904 SNAPTVPHGTGPrsefvedFAGNNAVGIQIEGLRkVFYPqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVG 983
Cdd:COG4988 317 APEPAAPAGTAP-------LPAAGPPSIELEDVS-FSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 984 MYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFPTlTVSEHIVFYSR-------LKGLSVAEAEAEVPvyikdiD 1055
Cdd:COG4988 386 FLPPYSGSILINGVDLSDlDPASWRRQIAWVPQNPYLFAG-TIRENLRLGRPdasdeelEAALEAAGLDEFVA------A 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1056 LENKADARVNS----LSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTH---FMEEA 1128
Cdd:COG4988 459 LPDGLDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHrlaLLAQA 538
|
250 260
....*....|....*....|
gi 167517209 1129 dilgDRIAILADGELRTVGS 1148
Cdd:COG4988 539 ----DRILVLDDGRIVEQGT 554
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
931-1142 |
1.22e-24 |
|
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: 104.57 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND----DIDGV 1006
Cdd:cd03256 1 IEVENLSKTY----PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHIV-----FYSRLKGLS--VAEAEAEVPVYI-KDIDLENKADARVNSLSGGQRRAVSCA 1078
Cdd:cd03256 77 RRQIGMIFQQFNLIERLSVLENVLsgrlgRRSTWRSLFglFPKEEKQRALAAlERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1079 LALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAILADGE 1142
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
931-1143 |
1.40e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.59 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN----DDIDGV 1006
Cdd:COG2884 2 IRFENVSKRY----PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQfDT-LFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGS 1085
Cdd:COG2884 78 RRRIGVVFQ-DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1086 TFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
931-1148 |
1.77e-24 |
|
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: 111.08 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkvF-YPqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRD 1008
Cdd:COG2274 474 IELENVS--FrYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SLGICPQFDTLFPTlTVSEHIVFYSR-------LKGLSVAEAEAEVpvyikdIDLENKADARV----NSLSGGQRRAVSC 1077
Cdd:COG2274 550 QIGVVLQDVFLFSG-TIRENITLGDPdatdeeiIEAARLAGLHDFI------EALPMGYDTVVgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1078 ALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTH---FMEEAdilgDRIAILADGELRTVGS 1148
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----DRIIVLDKGRIVEDGT 692
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
930-1149 |
2.79e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.19 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 930 GIQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI-NDDIDgVRD 1008
Cdd:COG1137 3 TLEAENLVKSY-----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDItHLPMH-KRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SLGI--CPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGST 1086
Cdd:COG1137 77 RLGIgyLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1087 FVALDEPTSGMDP-----FKRrhtwdmLLKHKQDRTI-ILTT-HFMEEadILG--DRIAILADGELRTVGSS 1149
Cdd:COG1137 157 FILLDEPFAGVDPiavadIQK------IIRHLKERGIgVLITdHNVRE--TLGicDRAYIISEGKVLAEGTP 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
932-1149 |
3.11e-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: 103.14 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 932 QIEGLRkVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN----DDIdgVR 1007
Cdd:COG0410 5 EVENLH-AGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglppHRI--AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1008 DSLGICPQFDTLFPTLTVSEHIV--FYSRLKGLSVAEAEAEV----PVyikdidLENKADARVNSLSGGQRRAVSCALAL 1081
Cdd:COG0410 78 LGIGYVPEGRRIFPSLTVEENLLlgAYARRDRAEVRADLERVyelfPR------LKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1082 CGGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
931-1148 |
3.16e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.57 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND------DID 1004
Cdd:PRK09452 15 VELRGISKSF-----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaenrHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1005 GVRDSLGicpqfdtLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGG 1084
Cdd:PRK09452 90 TVFQSYA-------LFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1085 STFVALDEPTSGMDpFKRRHTWDMLLKHKQDR---TIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK09452 163 PKVLLLDESLSALD-YKLRKQMQNELKALQRKlgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
943-1143 |
6.83e-24 |
|
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: 101.18 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 943 QTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDgvRDSLGICPQ-FDTLFP 1021
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVMQdVDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1022 TLTVSEHIVFYSRLKGLSVAEAEAevpvYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFK 1101
Cdd:cd03226 86 TDSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 167517209 1102 RRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:cd03226 162 MERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
966-1149 |
7.21e-24 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 104.50 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 966 LLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdIDGVRDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEA 1045
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN-VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1046 EVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDpFKRRHTWDMLLKHKQDR---TIILTT 1122
Cdd:TIGR01187 80 RVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD-KKLRDQMQLELKTIQEQlgiTFVFVT 158
|
170 180
....*....|....*....|....*..
gi 167517209 1123 HFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:TIGR01187 159 HDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
934-1184 |
2.34e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.34 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 934 EGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGV-----RD 1008
Cdd:PRK10070 27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFV 1088
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1089 ALDEPTSGMDPFKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSSMFLKNTFGVGYHMTVVK 1166
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKlqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
250
....*....|....*...
gi 167517209 1167 GSNCDVVGLLNLVQRYAP 1184
Cdd:PRK10070 267 GVDISQVFSAKDIARRTP 284
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
962-1147 |
2.45e-23 |
|
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: 99.68 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGH-----NINDDIDGVRDSLGICPQFDTLFPTLTVSEHIVFysRLK 1036
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAF--GLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1037 GLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDpfkrRHTWDMLLKHKQDR 1116
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD----RALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 167517209 1117 ------TIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:cd03297 178 kknlniPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
962-1143 |
2.75e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 99.16 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVG--MYPPTAGTAKVNGHNIndDIDGVRDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLS 1039
Cdd:cd03213 36 ELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLRGLS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1040 vaeaeaevpvyikdidlenkadarvnslsGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTI 1118
Cdd:cd03213 114 -----------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTI 164
|
170 180
....*....|....*....|....*....
gi 167517209 1119 ILTTH----FMEEadiLGDRIAILADGEL 1143
Cdd:cd03213 165 ICSIHqpssEIFE---LFDKLLLLSQGRV 190
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
931-1143 |
7.18e-23 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 99.29 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND----DIDGV 1006
Cdd:TIGR02315 2 LEVENLSKVY----PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHIV-----FYSRLKGLS--VAEAEAEVPVYIKD-IDLENKADARVNSLSGGQRRAVSCA 1078
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVLhgrlgYKPTWRSLLgrFSEEDKERALSALErVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1079 LALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDR--TIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
950-1148 |
7.35e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI-----NDDIDGVRDSLGICPQF--DTLFPT 1022
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDIKQIRKKVGLVFQFpeSQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 lTVSEHIVFYSRLKGLSVAEAE--AEVPVYIKDIDlENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPF 1100
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEalAREKLALVGIS-ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167517209 1101 KRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK13649 180 GRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
949-1143 |
7.70e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 7.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 949 VALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDG---VRDSLGICPQF--DTLFPTl 1023
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlleVRKTVGIVFQNpdDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1024 TVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRR 1103
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 167517209 1104 HTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:PRK13639 175 QIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
936-1147 |
1.35e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.44 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 936 LRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN-DDIDGVRDSLGICP 1014
Cdd:PRK13648 10 FKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1015 QF-DTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEP 1093
Cdd:PRK13648 90 QNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1094 TSGMDPFKRRHTWDMLLKHKQDR--TIILTTHFMEEAdILGDRIAILADGELRTVG 1147
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
946-1158 |
1.40e-22 |
|
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: 98.62 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAG-TAKVNGHNI-NDDIDGVRDSLGIC-PQFDTLFPT 1022
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLVsPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 LTVSEHIV---FYSRLkGLSV---AEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSG 1096
Cdd:COG1119 94 DETVLDVVlsgFFDSI-GLYReptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1097 MDPFKRRHTWDML--LKHKQDRTIILTTHFMEEAD------ILGDRIAILADGELRTVGSSMFLKNTFGV 1158
Cdd:COG1119 173 LDLGARELLLALLdkLAAEGAPTLVLVTHHVEEIPpgithvLLLKDGRVVAAGPKEEVLTSENLSEAFGL 242
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
932-1143 |
2.23e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 97.60 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 932 QIEGLRkVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGhninDDIDG------ 1005
Cdd:TIGR03410 2 EVSNLN-VYY----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG----EDITKlppher 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 VRDSLGICPQFDTLFPTLTVSEHIvfysrLKGLSV-AEAEAEVPVYIKDI--DLENKADARVNSLSGGQRRAVSCALALC 1082
Cdd:TIGR03410 73 ARAGIAYVPQGREIFPRLTVEENL-----LTGLAAlPRRSRKIPDEIYELfpVLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1083 GGSTFVALDEPTSGMDP--FKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPsiIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
931-1143 |
3.24e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.77 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFyPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND----DIDGV 1006
Cdd:COG1135 2 IELENLSKTF-PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCA--LA---- 1080
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIAraLAnnpk 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1081 --LCggstfvalDEPTSGMDPfkrrHTWDM---LLKHKQDR---TIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:COG1135 161 vlLC--------DEATSALDP----ETTRSildLLKDINRElglTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
931-1169 |
3.75e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAK-----VNGHNINDDIDG 1005
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 VRDSLGICPQF--DTLFPTlTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKA-DARVNSLSGGQRRAVSCALALC 1082
Cdd:PRK13643 82 VRKKVGVVFQFpeSQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1083 GGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGELRTVG--SSMFLKNTFGVG 1159
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtpSDVFQEVDFLKA 240
|
250
....*....|
gi 167517209 1160 YHMTVVKGSN 1169
Cdd:PRK13643 241 HELGVPKATH 250
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
931-1146 |
1.18e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.31 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLrkvfYPQTGGaKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNInddiDGVRDSL 1010
Cdd:PRK11248 2 LQISHL----YADYGG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAILADGELRTV 1146
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
946-1138 |
1.35e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.22 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHninddidgvrDSLGICPQ---FDTLFPt 1022
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQrseVPDSLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 LTVSE--------HIVFYSRLKglsvAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPT 1094
Cdd:NF040873 72 LTVRDlvamgrwaRRGLWRRLT----RDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 167517209 1095 SGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEAdILGDRIAIL 1138
Cdd:NF040873 148 TGLDAESRERIIALLAEeHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
931-1143 |
2.10e-21 |
|
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: 95.26 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVfYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGV-RDS 1009
Cdd:COG1124 2 LEVRNLSVS-YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LGICPQ--FDTLFPTLTVSEHIvfySR-LKGLSVAEAEAEVPVYIKDIDL-ENKADARVNSLSGGQRRAVSCALALCGGS 1085
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRIL---AEpLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1086 TFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLkdLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
952-1147 |
5.08e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 93.00 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 952 EHL----DLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRdSLGICPQFDTLFPTLTVSE 1027
Cdd:TIGR01277 11 EHLpmefDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR-PVSMLFQENNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1028 HIVFYSRlKGLSV-AEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRhtw 1106
Cdd:TIGR01277 90 NIGLGLH-PGLKLnAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE--- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 167517209 1107 DML-----LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:TIGR01277 166 EMLalvkqLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
931-1148 |
5.74e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDS 1009
Cdd:COG4604 2 IEIKNVSKRY-----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LGICPQFDTLFPTLTVSEHIVF----YSrlKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQR-RA-VscALALCG 1083
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFgrfpYS--KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRqRAfI--AMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1084 GSTFVALDEPTSGMDPfkrRHTWDM--LLK---HKQDRTIILTTHfmeeaDI-----LGDRIAILADGELRTVGS 1148
Cdd:COG4604 153 DTDYVLLDEPLNNLDM---KHSVQMmkLLRrlaDELGKTVVIVLH-----DInfascYADHIVAMKDGRVVAQGT 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
931-1146 |
7.27e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.42 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLrkvFYPQTGGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN-DDIDGVRDS 1009
Cdd:PRK13647 5 IEVEDL---HFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LGICPQ--FDTLFpTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTF 1087
Cdd:PRK13647 81 VGLVFQdpDDQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1088 VALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGelRTV 1146
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEG--RVL 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
931-1157 |
7.28e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.54 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVF-----YPQTGGA-----------KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKV 994
Cdd:COG4586 2 IEVENLSKTYrvyekEPGLKGAlkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 995 NGHNI-NDDIDGVRD-SL--GicpQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGG 1070
Cdd:COG4586 82 LGYVPfKRRKEFARRiGVvfG---QRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1071 QRraVSC--ALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDR--TIILTTHFMeeADI--LGDRIAILADGELR 1144
Cdd:COG4586 159 QR--MRCelAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDM--DDIeaLCDRVIVIDHGRII 234
|
250
....*....|...
