|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-1064 |
0e+00 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 2261.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 1 MDVVLHHVPEAKLVECIGQELIFLLPNKNFKHRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDSDSGPLFAG 80
Cdd:TIGR01257 1209 MDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAG 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 81 GAQQKRENVNPRHPCLGPREKAGQTPQDSNVCSPGAPAAHPEGQPPPEPECPGPQLNTGTQLVLQHVQALLVKRFQHTIR 160
Cdd:TIGR01257 1289 GAQQKRENANLRHPCSGPTEKAGQTPQASHTCSPGQPAAHPEGQPPPEPEDPGVPLNTGARLILQHVQALLVKRFQHTIR 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 161 SHKDFLAQIVLPATFVFLALMLSIVIPPFGEYPALTLHPWIYGQQYTFFSMDEPGSEQFTVLADVLLNKPGFGNRCLKEG 240
Cdd:TIGR01257 1369 SHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEPNSEHLEVLADVLLNKPGFGNRCLKEE 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 241 WLPEYPCGNSTPWKTPSVSPNITQLFQKQKWTQVNPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDR 320
Cdd:TIGR01257 1449 WLPEYPCGNSTPWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDR 1528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 321 NISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPVVPITGEALVGFLSDLGRIMNVSGGPITREASKEIPDFLKH 400
Cdd:TIGR01257 1529 NISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPITGEALVGFLSDLGQMMNVSGGPVTREASKEMPDFLKH 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 401 LETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRSPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIF 480
Cdd:TIGR01257 1609 LETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIF 1688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 481 SMSFVPASFVLYLIQERVNKSKHLQFISGVSPTTYWVTNFLWDIMNYSVSAGLVVGIFIGFQKKAYTSPENLPALVALLL 560
Cdd:TIGR01257 1689 AMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLM 1768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 561 LYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFILELFENNRTLLRFNAVLRKLLIVFPHFCLGRGLIDL 640
Cdd:TIGR01257 1769 LYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFCLGRGLIDL 1848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 641 ALSQAVTDVYARFGEEHSANPFHWDLIGKNLFAMVVEGVVYFLLTLLVQRHFFLSQWIAEPTKEPIVDEDDDVAEERQRI 720
Cdd:TIGR01257 1849 ALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEERQRI 1928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 721 ITGGNKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS 800
Cdd:TIGR01257 1929 ISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS 2008
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 801 EVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 880
Cdd:TIGR01257 2009 DVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 881 PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGDGYIVT 960
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVT 2168
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 961 MKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFQLLLSHKDSLLIEEYSVTQTTLDQVFVNF 1040
Cdd:TIGR01257 2169 MKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNF 2248
|
1050 1060
....*....|....*....|....
gi 50949876 1041 AKQQTESHDLPLHPRAAGASRQAQ 1064
Cdd:TIGR01257 2249 AKQQTETYDLPLHPRAAGASRQAK 2272
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
730-950 |
2.80e-121 |
|
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: 370.30 E-value: 2.80e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 809
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 890 TTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 950
Cdd:cd03263 161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
730-953 |
1.09e-80 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 262.69 E-value: 1.09e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 809
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50949876 890 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKF 953
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
734-950 |
7.11e-64 |
|
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: 215.70 E-value: 7.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 734 ELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFD 813
Cdd:cd03265 5 NLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 814 AIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 893
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 894 DPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 950
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
730-938 |
1.49e-57 |
|
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: 195.69 E-value: 1.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 809
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYlyarlrgvpaeeiekvanwsikslgltvyadclagtYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 50949876 890 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
730-955 |
2.72e-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: 189.30 E-value: 2.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPgtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 809
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 890 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGD 955
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
727-938 |
1.37e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 172.30 E-value: 1.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 727 TDILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNM 806
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
729-944 |
7.04e-47 |
|
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: 167.16 E-value: 7.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNM 806
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMG 944
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
724-938 |
5.10e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 166.16 E-value: 5.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 724 GNKTDI-LRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEV 802
Cdd:PRK13536 35 GSMSTVaIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 803 HQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPP 882
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 883 LVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
479-961 |
2.59e-44 |
|
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: 175.97 E-value: 2.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 479 IFSMSFVPASFVLyliqERVNKSKHLQFISGVSPTTYWVTNFL--WDIMNYSVsagLVVGIFIGFQKKAYTSpeNLPALV 556
Cdd:TIGR01257 664 IYSVSMTVKSIVL----EKELRLKETLKNQGVSNAVIWCTWFLdsFSIMSMSI---FLLTIFIMHGRILHYS--DPFILF 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 557 ALLLLYGWAVIPMMYPASFLFdvpSTAYVALSCanlfiginSSAITFILEL-------FENnrtllRFNAVLRKLLIVFP 629
Cdd:TIGR01257 735 LFLLAFSTATIMQCFLLSTFF---SKASLAAAC--------SGVIYFTLYLphilcfaWQD-----RMTADLKTAVSLLS 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 630 HFCLGRGlidlalsqavTDVYARFGEEHSAnpFHWDLIGKN------------LFAMVVEGVVYFLLTLLVQRHF----- 692
Cdd:TIGR01257 799 PVAFGFG----------TEYLVRFEEQGLG--LQWSNIGNSplegdefsfllsMKMMLLDAALYGLLAWYLDQVFpgdyg 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 693 ------FLSQ---WI-----------AEPTKEPIVDEDDDVAEERqriitGGNKTDILRLH----------ELTKIYPGT 742
Cdd:TIGR01257 867 tplpwyFLLQesyWLggegcstreerALEKTEPLTEEMEDPEHPE-----GINDSFFERELpglvpgvcvkNLVKIFEPS 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 743 SSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGR 822
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 823 EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 902
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 50949876 903 NVIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGDGYIVTM 961
Cdd:TIGR01257 1102 DLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTL 1159
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
730-938 |
5.49e-43 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 155.45 E-value: 5.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIsEVHQNMGYC 809
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 50949876 890 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
729-1046 |
5.56e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 156.04 E-value: 5.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnISEVHQNMGY 808
Cdd:COG4152 1 MLELKGLTKRFGDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPqfdaiDE--L---LTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 883
Cdd:COG4152 76 LP-----EErgLypkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 884 VLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGdGYIVTMKI 963
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 964 KSPKDDLLpdlnpveqffqgNFPGSVQRERHYNMLQFQVSSSSLAR-IFQLLLSHKDsllIEEYSVTQTTLDQVFVNFAK 1042
Cdd:COG4152 230 DGDAGWLR------------ALPGVTVVEEDGDGAELKLEDGADAQeLLRALLARGP---VREFEEVRPSLNEIFIEVVG 294
|
....
gi 50949876 1043 QQTE 1046
Cdd:COG4152 295 EKAE 298
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
730-920 |
1.21e-41 |
|
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: 151.86 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 809
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYLYARLRGVPA--EEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLD 887
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAdrEAIDEA----LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|...