gi 167517209 1145 TVGSSMFLKNTFG 1157
Cdd:COG4586 235 YDGSLEELKERFG 247
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
928-1129 |
1.55e-20 |
|
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: 97.36 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 928 AVGIQIEGLrKVFYPqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGV 1006
Cdd:TIGR02857 319 ASSLEFSGV-SVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTlTVSEHIVFYsrLKGLSVAE-AEAEVPVYIKDID------LENKADARVNSLSGGQRRAVSCAL 1079
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAG-TIAENIRLA--RPDASDAEiREALERAGLDEFVaalpqgLDTPIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1080 ALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTH---FMEEAD 1129
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
931-1148 |
4.15e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTggakvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINdDIDGVRDSL 1010
Cdd:PRK11607 20 LEIRNLTKSFDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1091 DEPTSGMDPfKRRHTWDMLLKHKQDR---TIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK11607 174 DEPMGALDK-KLRDRMQLEVVDILERvgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
941-1147 |
5.03e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.00 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 941 YPQTggAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDD-IDGVRDSLGICPQF-DT 1018
Cdd:PRK13635 15 YPDA--ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRRQVGMVFQNpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1019 LFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:PRK13635 93 QFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1099 PFKRRHTWDML--LKHKQDRTIILTTHFMEEAdILGDRIAILADGELRTVG 1147
Cdd:PRK13635 173 PRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEG 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
931-1149 |
5.97e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.13 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKVaLEHLDLNMYRDQITALLGHNGAGKTTTISM---LVGMYPP--TAGTAKVNGHNI-NDDID 1004
Cdd:PRK14247 4 IEIRDLKVSF----GQVEV-LDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQDIfKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1005 GVRDSLGICPQFDTLFPTLTVSEHIVFYSRLKGL--SVAEAEAEVPVYIKDIDL----ENKADARVNSLSGGQRRAVSCA 1078
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1079 LALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
936-1144 |
7.00e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.90 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 936 LRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGhninddidGVRDSLGICPQ 1015
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSSLLGLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1016 FDtlfPTLTVSEHIVFYSRLKGLSVAEAEAEVPvYIKDI-DLENKADARVNSLSGGQ--RRAVSCALALcGGSTFVaLDE 1092
Cdd:cd03220 95 FN---PELTGRENIYLNGRLLGLSRKEIDEKID-EIIEFsELGDFIDLPVKTYSSGMkaRLAFAIATAL-EPDILL-IDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1093 PTSGMDPFKRRHTWDMLL-KHKQDRTIILTTHFMEEADILGDRIAILADGELR 1144
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLReLLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
953-1141 |
1.21e-19 |
|
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: 89.09 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 953 HLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdIDGVRDSLGICPQFDTLFPTLTVSEHIVFy 1032
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA-APPADRPVSMLFQENNLFAHLTVEQNVGL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1033 SRLKGLSV-AEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK 1111
Cdd:cd03298 94 GLSPGLKLtAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|..
gi 167517209 1112 HKQDR--TIILTTHFMEEADILGDRIAILADG 1141
Cdd:cd03298 174 LHAETkmTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
951-1150 |
1.23e-19 |
|
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: 89.45 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDgvrDSLgICPQFDTLFPTLTVSEHIV 1030
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRM-VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 FY--SRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDM 1108
Cdd:TIGR01184 77 LAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 167517209 1109 LLKHKQDR--TIILTTHFMEEADILGDRIAILADGELRTVGSSM 1150
Cdd:TIGR01184 157 LMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIL 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
935-1141 |
1.40e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.21 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 935 GLRKVFyPqtgGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINddIDGVRDSLG--- 1011
Cdd:PRK11288 9 GIGKTF-P---GVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAALAagv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1012 -ICPQFDTLFPTLTVSEHIV---FYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTF 1087
Cdd:PRK11288 82 aIIYQELHLVPEMTVAENLYlgqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1088 VALDEPTSGMdpfKRRHTwDMLLK-----HKQDRTIILTTHFMEEADILGDRIAILADG 1141
Cdd:PRK11288 162 IAFDEPTSSL---SAREI-EQLFRvirelRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
931-1143 |
1.47e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.66 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI-----NDDIDG 1005
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 VRDSLGICPQF--DTLFPTlTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDL-ENKADARVNSLSGGQRRAVSCALALC 1082
Cdd:PRK13641 83 LRKKVSLVFQFpeAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1083 GGSTFVALDEPTSGMDPFKRRHTWDMLLKH-KQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
941-1148 |
1.84e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.24 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 941 YPQTggAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAK---VNGHNINDD-IDGVRDSLGICPQF 1016
Cdd:PRK13640 15 YPDS--KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTAKtVWDIREKVGIVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1017 -DTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTS 1095
Cdd:PRK13640 93 pDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1096 GMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADiLGDRIAILADGELRTVGS 1148
Cdd:PRK13640 173 MLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
931-1143 |
3.41e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.02 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVfYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI----NDDIDGV 1006
Cdd:PRK11153 2 IELKNISKV-FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGG--QRRAVSCALA---- 1080
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGqkQRVAIARALAsnpk 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1081 --LCggstfvalDEPTSGMDPFKRRHTWDmLLKHKQDR---TIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:PRK11153 161 vlLC--------DEATSALDPATTRSILE-LLKDINRElglTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
946-1148 |
4.00e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVaLEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNghniNDDI------DGVRDSLGICPQFDTL 1019
Cdd:PRK10895 15 GRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID----DEDIsllplhARARRGIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1020 FPTLTVSEHIVFYSRL-KGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:PRK10895 90 FRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1099 PFKrrhTWDM--LLKHKQDR--TIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK10895 170 PIS---VIDIkrIIEHLRDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
932-1148 |
4.27e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 88.64 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 932 QIEGLRKVFypqtGGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN--DDIDGVRds 1009
Cdd:COG4674 12 YVEDLTVSF----DGFK-ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTglDEHEIAR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LGICPQFD--TLFPTLTVSEHI---------VFYSRLKGLSVAEAE--AEVpvyIKDIDLENKADARVNSLSGGQRR--- 1073
Cdd:COG4674 85 LGIGRKFQkpTVFEELTVFENLelalkgdrgVFASLFARLTAEERDriEEV---LETIGLTDKADRLAGLLSHGQKQwle 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1074 -----AVSCALALcggstfvaLDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG4674 162 igmllAQDPKLLL--------LDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
962-1142 |
6.95e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.50 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRdslgicP-----QFDTLFPTLTVSEHIVF--YSR 1034
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER------PvsmlfQENNLFPHLTVAQNIGLglRPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1035 LKgLSVAEaEAEVPVYIKDIDLENKADARVNSLSGGQR-RAvscALALCggstFV------ALDEPTSGMDPFKRRhtwD 1107
Cdd:COG3840 100 LK-LTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRqRV---ALARC----LVrkrpilLLDEPFSALDPALRQ---E 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 167517209 1108 ML-----LKHKQDRTIILTTHFMEEADILGDRIAILADGE 1142
Cdd:COG3840 168 MLdlvdeLCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
931-1147 |
9.12e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.59 E-value: 9.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTT---TISMLVGMYPPT--AGTAKVNGHNI-NDDID 1004
Cdd:PRK14267 5 IETVNLR-VYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLELNEEArvEGEVRLFGRNIySPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1005 G--VRDSLGICPQFDTLFPTLTVSEHIVFYSRLKGL--SVAEAEAEVPVYIKDIDLENKADARVN----SLSGGQRRAVS 1076
Cdd:PRK14267 80 PieVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1077 CALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
946-1123 |
9.55e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 9.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIndDIDGVRDS---LGicPQfDTLFPT 1022
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEAchyLG--HR-NAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 LTVSEHIVFYSRLKG---LSVAEAeaevpvyIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDp 1099
Cdd:PRK13539 88 LTVAENLEFWAAFLGgeeLDIAAA-------LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD- 159
|
170 180
....*....|....*....|....*....
gi 167517209 1100 fkrRHTWDMLLK----H-KQDRTIILTTH 1123
Cdd:PRK13539 160 ---AAAVALFAEliraHlAQGGIVIAATH 185
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
946-1157 |
1.41e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.01 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDslgICPQFDT--LFPTL 1023
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---ICMVFQSyaLFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1024 TVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRR 1103
Cdd:PRK11432 94 SLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1104 HTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS---------SMFLKNTFG 1157
Cdd:PRK11432 174 SMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFMASFMG 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
931-1195 |
1.55e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTggakvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN--DDIDGVRD 1008
Cdd:PRK09700 6 ISMAGIGKSFGPVH-----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SLGICPQFDTLFPTLTVSEHIvFYSRLK-----GLSV---AEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALA 1080
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENL-YIGRHLtkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1081 LCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQD-RTIILTTHFMEEADILGDRIAILADGElrTVGSSMflkntfgvg 1159
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGS--SVCSGM--------- 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 167517209 1160 yhmtVVKGSNCDVVGLL---NLVQRYAPEAQMTSNVGSE 1195
Cdd:PRK09700 229 ----VSDVSNDDIVRLMvgrELQNRFNAMKENVSNLAHE 263
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
948-1143 |
1.72e-18 |
|
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: 86.13 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFPTlTVS 1026
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1027 EHIvfysRLKGLSVAEAEAEVPVYIKDID-----LENKADARVN----SLSGGQRRAVSCALALCGGSTFVALDEPTSGM 1097
Cdd:cd03254 95 ENI----RLGRPNATDEEVIEAAKEAGAHdfimkLPNGYDTVLGenggNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167517209 1098 DPFKRRHTWDMLLKHKQDRTIILTTHFM---EEAdilgDRIAILADGEL 1143
Cdd:cd03254 171 DTETEKLIQEALEKLMKGRTSIIIAHRLstiKNA----DKILVLDDGKI 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
931-1138 |
1.76e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 88.19 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPP---TAGTAKVNGHNIND----DI 1003
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVK-AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1004 DGVRDS-LGICPQ--FDTLFPTLTVSEHIV-FYSRLKGLSVAEAEAEVP-----VYIKDidlenkADARVNS----LSGG 1070
Cdd:COG0444 81 RKIRGReIQMIFQdpMTSLNPVMTVGDQIAePLRIHGGLSKAEARERAIellerVGLPD------PERRLDRypheLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1071 QRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAIL 1138
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
599-870 |
2.41e-18 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 88.22 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 599 MNSAYYDSGFTVMQALfDSLILMEVSGSDVPPVSYHLKPMPWPSYSDDNFIY---VIRSTLPLILIFAFIYSASSITREL 675
Cdd:pfam12698 105 INSSNLLVSKLILNAL-QSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPqsgYAYYLVGLILMIIILIGAAIIAVSI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 676 VFEKEQRLKEMMKMMGLSTWVHWLAWFTkCFLFLFISVVIIMIIFAVGdcsrsataMGAEFARYsdgGPVFLLFLLFAVN 755
Cdd:pfam12698 184 VEEKESRIKERLLVSGVSPLQYWLGKIL-GDFLVGLLQLLIILLLLFG--------IGIPFGNL---GLLLLLFLLYGLA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 756 TICLCFMFSTFFSKSNVASAAGAILFFLFyMPYLFISEGLDEMPQSDKAGACLLGPTCVSIGM-DILSrweasgqgltss 834
Cdd:pfam12698 252 YIALGYLLGSLFKNSEDAQSIIGIVILLL-SGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLlRLIY------------ 318
|
250 260 270
....*....|....*....|....*....|....*.