gi 50949876 888 EPTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 920
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
730-941 |
2.62e-40 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 148.11 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSspAVD----RLCVGVrpgecFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQN 805
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDgvslTLGPGM-----YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 885
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 886 LDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFR 941
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
731-938 |
1.42e-39 |
|
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: 146.07 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 731 RLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGYC 809
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQF--------DAIDELLTGREHLylyarlrGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCP 881
Cdd:cd03225 81 FQNpddqffgpTVEEEVAFGLENL-------GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 50949876 882 PLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
730-938 |
1.18e-38 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 143.19 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYpGTSSpAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTnisEVHQNMGYC 809
Cdd:cd03269 1 LEVENVTKRF-GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 50949876 890 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
730-938 |
2.89e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 137.08 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGY 808
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQ------FDAI--DELLTGREHLylyarlrGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 880
Cdd:COG1122 80 VFQnpddqlFAPTveEDVAFGPENL-------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 881 PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
731-938 |
1.51e-34 |
|
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: 129.67 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 731 RLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-ISEVHQNMGYC 809
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLpLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFdaidelltgrehlylyarlrgvpaeeiekvanwsikslgltvyadclagtySGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 50949876 890 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
730-938 |
8.84e-34 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 129.18 E-value: 8.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEVHQNMGYC 809
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 50949876 890 TTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03259 158 LSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
730-945 |
5.21e-32 |
|
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: 124.86 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---------NIS 800
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlppheiarlGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 801 EVHQNMGYCPQFDAIDELLTG----REHLYLYARLRGVPAEEIEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIA 876
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAaqarTGSGLLLARARREEREARERAEEL-LERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949876 877 LIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
725-948 |
1.59e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.05 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 725 NKTDILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVHQ 804
Cdd:COG1121 2 MMMPAIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK----PPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 805 NMGYCPQFDAIDEL--LTGRE--HLYLYAR---LRGVPAEEIEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIAL 877
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDvvLMGRYGRrglFRRPSRADREAVDEA-LERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 878 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFrCMGTIQH 948
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEE 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
730-938 |
3.07e-29 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 116.44 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYP--GTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEV----- 802
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 803 -HQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCP 881
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 882 PLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEEcEALCTRLAIMVKG 938
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDG 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
727-949 |
6.89e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 122.32 E-value: 6.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 727 TDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTG---DTTVTSGDATVAGKSILT-NISEV 802
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLElSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 803 HQNMGYCPQfDAIDEL--LTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 880
Cdd:COG1123 82 GRRIGMVFQ-DPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 881 PPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHL 949
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
730-935 |
8.89e-29 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 115.26 E-value: 8.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnISEVHQNMG 807
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP----VTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 808 YCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLD 887
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 50949876 888 EPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 935
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
754-891 |
9.24e-29 |
|
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: 112.74 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLR 832
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLLK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 833 GVPAEEIEKVANWSIKSLGLTVYAD----CLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 891
Cdd:pfam00005 88 GLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
729-939 |
1.37e-28 |
|
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: 115.91 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISeVH----- 803
Cdd:COG0411 4 LLEVRGLTKRFGGL--VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLP-PHriarl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 ------QNMGYCPQFDAIDELLTGREH------LYLYARLRGVPAEE---IEKVANWsIKSLGLTVYADCLAGTYSGGNK 868
Cdd:COG0411 80 giartfQNPRLFPELTVLENVLVAAHArlgrglLAALLRLPRARREEreaRERAEEL-LERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 869 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGA 939
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
746-935 |
3.04e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 122.93 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQ-FDAIDElLTGREH 824
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQaFSLYGE-LTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 825 LYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 904
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190
....*....|....*....|....*....|..