gi 167517209 835 tvnkspydGDSAkFSMAAVYGMLFLDSLIYLLVTWY 870
Cdd:pfam12698 319 --------GDSL-WEIAPSLIILLLFAVVLLLLALL 345
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
965-1141 |
2.96e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 85.33 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 965 ALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFPTlTVSEHIVFYSR-------LK 1036
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TLRDNITLGAPladderiLR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1037 GLSVAEAEAEVPVYIKDIDLEnkADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDR 1116
Cdd:cd03245 113 AAELAGVTDFVNKHPNGLDLQ--IGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK 190
|
170 180 190
....*....|....*....|....*....|
gi 167517209 1117 TIILTTH---FMEEAD--ILGDRIAILADG 1141
Cdd:cd03245 191 TLIIITHrpsLLDLVDriIVMDSGRIVADG 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
948-1164 |
4.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.37 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNG---HNINDD--IDGVRDSLGICPQF--DTLF 1020
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDkyIRPVRKRIGMVFQFpeSQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1021 PTlTVSEHIVFYSRLKGLSVAEAEAEvpVYIKDIDLENKADARVNS---LSGGQRRAVSCALALCGGSTFVALDEPTSGM 1097
Cdd:PRK13646 100 ED-TVEREIIFGPKNFKMNLDEVKNY--AHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1098 DPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS--SMFLKNTFGVGYHMTV 1164
Cdd:PRK13646 177 DPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSpkELFKDKKKLADWHIGL 247
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
946-1141 |
6.61e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.76 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND---DIDGVRDSLGICPQFDTLFPT 1022
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 LTVSEHIVFYS-RLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPfK 1101
Cdd:PRK09493 92 LTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP-E 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1102 RRHTwdmLLKHKQD-----RTIILTTHFMEEADILGDRI------AILADG 1141
Cdd:PRK09493 171 LRHE---VLKVMQDlaeegMTMVIVTHEIGFAEKVASRLifidkgRIAEDG 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
931-1148 |
8.92e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 8.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDG----- 1005
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1006 ------------VRDSLGICPQFD--TLFPTlTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDL-ENKADARVNSLSGG 1070
Cdd:PRK13631 102 npyskkiknfkeLRRRVSMVFQFPeyQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1071 QRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHK-QDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
931-1144 |
8.96e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 8.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVnGHNINddidgvrdsL 1010
Cdd:COG0488 316 LELEGLSKSY-----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQ-FDTLFPTLTVSEHIVfysrlkglsvAEAEAEVPVYIKDIdLE------NKADARVNSLSGGQRRAVSCALALCG 1083
Cdd:COG0488 381 GYFDQhQEELDPDKTVLDELR----------DGAPGGTEQEVRGY-LGrflfsgDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1084 GSTFVALDEPTSGMDPfkrrhtwDML------LKHkQDRTIILTTH---FMEEadiLGDRIAILADGELR 1144
Cdd:COG0488 450 PPNVLLLDEPTNHLDI-------ETLealeeaLDD-FPGTVLLVSHdryFLDR---VATRILEFEDGGVR 508
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
948-1143 |
9.16e-18 |
|
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: 82.75 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGICPQFDTLFPTltvse 1027
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1028 hivfysrlkglsvaeaeaevpvyikdiDLENKADARvnsLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWD 1107
Cdd:cd03247 90 ---------------------------TLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 167517209 1108 MLLKHKQDRTIILTTHF---MEEAdilgDRIAILADGEL 1143
Cdd:cd03247 140 LIFEVLKDKTLIWITHHltgIEHM----DKILFLENGKI 174
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
963-1148 |
1.02e-17 |
|
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: 86.70 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 963 ITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGV-----RDSLGICPQFDTLFPTLTVSEHIVF-YSRLK 1036
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRGNLRYgMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1037 GLSVAEAEAEVpvyIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDML--LKHKQ 1114
Cdd:TIGR02142 105 PSERRISFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLerLHAEF 181
|
170 180 190
....*....|....*....|....*....|....
gi 167517209 1115 DRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:TIGR02142 182 GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
941-1148 |
1.28e-17 |
|
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: 83.82 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 941 YPQTGGAkvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQfDTL 1019
Cdd:cd03251 10 YPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQ-DVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1020 FPTLTVSEHIVfYSRLkGLSVAEAE-----AEVPVYIKdiDLENKADARVNS----LSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03251 87 LFNDTVAENIA-YGRP-GATREEVEeaaraANAHEFIM--ELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFM---EEAdilgDRIAILADGELRTVGS 1148
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNRTTFVIAHRLstiENA----DRIVVLEDGKIVERGT 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
907-1148 |
1.36e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 88.30 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 907 PTVPHGTGPRSefVEDFAGnnavGIQIEGLRkvF-YPqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMY 985
Cdd:COG1132 322 PEIPDPPGAVP--LPPVRG----EIEFENVS--FsYP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 986 PPTAGTAKVNGHNIND-DIDGVRDSLGICPQfDT-LFpTLTVSEHIvfysRLKGLSVAEAE----AEVpVYIKDI--DLE 1057
Cdd:COG1132 391 DPTSGRILIDGVDIRDlTLESLRRQIGVVPQ-DTfLF-SGTIRENI----RYGRPDATDEEveeaAKA-AQAHEFieALP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1058 NKADARV----NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTH---FMEEAdi 1130
Cdd:COG1132 464 DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHrlsTIRNA-- 541
|
250
....*....|....*...
gi 167517209 1131 lgDRIAILADGELRTVGS 1148
Cdd:COG1132 542 --DRILVLDDGRIVEQGT 557
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
948-1148 |
2.09e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.37 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND--DIDGVRDSLGICPQF-DTLFPTLT 1024
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeeNLWDIRNKAGMVFQNpDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1025 VSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRH 1104
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 167517209 1105 TWDML--LKHKQDRTIILTTHFMEEAdILGDRIAILADGELRTVGS 1148
Cdd:PRK13633 183 VVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
941-1162 |
3.84e-17 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 82.59 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 941 YPQTGGAKVaLEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTL 1019
Cdd:cd03249 10 YPSRPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1020 FPTlTVSEHIVfYSRLKGLSVAEAEAEVPVYIKD--IDLENKADARV----NSLSGGQRRAVSCALALCGGSTFVALDEP 1093
Cdd:cd03249 89 FDG-TIAENIR-YGKPDATDEEVEEAAKKANIHDfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1094 TSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMeeADILG-DRIAILADGELRTVGSSMFLKNTFGVGYHM 1162
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMKGRTTIVIAHRL--STIRNaDLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
931-1141 |
7.16e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.11 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTggakvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDD-------- 1002
Cdd:PRK11264 4 IEVKNLVKKFHGQT-----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1003 -IDGVRDSLGICPQFDTLFPTLTVSEHIVFYSRL-KGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALA 1080
Cdd:PRK11264 79 lIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1081 LCGGSTFVALDEPTSGMDP---FKRRHTWDMLLKHKqdRTIILTTHFMEEADILGDRiAILADG 1141
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPelvGEVLNTIRQLAQEK--RTMVIVTHEMSFARDVADR-AIFMDQ 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
946-1148 |
8.81e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGV-RDSLGICPQFDTLFPTLT 1024
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1025 VSEhIVFYSRLKGLSV-----AEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDP 1099
Cdd:PRK11231 93 VRE-LVAYGRSPWLSLwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 167517209 1100 FKRRHTWDMLLKHKQD-RTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK11231 172 NHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
956-1158 |
8.96e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 81.05 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 956 LNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDidgvRDSLGICPQ---FDTLFPtLTVsEHIVFY 1032
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG----WRHIGYVPQrheFAWDFP-ISV-AHTVMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1033 SR------LKGLSVAEAEAeVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTW 1106
Cdd:TIGR03771 75 GRtghigwLRRPCVADFAA-VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1107 DMLLKHKQD-RTIILTTHFMEEADILGDRIAIL-----ADGELRTVGSSMFLKNTFGV 1158
Cdd:TIGR03771 154 ELFIELAGAgTAILMTTHDLAQAMATCDRVVLLngrviADGTPQQLQDPAPWMTTFGV 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
965-1146 |
9.48e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 965 ALLGHNGAGKTTTISMLVGMYPP---TAGTAKVNGHNIndDIDGVRDSLGICPQFDTLFPTLTVSEHIVFYSRLK---GL 1038
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRmprRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1039 SVAEAEAEVPVYIKDIDLENKAD------ARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKH 1112
Cdd:TIGR00955 133 TKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
170 180 190
....*....|....*....|....*....|....*..
gi 167517209 1113 KQD-RTIILTTHfMEEADI--LGDRIAILADGelRTV 1146
Cdd:TIGR00955 213 AQKgKTIICTIH-QPSSELfeLFDKIILMAEG--RVA 246
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
946-1099 |
1.00e-16 |
|
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: 80.10 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGICPQFDTLFPTLTV 1025
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1026 SEHIVFYSRLKG---LSVAEAEAEVpvyikdiDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDP 1099
Cdd:TIGR01189 91 LENLHFWAAIHGgaqRTIEDALAAV-------GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
931-1141 |
1.10e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKVaLEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:PRK15439 12 LCARSISKQY----SGVEV-LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GI--CPQFDTLFPTLTVSEHIVFysRLKGlsVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFV 1088
Cdd:PRK15439 87 GIylVPQEPLLFPNLSVKENILF--GLPK--RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1089 ALDEPTSGMDPFKRRHTW---DMLLkhKQDRTIILTTHFMEEADILGDRIAILADG 1141
Cdd:PRK15439 163 ILDEPTASLTPAETERLFsriRELL--AQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
931-1143 |
2.10e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDD-------- 1002
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1003 -----------------IDGVRDSLGICPQFD--TLFPTlTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDL-ENKADA 1062
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1063 RVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADG 1141
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 167517209 1142 EL 1143
Cdd:PRK13651 242 KI 243
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
900-1123 |
2.12e-16 |
|
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: 84.33 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 900 EETPSNAPTVPHGTGPRSEFVEDfagnNAVGIQIEGLRkVFYPqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTIS 979
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGAVGL----GKPTLELRDLS-AGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 980 MLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFPTlTVSEHIvfysRLKGLSVAEAEAE-----VPVYIKD 1053
Cdd:TIGR02868 380 TLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVRENL----RLARPDATDEELWaalerVGLADWL 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1054 IDLENKADARVN----SLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTH 1123
Cdd:TIGR02868 455 RALPDGLDTVLGeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
946-1148 |
2.23e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.59 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNInDDIDGVR--DSLGICPQFDTL-FPt 1022
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-ADWSPAElaRRRAVLPQHSSLsFP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 LTVSEhIVFYSRLK-GLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALC------GGSTFVALDEPTS 1095
Cdd:PRK13548 91 FTVEE-VVAMGRAPhGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1096 GMDPFKRRHTWDML--LKHKQDRTII-------LTTHFmeeadilGDRIAILADGELRTVGS 1148
Cdd:PRK13548 170 ALDLAHQHHVLRLArqLAHERGLAVIvvlhdlnLAARY-------ADRIVLLHQGRLVADGT 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
931-1147 |
2.52e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.08 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVnghNINDD-------- 1002
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDEwvdmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1003 IDG---VRDSLGICPQFDTLFPTLTVSEHIV---------FYSRLKGLSVAEAeaevpVYIKDIDLENKADARVNSLSGG 1070
Cdd:TIGR03269 357 PDGrgrAKRYIGILHQEYDLYPHRTVLDNLTeaiglelpdELARMKAVITLKM-----VGFDEEKAEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1071 QRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQD--RTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
936-1148 |
3.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 936 LRKVFYPQTGGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND--DIDGVRDSLGIC 1013
Cdd:PRK13644 4 LENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1014 PQF-DTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDE 1092
Cdd:PRK13644 83 FQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1093 PTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHFMEEADIlGDRIAILADGELRTVGS 1148
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
941-1143 |
3.63e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 83.61 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 941 YPQTGGAkvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTL 1019
Cdd:TIGR02203 340 YPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1020 FPTlTVSEHIVfYSRLKGLSVAEAE-AEVPVYIKD-ID-LENKADARVNS----LSGGQRRAVSCALALCGGSTFVALDE 1092
Cdd:TIGR02203 418 FND-TIANNIA-YGRTEQADRAEIErALAAAYAQDfVDkLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1093 PTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFM---EEAdilgDRIAILADGEL 1143
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLMQGRTTLVIAHRLstiEKA----DRIVVMDDGRI 545
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
931-1148 |
4.10e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.67 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKVaLEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHnindDIDGV--RD 1008
Cdd:PRK10851 3 IEIANIKKSF----GRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLhaRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 -SLGICPQFDTLFPTLTVSEHIVFysrlkGLSV---------AEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCA 1078
Cdd:PRK10851 74 rKVGFVFQHYALFRHMTVFDNIAF-----GLTVlprrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1079 LALCGGSTFVALDEPTSGMDPFKRRH--TWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKElrRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
931-1143 |
8.11e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 76.87 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkVFYPqtGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDS 1009
Cdd:cd03246 1 LEVENVS-FRYP--GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LGICPQFDTLFPTltvsehivfysrlkglSVAEaeaevpvyikdidlenkadarvNSLSGGQRRAVSCALALCGGSTFVA 1089
Cdd:cd03246 78 VGYLPQDDELFSG----------------SIAE----------------------NILSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1090 LDEPTSGMDPFKRRHTWDML--LKhKQDRTIILTTHFMEEADILgDRIAILADGEL 1143
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIaaLK-AAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
950-1148 |
9.38e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.67 E-value: 9.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGV------RDSLGICPQFD--TLFP 1021
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVFQFPeyQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1022 TlTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDL-ENKADARVNSLSGGQRRAVSCA-LALCGGSTFVaLDEPTSGMDP 1099
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAgIIAMDGNTLV-LDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1100 FKRRHTWDMLLK--HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK13645 184 KGEEDFINLFERlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
926-1148 |
1.01e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.18 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 926 NNAVGIQIEGLRkvF-YPQtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DI 1003
Cdd:PRK11160 334 ADQVSLTLNNVS--FtYPD--QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1004 DGVRDSLGICPQfdtlfptltvSEHIvFYSRLKG-LSVAEAEA---EVPVYIKDIDLEN--KADARVNS--------LSG 1069
Cdd:PRK11160 410 AALRQAISVVSQ----------RVHL-FSATLRDnLLLAAPNAsdeALIEVLQQVGLEKllEDDKGLNAwlgeggrqLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1070 GQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTH---FMEEAdilgDRIAILADGELRTV 1146
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltGLEQF----DRICVMDNGQIIEQ 554
|
..
gi 167517209 1147 GS 1148
Cdd:PRK11160 555 GT 556
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
948-1148 |
1.29e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.20 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHninddidgvrdslgICPQFDT---LFPTLT 1024
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--------------VSALLELgagFHPELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1025 VSEHIVFYSRLKGLSVAEAEAevpvYIKDI----DLENKADARVNSLSGGQR-R-AVSCALALcggsTF--VALDEPTSG 1096
Cdd:COG1134 105 GRENIYLNGRLLGLSRKEIDE----KFDEIvefaELGDFIDQPVKTYSSGMRaRlAFAVATAV----DPdiLLVDEVLAV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1097 MDP-FKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:COG1134 177 GDAaFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
950-1148 |
1.33e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 82.48 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFpTLTVSEH 1028
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIF-SGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1029 IVFYSR--------LKGLSVAEAEAEVPVYIKDIDLENKADArvNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPF 1100
Cdd:TIGR01193 568 LLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQTELSEEG--SSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 167517209 1101 KRRHTWDMLLKhKQDRTIILTTHFMEEADiLGDRIAILADGELRTVGS 1148
Cdd:TIGR01193 646 TEKKIVNNLLN-LQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGS 691
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
946-1148 |
2.22e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.85 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND----DIDGVRdslGICPQFDTL-F 1020
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwELARRR---AVLPQHSSLaF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1021 PtLTVSE--------HIVFYSRLKGLsVAEAEAEVpvyikdiDLENKADARVNSLSGGQRRAVSCALALC-------GGS 1085
Cdd:COG4559 89 P-FTVEEvvalgrapHGSSAAQDRQI-VREALALV-------GLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1086 TFVALDEPTSGMDpfkrrhtwdmlLKHKQdrtiilttHFMEEA---------------DI-----LGDRIAILADGELRT 1145
Cdd:COG4559 160 RWLFLDEPTSALD-----------LAHQH--------AVLRLArqlarrgggvvavlhDLnlaaqYADRILLLHQGRLVA 220
|
...
gi 167517209 1146 VGS 1148
Cdd:COG4559 221 QGT 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
962-1162 |
2.51e-15 |
|
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: 77.27 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFPTlTVsEHIVFYSRLkglSV 1040
Cdd:cd03253 28 KKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND-TI-GYNIRYGRP---DA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1041 AEAEAEVPVYIKDID-----LENKADARVNS----LSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK 1111
Cdd:cd03253 103 TDEEVIEAAKAAQIHdkimrFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1112 HKQDRTIILTTHFMEEAdILGDRIAILADGELRTVGSSMFLKNTFGVGYHM 1162
Cdd:cd03253 183 VSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
931-1142 |
2.59e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFyPqtgGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINddIDGVRDS- 1009
Cdd:PRK10762 5 LQLKGIDKAF-P---GVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT--FNGPKSSq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 ---LGICPQFDTLFPTLTVSEHIV----FYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALC 1082
Cdd:PRK10762 78 eagIGIIHQELNLIPQLTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1083 GGSTFVALDEPTsgmDPFKRRHTWDML-----LKhKQDRTIILTTHFMEEADILGDRIAILADGE 1142
Cdd:PRK10762 158 FESKVIIMDEPT---DALTDTETESLFrvireLK-SQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
931-1143 |
3.22e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.38 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRkVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGM---YPP--TAGTAKVNGHNIND---D 1002
Cdd:COG1117 12 IEVRNLN-VYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlIPGarVEGEILLDGEDIYDpdvD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1003 IDGVRDSLGICPQFDTLFPTlTVSEHIVFYSRLKGL-SVAEAEA-------------EVpvyiKDidlenKADARVNSLS 1068
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEiveeslrkaalwdEV----KD-----RLKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1069 GGQ-RRAvsC---ALA-----LCggstfvaLDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILA 1139
Cdd:COG1117 157 GGQqQRL--CiarALAvepevLL-------MDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFY 227
|
....
gi 167517209 1140 DGEL 1143
Cdd:COG1117 228 LGEL 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
931-1148 |
3.76e-15 |
|
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: 76.38 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLrKVFYPQtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDS 1009
Cdd:cd03244 3 IEFKNV-SLRYRP--NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LGICPQFDTLFPTlTVSEHIVFYSRLKGLSVAEAEAEvpVYIKDI--DLENKADARV----NSLSGGQRRAVSCALALCG 1083
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLDPFGEYSDEELWQALER--VGLKEFveSLPGGLDTVVeeggENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1084 GSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEadILG-DRIAILADGELRTVGS 1148
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDT--IIDsDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
946-1148 |
4.34e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.54 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN-DDIDGVRDSLGICPQF--DTLFPT 1022
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVGLVFQNpdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 lTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKR 1102
Cdd:PRK13652 95 -TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 167517209 1103 RHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK13652 174 KELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
946-1123 |
5.25e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.22 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGICPQFDTLFPTLTV 1025
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1026 SEHIVFYSRLKGLS-VAEAEAEVpvyikdiDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRH 1104
Cdd:cd03231 91 LENLRFWHADHSDEqVEEALARV-------GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 167517209 1105 TWDMLLKH-KQDRTIILTTH 1123
Cdd:cd03231 164 FAEAMAGHcARGGMVVLTTH 183
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
951-1145 |
9.74e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVR-----DSLGICPQFDTLFPTLTV 1025
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1026 SEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHT 1105
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 167517209 1106 WDML--LKHKQDRTIILTTHFMEEADILgDRIAILADGELRT 1145
Cdd:PRK11629 185 FQLLgeLNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
947-1142 |
1.14e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 74.43 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 947 AKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGhninddidgvrdSLGICPQFDTLFPTlTVS 1026
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1027 EHIVFYS-----RLKglSVAEAEAEVPvyikDIDLENKADA-----RVNSLSGGQRRAVSCALALCGGSTFVALDEPTSG 1096
Cdd:cd03250 84 ENILFGKpfdeeRYE--KVIKACALEP----DLEILPDGDLteigeKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1097 MDPFKRRHTWDMLLKH--KQDRTIILTTH---FMEEAdilgDRIAILADGE 1142
Cdd:cd03250 158 VDAHVGRHIFENCILGllLNNKTRILVTHqlqLLPHA----DQIVVLDNGR 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
936-1141 |
2.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 936 LRKVFYPQTGGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGV---RDSLGI 1012
Cdd:PRK13636 8 VEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLmklRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1013 CPQF-DTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALD 1091
Cdd:PRK13636 87 VFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1092 EPTSGMDPFKRRHTWDMLLKHKQ--DRTIILTTHFMEEADILGDRIAILADG 1141
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
945-1150 |
3.88e-14 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 77.00 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 945 GGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFPTl 1023
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFGKHIGYLPQDVELFPG- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1024 TVSEHIV-FYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVN----SLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:TIGR01842 407 TVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1099 PFKRRHTWDMLLK-HKQDRTIILTTHfmeEADILG--DRIAILADGELRTVGSSM 1150
Cdd:TIGR01842 487 EEGEQALANAIKAlKARGITVVVITH---RPSLLGcvDKILVLQDGRIARFGERD 538
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
946-1129 |
4.39e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDidGVRDSlgICPQF--------D 1017
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA--RHRRA--VCPRIaympqglgK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1018 TLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGG--QRRAVSCALA----LcggstfVALD 1091
Cdd:NF033858 88 NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGmkQKLGLCCALIhdpdL------LILD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 167517209 1092 EPTSGMDPFKRRHTWDMLLKHKQDR---TIILTTHFMEEAD 1129
Cdd:NF033858 162 EPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAE 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
931-1141 |
8.47e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL 1010
Cdd:PRK11300 6 LSVSGLMMRF-----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDT--LFPTLTVSEHI-----------VFYSRLKGLSVAEAEAE----VPVYIKDIDLENKADARVNSLSGGQRR 1073
Cdd:PRK11300 81 GVVRTFQHvrLFREMTVIENLlvaqhqqlktgLFSGLLKTPAFRRAESEaldrAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1074 AVSCALALCGGSTFVALDEPTSGMDPfKRRHTWDML---LKHKQDRTIILTTHFMEEADILGDRIAILADG 1141
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNP-KETKELDELiaeLRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
951-1143 |
1.51e-13 |
|
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: 71.73 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFpTLTVSEHI 1029
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEPVLF-ARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1030 VF------YSRLKGLSV-AEAEAEVPVYIKDIDLEnkADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKR 1102
Cdd:cd03248 109 AYglqscsFECVKEAAQkAHAHSFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 167517209 1103 RHTWDMLLKHKQDRTIILTTHFM---EEAdilgDRIAILADGEL 1143
Cdd:cd03248 187 QQVQQALYDWPERRTVLVIAHRLstvERA----DQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
951-1148 |
1.52e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVrdsLGICPQFDTLFPTltvSEHIV 1030
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGL---LALRQQVATVFQD---PEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 FYS--------RLKGLSVAEAEA--EVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPF 1100
Cdd:PRK13638 91 FYTdidsdiafSLRNLGVPEAEItrRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167517209 1101 KRRHTWDMLLK-HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK13638 171 GRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
965-1148 |
1.75e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.46 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 965 ALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN-DDIDGVRDSLGICPQF-DTLFPTLTVSEHIVFYSRLKGLSVAE 1042
Cdd:PRK13650 37 SIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeENVWDIRHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1043 AEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDR--TIIL 1120
Cdd:PRK13650 117 MKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVIS 196
|
170 180
....*....|....*....|....*...
gi 167517209 1121 TTHFMEEAdILGDRIAILADGELRTVGS 1148
Cdd:PRK13650 197 ITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
953-1160 |
2.08e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 953 HLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdIDGVRDSLGICPQFDTLFPTLTVSEHIVFY 1032
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND-VPPAERGVGMVFQSYALYPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1033 SRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCalalcgGSTFVA------LDEPTSGMDPFKRRHTW 1106
Cdd:PRK11000 100 LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAI------GRTLVAepsvflLDEPLSNLDAALRVQMR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1107 DMLLK-HKQ-DRTIILTTHFMEEADILGDRIAILADGELRTVGSSMFL----KNTFGVGY 1160
Cdd:PRK11000 174 IEISRlHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFVAGF 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
931-1143 |
2.69e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.76 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVfYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGV--- 1006
Cdd:PRK10535 5 LELKDIRRS-YPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 -RDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGS 1085
Cdd:PRK10535 84 rREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1086 TFVALDEPTSGMDpfkrRHTWD---MLLKHKQDR--TIILTTHFMEEADiLGDRIAILADGEL 1143
Cdd:PRK10535 164 QVILADEPTGALD----SHSGEevmAILHQLRDRghTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
930-1143 |
3.42e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.27 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 930 GIQIEGLRkvfypqTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPtaGTAKVNGHNInddIDGVRDS 1009
Cdd:PRK10418 4 QIELRNIA------LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVL---LDGKPVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LG---------ICPQFDTLF-PTLTVSEHIVfySRLKGLSVAEAEAEVPVYIKDIDLENkaDARVNSL-----SGG--QR 1072
Cdd:PRK10418 73 PCalrgrkiatIMQNPRSAFnPLHTMHTHAR--ETCLALGKPADDATLTAALEAVGLEN--AARVLKLypfemSGGmlQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1073 RAVscALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRT--IILTTHFMEEADILGDRIAILADGEL 1143
Cdd:PRK10418 149 MMI--ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
897-1131 |
3.84e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.76 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 897 KADEETPSNAPTVPHGT-GPRSEFVEDFAGNN-------AVGIQIEGLRKVFYPQ--TGGAKVALEHLDLNMYRDQITAL 966
Cdd:TIGR00956 715 KAGETSASNKNDIEAGEvLGSTDLTDESDDVNdekdmekESGEDIFHWRNLTYEVkiKKEKRVILNNVDGWVKPGTLTAL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 967 LGHNGAGKTTTISML---VGMYPPTAGTAKVNGHNINDDIdgvRDSLGICPQFDTLFPTLTVSEHIVFYSRL---KGLSV 1040
Cdd:TIGR00956 795 MGASGAGKTTLLNVLaerVTTGVITGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSK 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1041 AEAEAEVPVYIKDIDLENKADARVN----SLSGGQRRAVSCALALCGG-STFVALDEPTSGMDPfkrRHTWDM--LLKHK 1113
Cdd:TIGR00956 872 SEKMEYVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELVAKpKLLLFLDEPTSGLDS---QTAWSIckLMRKL 948
|
250 260
....*....|....*....|....*
gi 167517209 1114 QD--RTIILTTH-----FMEEADIL 1131
Cdd:TIGR00956 949 ADhgQAILCTIHqpsaiLFEEFDRL 973
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
951-1144 |
4.33e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSL-----GICPQFDTLFPTLTV 1025
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1026 SEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDpfkrRHT 1105
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD----RQT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 167517209 1106 WDML------LKHKQDRTIILTTHFMEEADILGDRIAiLADGELR 1144
Cdd:PRK10584 182 GDKIadllfsLNREHGTTLILVTHDLQLAARCDRRLR-LVNGQLQ 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
933-1145 |
5.22e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 933 IEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGhninddidGVRdsLGI 1012
Cdd:COG0488 1 LENLSKSF-----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------GLR--IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1013 CPQFDTLFPTLTVSEHIvfysrLKGLS--------VAEAEAEVPVYIKDI----------------DLENKA-------- 1060
Cdd:COG0488 66 LPQEPPLDDDLTVLDTV-----LDGDAelraleaeLEELEAKLAEPDEDLerlaelqeefealggwEAEARAeeilsglg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1061 ------DARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDpfkrRHT--W--DMLLKHKqdRTIILTTH---FMEE 1127
Cdd:COG0488 141 fpeedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESieWleEFLKNYP--GTVLVVSHdryFLDR 214
|
250
....*....|....*...
gi 167517209 1128 adiLGDRIAILADGELRT 1145
Cdd:COG0488 215 ---VATRILELDRGKLTL 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
931-1099 |
5.80e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKvFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN-------DDI 1003
Cdd:PRK11124 3 IQLNGINC-FY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpsdKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1004 DGVRDSLGICPQFDTLFPTLTVSEHIVFYS-RLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALC 1082
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170
....*....|....*..
gi 167517209 1083 GGSTFVALDEPTSGMDP 1099
Cdd:PRK11124 158 MEPQVLLFDEPTAALDP 174
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
951-1143 |
5.85e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN-DDIDGVRDSLGICPQF-DTLFPTLTVSEH 1028
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1029 IVFYSRLKGLSVAEAEAEVP---VYIKDIDLENKADARvnsLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHT 1105
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDealLAVNMLDFKTREPAR---LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 167517209 1106 WDML--LKHKQDRTIILTTHFMEEAdILGDRIAILADGEL 1143
Cdd:PRK13642 180 MRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
951-1158 |
6.38e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI-NDDIDGVRDSLGICPQFDTL---FPTLTVS 1026
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLsfeFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1027 E-----HIvfySRLKGLSVAEaEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFK 1101
Cdd:PRK09536 99 EmgrtpHR---SRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1102 RRHTWDMLLKHKQD-RTIILTTHFMEEADILGDRIAILADGELRTVG------SSMFLKNTFGV 1158
Cdd:PRK09536 175 QVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAFDA 238
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
962-1147 |
8.25e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 72.86 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNInDDIDgvRDSLGIC----PQFDTLFPTlTVSEHIvfySRLkg 1037
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL-SQWD--REELGRHigylPQDVELFDG-TIAENI---ARF-- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1038 lsvAEAEAEvpvyiKDIDLENKADA-------------RV----NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPF 1100
Cdd:COG4618 430 ---GDADPE-----KVVAAAKLAGVhemilrlpdgydtRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1101 KRRHTWDMLLKHKQD-RTIILTTH---FMEEAdilgDRIAILADGELRTVG 1147
Cdd:COG4618 502 GEAALAAAIRALKARgATVVVITHrpsLLAAV----DKLLVLRDGRVQAFG 548
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
936-1148 |
9.09e-13 |
|
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: 69.82 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 936 LRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICP 1014
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1015 QFDTLF------------PTLTVsEHIVFYSRLKGlsVAEAEAEVPVYIKDIDLENKAdarvnSLSGGQRRAVSCALALC 1082
Cdd:cd03252 83 QENVLFnrsirdnialadPGMSM-ERVIEAAKLAG--AHDFISELPEGYDTIVGEQGA-----GLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1083 GGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMeEADILGDRIAILADGELRTVGS 1148
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
952-1123 |
9.19e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 952 EHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdidgVRDSLgicpQFDTLF--------PTL 1023
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR----QRDEY----HQDLLYlghqpgikTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1024 TVSEHIVFYSRLKGLSVAEAEAEVpvyIKDIDLENKADARVNSLSGGQRRAVSCA-LALCGGSTFVaLDEP-----TSGM 1097
Cdd:PRK13538 90 TALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALArLWLTRAPLWI-LDEPftaidKQGV 165
|
170 180
....*....|....*....|....*..
gi 167517209 1098 DPFKRRhtwdmLLKH-KQDRTIILTTH 1123
Cdd:PRK13538 166 ARLEAL-----LAQHaEQGGMVILTTH 187
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
930-1145 |
1.60e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.92 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 930 GIQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTiSMLVGMYPPTAGTAKVNGHNINDDIDGVRDS 1009
Cdd:NF000106 13 AVEVRGLVKHF-----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 LGIC-PQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFV 1088
Cdd:NF000106 87 IG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1089 ALDEPTSGMDPFKRRHTWDMLLKHKQD-RTIILTTHFMEEADILG------DRIAILADG---ELRT 1145
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAheltviDRGRVIADGkvdELKT 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
962-1141 |
1.95e-12 |
|
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: 67.65 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMypPTAGTAK----VNGHNINDDIdgvRDSLGICPQFDTLFPTLTVSEHIVFYSRLKG 1037
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLAGR--KTAGVITgeilINGRPLDKNF---QRSTGYVEQQDVHSPNLTVREALRFSALLRG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1038 LSVAeaeaevpvyikdidlenkadarvnslsggQRRAVSCALALCGGSTFVALDEPTSGMDPfkrRHTWDM--LLKHKQD 1115
Cdd:cd03232 109 LSVE-----------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDS---QAAYNIvrFLKKLAD 156
|
170 180 190
....*....|....*....|....*....|
gi 167517209 1116 --RTIILTTHfMEEADILG--DRIAILADG 1141
Cdd:cd03232 157 sgQAILCTIH-QPSASIFEkfDRLLLLKRG 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
939-1136 |
2.19e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.04 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 939 VFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTI---SMLVGMYPPTAGTAKV--NGHNIND-DID--GVRDSL 1010
Cdd:PRK14243 18 VYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVtfHGKNLYApDVDpvEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQFDTLFPTlTVSEHIVFYSRLKGLSVAEAEAeVPVYIKDIDL--ENKADARVN--SLSGGQRRAVSCALALCGGST 1086
Cdd:PRK14243 94 GMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDEL-VERSLRQAALwdEVKDKLKQSglSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 167517209 1087 FVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIA 1136
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
951-1144 |
4.03e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMyPPTAGTAKVNG------HNIND---DIDGVRDSLGICPQFDTLFP 1021
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrveffnQNIYErrvNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1022 tLTVSEHIVFYSRLKGL-SVAEAEAEVPVYIKDIDL----ENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSG 1096
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 167517209 1097 MDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELR 1144
Cdd:PRK14258 181 LDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
931-1154 |
4.27e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.12 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTggakvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMyppTAGTAKVNGH------------N 998
Cdd:PRK09984 5 IRVEKLAKTFNQHQ-----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHiellgrtvqregR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 999 INDDIDGVRDSLG-ICPQFDtLFPTLTVSEHIV---------------FYSRLKGLSVAEAeaevpvyIKDIDLENKADA 1062
Cdd:PRK09984 77 LARDIRKSRANTGyIFQQFN-LVNRLSVLENVLigalgstpfwrtcfsWFTREQKQRALQA-------LTRVGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1063 RVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDR--TIILTTHFMEEADILGDRIAILAD 1140
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQ 228
|
250
....*....|....
gi 167517209 1141 GELRTVGSSMFLKN 1154
Cdd:PRK09984 229 GHVFYDGSSQQFDN 242
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
948-1149 |
4.89e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI---ND--DIDGV--RDSLGICPQFDTLF 1020
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDifQIDAIklRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1021 PTLTVSEHIVFYSRLKGLSVA-EAEAEVPVYIKDIDLENKADARVNS----LSGGQRRAVSCALALCGGSTFVALDEPTS 1095
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1096 GMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
950-1143 |
5.50e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND--DIDGVRDSLGICPQFDTLFPTLTVSE 1027
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1028 HIV----FYSRLKGLSVAEAeaevpVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRR 1103
Cdd:PRK11614 100 NLAmggfFAERDQFQERIKW-----VYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 167517209 1104 HTWDMLLKHKQD-RTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
963-1147 |
7.29e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 963 ITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN--DDIDG------------VRDSLGICPQFDTLFPTLTVSEH 1028
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvRDKDGqlkvadknqlrlLRTRLTMVFQHFNLWSHMTVLEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1029 IVFYS-RLKGLSVAEAEAEVPVYIKDIDLENKADARVNS-LSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTW 1106
Cdd:PRK10619 113 VMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 167517209 1107 DMLLKHKQD-RTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:PRK10619 193 RIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
931-1098 |
1.06e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.05 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYpqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI----NDDIDGV 1006
Cdd:PRK10908 2 IRFEHVSKAYL----GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGST 1086
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170
....*....|..
gi 167517209 1087 FVALDEPTSGMD 1098
Cdd:PRK10908 158 VLLADEPTGNLD 169
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
931-1123 |
1.68e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 63.62 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTakvnghninddidgvrdsl 1010
Cdd:cd03221 1 IELENLSKTY-----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 gicpqfdtlfptltvsehivfYSRLKGLSVAeaeaevpvYikdidlenkadarVNSLSGGQRRAVSCALALCGGSTFVAL 1090
Cdd:cd03221 57 ---------------------VTWGSTVKIG--------Y-------------FEQLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|...
gi 167517209 1091 DEPTSGMDPFKRRHTWDMLLKHKqdRTIILTTH 1123
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYP--GTVILVSH 125
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
948-1148 |
1.83e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVnghninddidgVRDSLGICPQFDTLFpTLTVSE 1027
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1028 HIVFYSRLKGLSVAEAeAEVPVYIKDIDLENKAD-----ARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKR 1102
Cdd:PLN03232 698 NILFGSDFESERYWRA-IDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 167517209 1103 RHTWDMLLKHK-QDRTIILTT---HFMEeadiLGDRIAILADGELRTVGS 1148
Cdd:PLN03232 777 HQVFDSCMKDElKGKTRVLVTnqlHFLP----LMDRIILVSEGMIKEEGT 822
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
946-1131 |
3.63e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.43 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPP---TAGTAKVNGHNInDDIDGVRDSLGICPQFDTLFPT 1022
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-TALPAEQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 LTVSEHIVFYSRlKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDP--- 1099
Cdd:COG4136 91 LSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAalr 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 167517209 1100 --FkRRHTWDMLlkhkQDRTI--ILTTHfmEEADIL 1131
Cdd:COG4136 170 aqF-REFVFEQI----RQRGIpaLLVTH--DEEDAP 198
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
937-1148 |
3.71e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.74 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 937 RKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQ 1015
Cdd:PRK11176 345 RNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1016 FDTLFPTlTVSEHIVfYSRLKGLSVAEAE--AEVPVYIKDID-LENKADARVN----SLSGGQRRAVSCALALCGGSTFV 1088
Cdd:PRK11176 425 NVHLFND-TIANNIA-YARTEQYSREQIEeaARMAYAMDFINkMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1089 ALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFM---EEAdilgDRIAILADGELRTVGS 1148
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLstiEKA----DEILVVEDGEIVERGT 561
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
933-1143 |
4.75e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 933 IEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPT-----AGTAKVngHNINDDIDgvr 1007
Cdd:PRK11247 15 LNAVSKRY-----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSagellAGTAPL--AEAREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1008 dslgICPQFDTLFPTLTVSEHIVFysRLKGLSVAEAEAEvpvyIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTF 1087
Cdd:PRK11247 85 ----LMFQDARLLPWKKVIDNVGL--GLKGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1088 VALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
951-1142 |
6.04e-11 |
|
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: 64.88 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHninddidgvrdsLGICPQFDTLFPTlTVSEHIV 1030
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------ISFSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 F---YSRLKGLSVAEA---EAEVPVYiKDIDLENKADARVNsLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRH 1104
Cdd:cd03291 120 FgvsYDEYRYKSVVKAcqlEEDITKF-PEKDNTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190
....*....|....*....|....*....|....*....
gi 167517209 1105 TWD-MLLKHKQDRTIILTTHFMEEADIlGDRIAILADGE 1142
Cdd:cd03291 198 IFEsCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGS 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
957-1142 |
6.36e-11 |
|
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: 64.35 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 957 NMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGtakvnghnindDIDGVRDSLGICPQFDTLFPTLTVSEhiVFYSRLK 1036
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----------DIEIELDTVSYKPQYIKADYEGTVRD--LLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1037 GL-SVAEAEAEVpvyIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTwDMLLKH--- 1112
Cdd:cd03237 88 DFyTHPYFKTEI---AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA-SKVIRRfae 163
|
170 180 190
....*....|....*....|....*....|
gi 167517209 1113 KQDRTIILTTHFMEEADILGDRIaILADGE 1142
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRL-IVFEGE 192
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
948-1148 |
7.50e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFPTLTVS 1026
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1027 EHIV-----FYSRLKGLSVAEAEaEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPfk 1101
Cdd:PRK10575 104 ELVAigrypWHGALGRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI-- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1102 rRHTWDML-----LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK10575 181 -AHQVDVLalvhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
946-1148 |
8.47e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDG-VRDSLGICPQFDTLFPTLT 1024
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1025 VSE--------HIVFYSRLKglsvAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSG 1096
Cdd:PRK10253 98 VQElvargrypHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1097 MDPfkrRHTWDML-----LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK10253 174 LDI---SHQIDLLellseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
963-1098 |
1.66e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 963 ITALLGHNGAGKTT---TISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGICPQFDTLFPTLTVSEHIVFYSRLKGls 1039
Cdd:cd03233 35 MVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKG-- 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1040 vaeaeaevpvyikdidlenkaDARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:cd03233 113 ---------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
931-1098 |
1.71e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNghninddiDGVRdsL 1010
Cdd:TIGR03719 323 IEAENLTKAF-----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--------ETVK--L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQF-DTLFPTLTVSEHIVfysrlKGLSVAE-AEAEVP--VYI-----KDIDLENKadarVNSLSGGQRRAVSCALAL 1081
Cdd:TIGR03719 388 AYVDQSrDALDPNKTVWEEIS-----GGLDIIKlGKREIPsrAYVgrfnfKGSDQQKK----VGQLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 167517209 1082 CGGSTFVALDEPTSGMD 1098
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
951-1162 |
2.07e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.51 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFpTLTVSEHI 1029
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLF-SGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1030 VF---YSRLKGLSVAEAEAEVPVYIKDidLENKADARV----NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKR 1102
Cdd:TIGR00958 576 AYgltDTPDEEIMAAAKAANAHDFIME--FPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1103 RHTWDmlLKHKQDRTIILTTH---FMEEAdilgDRIAILADGELRTVGSSMFLKNTFGVGYHM 1162
Cdd:TIGR00958 654 QLLQE--SRSRASRTVLLIAHrlsTVERA----DQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
950-1142 |
2.84e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN--DDIDGVRDSLGICPQFDTLFPTLTVSE 1027
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1028 HIvFYSR--LKGLSVAEAEA--EVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRR 1103
Cdd:PRK10982 93 NM-WLGRypTKGMFVDQDKMyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 167517209 1104 HTWDMLLKHKQDRT-IILTTHFMEEADILGDRIAILADGE 1142
Cdd:PRK10982 172 HLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
952-1141 |
3.60e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 952 EHL----DLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRdSLGICPQFDTLFPTLTVSE 1027
Cdd:PRK10771 12 HHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR-PVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1028 HIvfysrlkGLSV-------AEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVscALALCggstFVA------LDEPT 1094
Cdd:PRK10771 91 NI-------GLGLnpglklnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRV--ALARC----LVReqpillLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1095 SGMDPFKRRhtwDML-----LKHKQDRTIILTTHFMEEADILGDRIAILADG 1141
Cdd:PRK10771 158 SALDPALRQ---EMLtlvsqVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
931-1142 |
4.88e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtGGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDS- 1009
Cdd:TIGR02633 2 LEMKGIVKTF----GGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 ---LGICPQFDTLFPTLTVSEHIVFYSR--LKGLSVAEAEA--EVPVYIKDIDLENKADAR-VNSLSGGQRRAVSCALAL 1081
Cdd:TIGR02633 77 ragIVIIHQELTLVPELSVAENIFLGNEitLPGGRMAYNAMylRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1082 CGGSTFVALDEPTSGMDPFKRRHTWDmLLKHKQDRTI--ILTTHFMEEADILGDRIAILADGE 1142
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLD-IIRDLKAHGVacVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
931-1146 |
5.10e-10 |
|
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: 64.05 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDD-IDGVRDs 1009
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADnREAYRQ- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1010 lgicpQFDTLFptltvSEHIVFySRLKGLSVAEAEAEVPVYIKDIDLENK---ADARV--NSLSGGQRRAVSCALALCGG 1084
Cdd:COG4615 407 -----LFSAVF-----SDFHLF-DRLLGLDGEADPARARELLERLELDHKvsvEDGRFstTDLSQGQRKRLALLVALLED 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1085 STFVALDEPTSGMDP-FKRR--HTWDMLLKhKQDRTIILTTH----FmeeadILGDRIAILADGELRTV 1146
Cdd:COG4615 476 RPILVFDEWAADQDPeFRRVfyTELLPELK-ARGKTVIAISHddryF-----DLADRVLKMDYGKLVEL 538
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
946-1123 |
6.22e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNghninddiDGVRdsLGICPQFDTLFPTLTV 1025
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN--------GKLR--IGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1026 SehivfYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHT 1105
Cdd:PRK09544 85 T-----VNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|
gi 167517209 1106 WDML--LKHKQDRTIILTTH 1123
Cdd:PRK09544 160 YDLIdqLRRELDCAVLMVSH 179
|
|
| PGRP |
COG3409 |
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ... |
33-97 |
7.70e-10 |
|
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442635 [Multi-domain] Cd Length: 69 Bit Score: 56.45 E-value: 7.70e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 33 DRVLALGDAGQDVFILQNLIRNNNQSIVlrNASAVFDNATQAAVVALQQAWGLSATGVADATTLA 97
Cdd:COG3409 3 APTLRLGDSGEDVRELQQRLNALGYYPG--PVDGIFGPATEAAVRAFQRANGLPVDGIVGPATWA 65
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
951-1123 |
8.63e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGICPQFDTLFPTLTVSEHIV 1030
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 FysrlkGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLL 1110
Cdd:PRK13540 97 Y-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....
gi 167517209 1111 KH-KQDRTIILTTH 1123
Cdd:PRK13540 172 EHrAKGGAVLLTSH 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
944-1154 |
1.13e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.93 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 944 TGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI----NDDIDGVRDSLGICPQFDTL 1019
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1020 FPTLTVSEHIVFYSR-LKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:PRK11831 96 FTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1099 PFkrrhTWDMLLK------HKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSSMFLKN 1154
Cdd:PRK11831 176 PI----TMGVLVKliselnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
925-1098 |
1.23e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 925 GNNAVGIQIEGLRKVFYPQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTT----TISMLVGMYPPTAGTAKVNGHNIN 1000
Cdd:TIGR00956 51 PNALLKILTRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1001 DDIDGVRDSLGICPQFDTLFPTLTVSEHIVFYSRLK-------GLSVAE-AEAEVPVYIKDIDLENKADARVNS-----L 1067
Cdd:TIGR00956 131 EIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgV 210
|
170 180 190
....*....|....*....|....*....|.
gi 167517209 1068 SGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
944-1147 |
1.29e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.86 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 944 TGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-----------DIDGV-RDSLG 1011
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrDIQMVfQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1012 -ICPQFdtlfptlTVSEHIVFYSR-LKGLSVAEAEAEVPVYIKDIDL-ENKADARVNSLSGGQRRAVSCALALCGGSTFV 1088
Cdd:PRK10419 101 aVNPRK-------TVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1089 ALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADG---ELRTVG 1147
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGqivETQPVG 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
951-1141 |
1.64e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 59.65 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGtaKVNGHNINDDIDGV-------RDSLGICPQFDTLFpTL 1023
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNKNESEPSFeatrsrnRYSVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1024 TVSEHIVF---YSRLKGLSVAEAEAEVPvyikDIDL-----ENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTS 1095
Cdd:cd03290 94 TVEENITFgspFNKQRYKAVTDACSLQP----DIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167517209 1096 GMDPFKRRH-TWDMLLKHKQD--RTIILTTHFMEEAdILGDRIAILADG 1141
Cdd:cd03290 170 ALDIHLSDHlMQEGILKFLQDdkRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
931-1156 |
1.95e-09 |
|
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: 62.13 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGM--YPPTAG------------------ 990
Cdd:TIGR03269 1 IEVKNLTKKF-----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 991 ------TAKVNGHNINDDID----------GVRDSLGICPQ--FdTLFPTLTVSEHIvfysrLKGLSVAEAEAEVPVY-- 1050
Cdd:TIGR03269 76 skvgepCPVCGGTLEPEEVDfwnlsdklrrRIRKRIAIMLQrtF-ALYGDDTVLDNV-----LEALEEIGYEGKEAVGra 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1051 ---IKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK--HKQDRTIILTTHFM 1125
Cdd:TIGR03269 150 vdlIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWP 229
|
250 260 270
....*....|....*....|....*....|.
gi 167517209 1126 EEADILGDRIAILADGELRTVGSSMFLKNTF 1156
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
971-1143 |
2.47e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.57 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 971 GAGKTTTISMLVGMYPPTAGTAKVNGHNIndDIDGVRDSL--GI--CP---QFDTLFPTLTVSEHIVF-----YSRLKGL 1038
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPV--RIRSPRDAIraGIayVPedrKGEGLVLDLSIRENITLasldrLSRGGLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1039 SVAEAEAEVPVYIKDIDLenKA---DARVNSLSGG-QRRAVscaLA--LCGGSTFVALDEPTSGMDP------FKrrhtw 1106
Cdd:COG1129 366 DRRRERALAEEYIKRLRI--KTpspEQPVGNLSGGnQQKVV---LAkwLATDPKVLILDEPTRGIDVgakaeiYR----- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 167517209 1107 dmLLKH--KQDRTIILTTHFMEEadILG--DRIAILADGEL 1143
Cdd:COG1129 436 --LIRElaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
948-1123 |
2.65e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYP--PTAGTAKVNGHNINDDIDGVrDSLGICPQFDTLFPTLTV 1025
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLI-DAIGRKGDFKDAVELLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1026 SehivfysrlkGLSvaeaeaEVPVYIkdidlenkadARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDP-FKRR- 1103
Cdd:COG2401 122 V----------GLS------DAVLWL----------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAKRv 175
|
170 180
....*....|....*....|.
gi 167517209 1104 -HTWDMLLKhKQDRTIILTTH 1123
Cdd:COG2401 176 aRNLQKLAR-RAGITLVVATH 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
946-1149 |
6.25e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.95 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAG-----TAKVNGHNIND--DIDGVRDSLGICPQFDT 1018
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNyrDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1019 LFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNS----LSGGQRRAVSCALALCGGSTFVALDEPT 1094
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1095 SGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPT 246
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
959-1123 |
7.22e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 57.23 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 959 YRDQITALLGHNGAGKTTTI-SMLVGMYPPTAGTAKVNGHNinDDIDGVRDSLGicpqfdtlfptltvSEHIVFYSRLKG 1037
Cdd:cd03240 20 FFSPLTLIVGQNGAGKTTIIeALKYALTGELPPNSKGGAHD--PKLIREGEVRA--------------QVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1038 LSVAEAEAEV---PVYIK--DID--LENKADarvnSLSGGQRRAVS----CALA--LCGGSTFVALDEPTSGMDPFKRRH 1104
Cdd:cd03240 84 KYTITRSLAIlenVIFCHqgESNwpLLDMRG----RCSGGEKVLASliirLALAetFGSNCGILALDEPTTNLDEENIEE 159
|
170 180
....*....|....*....|..
gi 167517209 1105 TWDMLL---KHKQDRTIILTTH 1123
Cdd:cd03240 160 SLAEIIeerKSQKNFQLIVITH 181
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
945-1148 |
8.20e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.97 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 945 GGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFpTL 1023
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLF-NR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1024 TVSEHIvfysRLKGLSVAEAE-------AEVPVYI--KDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPT 1094
Cdd:PRK13657 424 SIEDNI----RVGRPDATDEEmraaaerAQAHDFIerKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1095 SGMDPFKRRHTWDMLLKHKQDRT--II---LTThfMEEAdilgDRIAILADGELRTVGS 1148
Cdd:PRK13657 500 SALDVETEAKVKAALDELMKGRTtfIIahrLST--VRNA----DRILVFDNGRVVESGS 552
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
962-1098 |
1.10e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMYPPTAGTAKV--NGHNINDDIdgvRDSLGICPQFDTLFPTLTVSEHIVFYSRL---K 1036
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNFTGTIlaNNRKPTKQI---LKRTGFVTQDDILYPHLTVRETLVFCSLLrlpK 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1037 GLSVAEAEAEVPVYIKDIDL---ENK--ADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLtkcENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
945-1148 |
1.54e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.17 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 945 GGAKvALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPptAGT---------AKVNGHNINDDidgVRDSLGICPQ 1015
Cdd:PRK13549 16 GGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--HGTyegeiifegEELQASNIRDT---ERAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1016 FDTLFPTLTVSEHIVF---------------YSRLKGLSvaeaeAEVPVyikDIDlenkADARVNSLSGGQRRAVSCALA 1080
Cdd:PRK13549 90 ELALVKELSVLENIFLgneitpggimdydamYLRAQKLL-----AQLKL---DIN----PATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1081 LCGGSTFVALDEPTSGMDPFKRRHTWDML--LKHKqDRTIILTTHFMEEADILGDRIAILADGelRTVGS 1148
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIrdLKAH-GIACIYISHKLNEVKAISDTICVIRDG--RHIGT 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
951-1148 |
1.59e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVnghninddidgVRDSLGICPQFDTLFpTLTVSEHIV 1030
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIF-NATVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 FYSRLKGLSVAEAeAEVPVYIKDIDLENKAD-----ARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHT 1105
Cdd:PLN03130 701 FGSPFDPERYERA-IDVTALQHDLDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 167517209 1106 WDMLLKHK-QDRTIILTT---HFMEEAdilgDRIAILADGELRTVGS 1148
Cdd:PLN03130 780 FDKCIKDElRGKTRVLVTnqlHFLSQV----DRIILVHEGMIKEEGT 822
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
951-1154 |
2.29e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHninddidgvrdsLGICPQFDTLFPTlTVSEHIV 1030
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------------ISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 F---YSRLKGLSVAEA-EAEvpvyiKDIDLENKADARV-----NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFK 1101
Cdd:TIGR01271 509 FglsYDEYRYTSVIKAcQLE-----EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 167517209 1102 RRHTWD-MLLKHKQDRTIILTTHFMEEADiLGDRIAILADGELRTVGSSMFLKN 1154
Cdd:TIGR01271 584 EKEIFEsCLCKLMSNKTRILVTSKLEHLK-KADKILLLHEGVCYFYGTFSELQA 636
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
953-1143 |
2.39e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 953 HLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGIC--P---QFDTLF------- 1020
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPedrQSSGLYldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1021 --PTLTVSEHIVFYSRLKGLSVAEAeaevpvYIKDIDLE-NKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGM 1097
Cdd:PRK15439 361 nvCALTHNRRGFWIKPARENAVLER------YRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 167517209 1098 DPFKRRHTWDmLLKH--KQDRTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:PRK15439 435 DVSARNDIYQ-LIRSiaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
946-1143 |
3.35e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 56.35 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdIDG-----VRDSLGICPQ--FDT 1018
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ-LDRkqrraFRRDVQLVFQdsPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1019 LFPTLTVSEHIVFYSR-LKGLSVAEAEAEVPVYIKDIDLENK-ADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSG 1096
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167517209 1097 MDPFKRRHTWDMLLKHKQDRTI--ILTTHFMEEADILGDRIAILADGEL 1143
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
931-1098 |
1.91e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNghninddiDGVRdsL 1010
Cdd:PRK11819 325 IEAENLSKSF-----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--------ETVK--L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1011 GICPQF-DTLFPTLTVSEHIvfySrlKGLSVAE-AEAEVP--VYI-----KDIDlENKadaRVNSLSGGQRRAVSCALAL 1081
Cdd:PRK11819 390 AYVDQSrDALDPNKTVWEEI---S--GGLDIIKvGNREIPsrAYVgrfnfKGGD-QQK---KVGVLSGGERNRLHLAKTL 460
|
170
....*....|....*..
gi 167517209 1082 CGGSTFVALDEPTSGMD 1098
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLD 477
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
963-1098 |
2.21e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.01 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 963 ITALLGHNGAGKTTTISMLVGM----YppTAGTAKVNGHNINDDIdGVRDSlGICPQFDTLFPTLTVSEHIVF--YSRL- 1035
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAGRktggY--IEGDIRISGFPKKQET-FARIS-GYCEQNDIHSPQVTVRESLIYsaFLRLp 983
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 1036 KGLSVAEAEAEVPVYIKDIDLENKADARV-----NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:PLN03140 984 KEVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
957-1144 |
2.50e-07 |
|
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: 55.22 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 957 NMYRDQITALLGHNGAGKTTTISMLVGMYPPT-AGTAKVNGH--NINDDIDGVRDSLGICPQ---FDTLFPTLTVSEHIV 1030
Cdd:TIGR02633 282 SLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkRHGIVPILGVGKNIT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 FYS--RLKGLSVAEAEAEVPVYIKDID-LENKA---DARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRH 1104
Cdd:TIGR02633 362 LSVlkSFCFKMRIDAAAELQIIGSAIQrLKVKTaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYE 441
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 167517209 1105 TWDMLLKHKQdRTIILTTHFMEEADILG--DRIAILADGELR 1144
Cdd:TIGR02633 442 IYKLINQLAQ-EGVAIIVVSSELAEVLGlsDRVLVIGEGKLK 482
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1067-1129 |
2.97e-07 |
|
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: 51.59 E-value: 2.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1067 LSGGQRRAVSCALAL----CGGSTFVALDEPTSGMDPFKRRHTWDMLLKH-KQDRTIILTTH---FMEEAD 1129
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlVKGAQVIVITHlpeLAELAD 148
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
950-1167 |
3.39e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.35 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDdidGVRDSL-GICPQ---FDTLFPTLTv 1025
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLvAYVPQseeVDWSFPVLV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1026 sEHIVF---YSRLKGLSVAEAE--AEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDpF 1100
Cdd:PRK15056 98 -EDVVMmgrYGHMGWLRRAKKRdrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD-V 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1101 KRRHTWDMLLKHKQD--RTIILTTHFMEEADILGD-----RIAILADGELRTVGSSMFLKNTF-GVGYHMTVVKG 1167
Cdd:PRK15056 176 KTEARIISLLRELRDegKTMLVSTHNLGSVTEFCDytvmvKGTVLASGPTETTFTAENLELAFsGVLRHVALNGS 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
950-1147 |
3.82e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGVRDSLGICPQF------DTLFPTL 1023
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFifqdpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1024 TVSEHIVFYSRLKGLSVAEAEAE-VPVYIKDIDLENKADARV-NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFK 1101
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAArVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 167517209 1102 RRHTWDMLLKHKQDRTI--ILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
962-1138 |
4.02e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.14 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNG--------------HN-----INDDIDGVRDslgicPQFDTLFPt 1022
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeildefrgselQNyftklLEGDVKVIVK-----PQYVDLIP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1023 ltvsehivfySRLKG-----LSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGM 1097
Cdd:cd03236 101 ----------KAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 167517209 1098 DpFKRRHTWDMLLKH--KQDRTIILTTHFMEEADILGDRIAIL 1138
Cdd:cd03236 171 D-IKQRLNAARLIRElaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
951-1148 |
4.37e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMypptagTAKVNGHNinddidGVRDSLGICPQfDTLFPTLTVSEHIV 1030
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE------MDKVEGHV------HMKGSVAYVPQ-QAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1031 FYSRLKG---LSVAEAEAEVPvyikDIDLENKADAR------VNsLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFK 1101
Cdd:TIGR00957 721 FGKALNEkyyQQVLEACALLP----DLEILPSGDRTeigekgVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1102 RRHTWDMLLKHK---QDRTIILTTH---FMEEADIlgdrIAILADGELRTVGS 1148
Cdd:TIGR00957 796 GKHIFEHVIGPEgvlKNKTRILVTHgisYLPQVDV----IIVMSGGKISEMGS 844
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
914-1098 |
1.23e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.18 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 914 GPRSEFVEDFAGNNAVGIQIEGLRKVFYPQtggaKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAK 993
Cdd:PRK10790 324 GPRQQYGNDDRPLQSGRIDIDNVSFAYRDD----NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 994 VNGHNINDDIDGV-RDSLGICPQ-----FDTLFPTLT----VSEHIVfYSRLKGLSVAEAEAEVPVYIKDIDLENKadar 1063
Cdd:PRK10790 400 LDGRPLSSLSHSVlRQGVAMVQQdpvvlADTFLANVTlgrdISEEQV-WQALETVQLAELARSLPDGLYTPLGEQG---- 474
|
170 180 190
....*....|....*....|....*....|....*
gi 167517209 1064 vNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:PRK10790 475 -NNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
941-1143 |
1.24e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 941 YP----QTGGAKVALEHL--------DLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINddIDGVRD 1008
Cdd:PRK10762 246 YPrldkAPGEVRLKVDNLsgpgvndvSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV--TRSPQD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1009 SL--GIC-----PQFDTLFPTLTVSEHIV-----FYSRLKG-LSVAEAEAEVPVYIKDIDLENKA-DARVNSLSGGQRRA 1074
Cdd:PRK10762 324 GLanGIVyisedRKRDGLVLGMSVKENMSltalrYFSRAGGsLKHADEQQAVSDFIRLFNIKTPSmEQAIGLLSGGNQQK 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1075 VSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQD-RTIILTTHFMEEadILG--DRIAILADGEL 1143
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
918-1144 |
1.41e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 918 EFVEDFAGNNAV-GIQIEGLRKVFYpQTGGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNG 996
Cdd:PRK10522 306 PYKAEFPRPQAFpDWQTLELRNVTF-AYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 997 HNIndDIDGVRDslgicpqFDTLFPTLTVSEHIvfYSRLKGLSVAEAEAE-VPVYIKDIDLENK---ADARVN--SLSGG 1070
Cdd:PRK10522 385 KPV--TAEQPED-------YRKLFSAVFTDFHL--FDQLLGPEGKPANPAlVEKWLERLKMAHKlelEDGRISnlKLSKG 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1071 QRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQD--RTIILTTH----FmeeadILGDRIAILADGELR 1144
Cdd:PRK10522 454 QKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHddhyF-----IHADRLLEMRNGQLS 528
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
922-1143 |
2.21e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.15 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 922 DFAGNNAVGIQIEGLrKVFYPQtggAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGmYPPTAGTAKVNGHNIND 1001
Cdd:PRK11174 341 ELASNDPVTIEAEDL-EILSPD---GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1002 -DIDGVRDSLGICPQFDTLFPTlTVSEHIvfysRLKGLSVAEAEAEVPV---YIKDI--DLENKADARVN----SLSGGQ 1071
Cdd:PRK11174 416 lDPESWRKHLSWVGQNPQLPHG-TLRDNV----LLGNPDASDEQLQQALenaWVSEFlpLLPQGLDTPIGdqaaGLSVGQ 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1072 RRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTIILTTHFMEEADILgDRIAILADGEL 1143
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
950-1146 |
2.44e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPptAGTakVNGhnindDI--DG-------VRDS--LGIC--PQF 1016
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGS--YEG-----EIlfDGevcrfkdIRDSeaLGIViiHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1017 DTLFPTLTVSEHIvFYS--RLKG--LSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDE 1092
Cdd:NF040905 87 LALIPYLSIAENI-FLGneRAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1093 PTSGMDPFKRRHTWDMLLKHK-QDRTIILTTHFMEEADILGDRIAILADGelRTV 1146
Cdd:NF040905 166 PTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSITVLRDG--RTI 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
956-1099 |
4.63e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 956 LNMYRDQITALL--GHNGAGKTTTISMLVGMYPPTAGTAKVNGH-NINDDIDGVRDSLGICPqfdTLFPTLTVSEHIVFY 1032
Cdd:PRK13543 30 LDFHVDAGEALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRFMAYLGHLP---GLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167517209 1033 SRLKGLSVAEAEAEVpvyIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDP 1099
Cdd:PRK13543 107 CGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
950-1147 |
4.89e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGhnindDIDGVRDSLGICPQfdtlfptLTVSEHI 1029
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1030 VFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDML 1109
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 167517209 1110 LKHK-QDRTIILTTHFMEEADILGDRIAILADGELRTVG 1147
Cdd:PRK13546 187 YEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PG_binding_1 |
pfam01471 |
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
42-97 |
6.28e-06 |
|
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.
Pssm-ID: 460223 [Multi-domain] Cd Length: 57 Bit Score: 44.81 E-value: 6.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 42 GQDVFILQNLIRNNNQSIVlrNASAVFDNATQAAVVALQQAWGLSATGVADATTLA 97
Cdd:pfam01471 2 GEDVKELQRYLNRLGYYPG--PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLA 55
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
947-1148 |
8.55e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 947 AKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPptaGTAKVNGHNINDD----------IDGVRDSL--GICP 1014
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDvtlngeplaaIDAPRLARlrAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1015 QF-DTLFPtLTVSEhIVFYSRLKGLSVAEAEAEVPVYIKDIDLEnKADAR------VNSLSGGQRRAVSCALALC----- 1082
Cdd:PRK13547 90 QAaQPAFA-FSARE-IVLLGRYPHARRAGALTHRDGEIAWQALA-LAGATalvgrdVTTLSGGELARVQFARVLAqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1083 ----GGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTI-ILT-THFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK13547 167 hdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAiVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
929-1143 |
1.55e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 929 VGIQIEGLRkvfypqtgGAKVAlEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGH--NINDDIDGV 1006
Cdd:PRK11288 256 VRLRLDGLK--------GPGLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RDSLGICPQ---FDTLFPTLTVSEHIV-----FYSRLKGLSVAEAEAE-VPVYIKDIDLENK-ADARVNSLSGGQRRAVS 1076
Cdd:PRK11288 327 RAGIMLCPEdrkAEGIIPVHSVADNINisarrHHLRAGCLINNRWEAEnADRFIRSLNIKTPsREQLIMNLSGGNQQKAI 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1077 CALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLK-HKQDRTIILTTHfmEEADILG--DRIAILADGEL 1143
Cdd:PRK11288 407 LGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSS--DLPEVLGvaDRIVVMREGRI 474
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
962-1142 |
1.72e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 962 QITALLGHNGAGKTTTISMLVGMYPPTAGtakvnghniNDDIDGVRDSLGicpqfdtlfptltvsehivfysrlkglsva 1041
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIPNGD---------NDEWDGITPVYK------------------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1042 eaeaevPVYIKdidlenkadarvnsLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTII 1119
Cdd:cd03222 67 ------PQYID--------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIrrLSEEGKKTAL 126
|
170 180
....*....|....*....|...
gi 167517209 1120 LTTHFMEEADILGDRIaILADGE 1142
Cdd:cd03222 127 VVEHDLAVLDYLSDRI-HVFEGE 148
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
960-1144 |
2.51e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 960 RDQITALLGHNGAGKTTTISMLVGMYP-PTAGTAKVNGHNIndDIDGVRDSL--GIC--PQ---FDTLFPTLTVSEHIVF 1031
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPV--KIRNPQQAIaqGIAmvPEdrkRDGIVPVMGVGKNITL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1032 --YSRLKGLSVAEAEAEVPVYIKDID-LENKA---DARVNSLSGG-QRRAVsCALALCGGSTFVALDEPTSGMDPFKRRH 1104
Cdd:PRK13549 365 aaLDRFTGGSRIDDAAELKTILESIQrLKVKTaspELAIARLSGGnQQKAV-LAKCLLLNPKILILDEPTRGIDVGAKYE 443
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 167517209 1105 TWDMLLK-HKQDRTIILTTHfmEEADILG--DRIAILADGELR 1144
Cdd:PRK13549 444 IYKLINQlVQQGVAIIVISS--ELPEVLGlsDRVLVMHEGKLK 484
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
950-1148 |
4.27e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 950 ALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGH----------NIND-------DIDGVRDSLGI 1012
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEqsaaqmrHVRGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1013 CPQFDTLFPTLTVSEHIVFYSRL-KGLSVAEAEAEVPvyiKDIDLENKADARV------NSLSGGQRRAVSCALAL-CGG 1084
Cdd:PRK10261 111 QEPMTSLNPVFTVGEQIAESIRLhQGASREEAMVEAK---RMLDQVRIPEAQTilsrypHQLSGGMRQRVMIAMALsCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167517209 1085 STFVAlDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGS 1148
Cdd:PRK10261 188 AVLIA-DEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
931-1149 |
7.32e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAK----VALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNINDDIDGV 1006
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1007 RdSLGICPQF----DTLFPTLTVSEHIVFYSRLK-GLSVAEAEAEVPVYIKDIDL-ENKADARVNSLSGGQRRAVSCALA 1080
Cdd:PRK15112 85 R-SQRIRMIFqdpsTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167517209 1081 LCGGSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTHFMEEADILGDRIAILADGELRTVGSS 1149
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMleLQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
931-1123 |
1.57e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.49 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 931 IQIEGLRKVFYPQTGGAkVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPP---TAGTAKVNGHNI----NDDI 1003
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDV-TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1004 DGVR-DSLGICPQ--FDTLFPTLTVSEHIVFYSRL-KGLSVAEAEAEVpvyIKDIDLENKADARV------NSLSGGQRR 1073
Cdd:PRK09473 92 NKLRaEQISMIFQdpMTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEES---VRMLDAVKMPEARKrmkmypHEFSGGMRQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1074 AVSCALAL-CGGSTFVAlDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTH 1123
Cdd:PRK09473 169 RVMIAMALlCRPKLLIA-DEPTTALDVTVQAQIMTLLneLKREFNTAIIMITH 220
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
963-1126 |
2.12e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 963 ITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND----DIDGVRDSLGICPQfdtlfptLTVSEHIVFYSRlkgl 1038
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiakpYCTYIGHNLGLKLE-------MTVFENLKFWSE---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1039 sVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDMLLKHKQDRTI 1118
Cdd:PRK13541 97 -IYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGI 175
|
....*...
gi 167517209 1119 ILTTHFME 1126
Cdd:PRK13541 176 VLLSSHLE 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
960-1143 |
2.16e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 960 RDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIN--DDIDGVRDSLGICPQF---DTLFPTLTVSEHIVFYSR 1034
Cdd:PRK09700 288 RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1035 LK--------GL-------SVAEAEAEVpVYIKDIDLENKadarVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDP 1099
Cdd:PRK09700 368 LKdggykgamGLfhevdeqRTAENQREL-LALKCHSVNQN----ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 167517209 1100 FKRRHTWDMLLKHKQD-RTIILTTHFMEEADILGDRIAILADGEL 1143
Cdd:PRK09700 443 GAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1036-1123 |
2.99e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.69 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1036 KGLSVAEAEAEVPVYIKDIDLENKADARvnSLSGGQRRAVSCALAL---CGGSTFVALDEPTSGMDPFKRRHTWDMLLKH 1112
Cdd:pfam13304 208 KSLLVDDRLRERGLILLENGGGGELPAF--ELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKEL 285
|
90
....*....|..
gi 167517209 1113 KQDRT-IILTTH 1123
Cdd:pfam13304 286 SRNGAqLILTTH 297
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
957-1141 |
3.09e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 957 NMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNG-----HNINDDIDG-------VRDSLGICPQFDTLFPTLt 1024
Cdd:PRK10982 270 DLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnHNANEAINHgfalvteERRSTGIYAYLDIGFNSL- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1025 VSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKA-DARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRR 1103
Cdd:PRK10982 349 ISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGhRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKF 428
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 167517209 1104 HTWDMLLK-HKQDRTIILTTHFMEEadILG--DRIAILADG 1141
Cdd:PRK10982 429 EIYQLIAElAKKDKGIIIISSEMPE--LLGitDRILVMSNG 467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
946-1162 |
3.78e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.32 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLF---- 1020
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiGLHDLRFKITIIPQDPVLFsgsl 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1021 -----PTLTVSEHIVFYSrlkgLSVAEAEAEVPVYIKDIDLENKADARvnSLSGGQRRAVSCALALCGGSTFVALDEPTS 1095
Cdd:TIGR00957 1377 rmnldPFSQYSDEEVWWA----LELAHLKTFVSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1096 GMDPFKRRHTWDMLLKHKQDRTIILTTHFMeeaDILGD--RIAILADGELRTVGSSMFLKNTFGVGYHM 1162
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFEDCTVLTIAHRL---NTIMDytRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
989-1123 |
3.96e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 989 AGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFpTLTVSEHIVF---YSRLKGLSVAEAEAEVPVYIKDidLENKADARV 1064
Cdd:PTZ00265 1276 SGKILLDGVDICDyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFgkeDATREDVKRACKFAAIDEFIES--LPNKYDTNV 1352
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1065 ----NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKRRHTWDML--LKHKQDRTIILTTH 1123
Cdd:PTZ00265 1353 gpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAH 1417
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
658-786 |
4.60e-04 |
|
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 43.27 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 658 LILIFAFIYSASSITRElvfeKEQRLKEMMKMMGLSTWV----HWLAWFTKCFLFLFISVVIIMIIFAVgdcsrSATAMG 733
Cdd:COG1277 60 LLPLLAPALGMDAISGE----RESGTLELLLTLPISRWEivlgKFLGALLVLLLALLITFLLALLLGLL-----LFGSPP 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 167517209 734 AEFARYsdGGPVFLLFLLFAVnTICLCFMFSTFFSKSNVASAAGAILFFLFYM 786
Cdd:COG1277 131 PDLGAI--LGFYLGLLLLGLA-FLAIGLFISALTRNQIVAAILAIALWLLLVI 180
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
951-1098 |
9.90e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 951 LEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND-DIDGVRDSLGICPQFDTLFpTLTVSEHI 1029
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLF-SGTVRFNI 1330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167517209 1030 VFYSRLKGLSVAEAEAEVpvYIKDIDLENK--ADARV----NSLSGGQRRAVSCALALCGGSTFVALDEPTSGMD 1098
Cdd:PLN03232 1331 DPFSEHNDADLWEALERA--HIKDVIDRNPfgLDAEVseggENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
930-1150 |
1.06e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.29 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 930 GIQIEGLRKVfYPqtGGAKVaLEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNIND------DI 1003
Cdd:PRK11650 3 GLKLQAVRKS-YD--GKTQV-IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepadrDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1004 DGVRdslgicpQFDTLFPTLTVSEHIVFYSRLKGLSVAEAEAEVPVYIKDIDLENKADARVNSLSGGQRRAVSCALALCG 1083
Cdd:PRK11650 79 AMVF-------QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167517209 1084 GSTFVALDEPTSGMDPFKRRHtwdMLL--KHKQDR---TIILTTHFMEEADILGDRIAILADGELRTVGSSM 1150
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRVQ---MRLeiQRLHRRlktTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
948-1143 |
2.10e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.32 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 948 KVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAKVNGHNI-NDDIDGVRDsLGIC-----PQFDTLFP 1021
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItGLSPRERRR-LGVAyipedRLGRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1022 TLTVSEHIVF-------YSRLKGLSVAEAEAEVPVYIKDIDLenKA---DARVNSLSGG--QR----RAVSCALALcggs 1085
Cdd:COG3845 350 DMSVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDV--RTpgpDTPARSLSGGnqQKvilaRELSRDPKL---- 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167517209 1086 tFVAlDEPTSGMDPFKRRHTWDMLLKHKQDRT-IILTTHFMEEADILGDRIAILADGEL 1143
Cdd:COG3845 424 -LIA-AQPTRGLDVGAIEFIHQRLLELRDAGAaVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1058-1140 |
2.35e-03 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 41.04 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1058 NKADAR-VNSLSGGQRRAVSCALAL----CGGSTFVALDEPTSGMDPFKRRHTWDMLLK------HKQdrTIILTTHFME 1126
Cdd:cd03276 100 NKAAVRdVKTLSGGERSFSTVCLLLslweVMESPFRCLDEFDVFMDMVNRKISTDLLVKeakkqpGRQ--FIFITPQDIS 177
|
90
....*....|....*
gi 167517209 1127 E-ADILGDRIAILAD 1140
Cdd:cd03276 178 GlASSDDVKVFRMKD 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
926-993 |
3.38e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 3.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167517209 926 NNAVgiQIEGLRKVFypqtgGAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGTAK 993
Cdd:PRK15064 317 RNAL--EVENLTKGF-----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1060-1142 |
4.21e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517209 1060 ADARVNSLSGGQRRAVSCALALCGGSTFVALDEPTSGMDPFKR---RHTWDMLLKHKQDRtIILTTHFMEEA-DILGDRI 1135
Cdd:PRK10938 395 ADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLISEGETQ-LLFVSHHAEDApACITHRL 473
|
....*..
gi 167517209 1136 AILADGE 1142
Cdd:PRK10938 474 EFVPDGD 480
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1067-1131 |
4.32e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 39.98 E-value: 4.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167517209 1067 LSGGQRRAVSCALAL----CGGSTFVALDEPTSGMDPFKRRHTWDMLLKH-KQDRTIILTTH---FMEEADIL 1131
Cdd:cd03239 95 LSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMaKHTSQFIVITLkkeMFENADKL 167
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
946-991 |
5.11e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 5.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167517209 946 GAKVALEHLDLNMYRDQITALLGHNGAGKTTTISMLVGMYPPTAGT 991
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE 368
|
|
| |