gi 50949876 905 IVSIIREGRAVVLTS-HSMEECEaLCTRLAIM 935
Cdd:NF033858 440 LIELSREDGVTIFIStHFMNEAE-RCDRISLM 470
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
730-938 |
3.90e-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: 113.79 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIsEVHQ----N 805
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKL-PMHKrarlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 885
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50949876 886 LDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEG 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
729-945 |
1.05e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 113.21 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS--EVHQNM 806
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLSrrELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQFDAIDELLTGREhLYLYAR------LRGVPAEEIEKVAnWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 880
Cdd:COG1120 78 AYVPQEPPAPFGLTVRE-LVALGRyphlglFGRPSAEDREAVE-EALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 881 PPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
730-957 |
1.13e-27 |
|
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: 112.97 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYP--GTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-EVHQNM 806
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQ--FDAIDELLTGREHLYLYARLRGVPAEEiEKVANWsIKSLGLTV-YADCLAGTYSGGNKRKLSTAIALIGCPPL 883
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE-ERIAEL-LEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949876 884 VLLDEPTTGMDP--QARrmLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGDGY 957
Cdd:COG1124 160 LLLDEPTSALDVsvQAE--ILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
729-938 |
1.15e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.43 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISeVHQ---- 804
Cdd:COG1137 3 TLEAENLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLP-MHKrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 805 NMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLV 884
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 885 LLDEPTTGMDPQArrmlwnV--IVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG1137 159 LLDEPFAGVDPIA------VadIQKIIRHlkerGIGVLITDHNVRETLGICDRAYIISEG 212
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
395-687 |
2.79e-27 |
|
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: 114.41 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 395 PDFLKHLETEDN--IKVWFNNKGWHALVSFLNVAHNaiLRASLPKDRSPEEYGITVISQPLNLTKEQLSEitVLTTSVDA 472
Cdd:pfam12698 87 KGFSKDLLKGESatVTVYINSSNLLVSKLILNALQS--LLQQLNASALVLLLEALSTSAPIPVESTPLFN--PQSGYAYY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 473 VVAICVIFSMSFVPASFVLYLIQERVNKSKHLQFISGVSPTTYWVTNFLWDIMNYSVSAGLVVGIFIGFqkkaYTSPENL 552
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI----GIPFGNL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 553 PALVALLLLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGInSSAITFILELFENnrtllrfnaVLRKLLIVFPHFC 632
Cdd:pfam12698 239 GLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDPPS---------FLQWIFSIIPFFS 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 633 LGRGLIDLALSQAVTDvyarfgeehsanpfhwdlIGKNLFAMVVEGVVYFLLTLL 687
Cdd:pfam12698 309 PIDGLLRLIYGDSLWE------------------IAPSLIILLLFAVVLLLLALL 345
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
729-938 |
6.19e-27 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 110.29 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYP--GTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN----ISEV 802
Cdd:cd03257 1 LLEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 803 HQNMGYCPQ--FDAIDELLTGREHLY--LYARLRGVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSGGNKRKLSTAIAL 877
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 878 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
729-939 |
8.13e-27 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 109.98 E-value: 8.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSS--PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISEV 802
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 803 HQNMGYCPQ-FDaideLLTGR---EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALI 878
Cdd:cd03258 81 RRRIGMIFQhFN----LLSSRtvfENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 879 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGA 939
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
730-982 |
9.25e-27 |
|
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: 110.08 E-value: 9.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGY 808
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGL--TVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLkskfgdgyivtmkIKS 965
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI-------------LRS 226
|
250
....*....|....*..
gi 50949876 966 PKDDLlpdlnpVEQFFQ 982
Cdd:cd03295 227 PANDF------VAEFVG 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
730-945 |
1.31e-26 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 109.25 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISEVH 803
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 QNMGYCPQFDAIDELLTGrehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 883
Cdd:cd03300 79 QNYALFPHLTVFENIAFG-------LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 884 VLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
746-1036 |
2.59e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 110.95 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTNISEVhqnMGycpQ-----FD 813
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrKEFARRIGVV---FG---QrsqlwWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 814 aidelLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLtvyADCLagtysggNK--RKLS--------TAIALIGCPPL 883
Cdd:COG4586 111 -----LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDL---GELL-------DTpvRQLSlgqrmrceLAAALLHRPKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 884 VLLDEPTTGMDPQARRMLWNVIVSIIREGRA-VVLTSHSMEECEALCTRLAIMVKGafRCM--GTIQHLKSKFGDGYIVT 960
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRVIVIDHG--RIIydGSLEELKERFGPYKTIV 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 961 MKIKSPKDDL-LPDLNPVEqffqgnfpgsvqrERHYNMLQFQVSS-SSLARIFQLLLSHKDsllIEEYSVTQTTLDQV 1036
Cdd:COG4586 254 LELAEPVPPLeLPRGGEVI-------------EREGNRVRLEVDPrESLAEVLARLLARYP---VRDLTIEEPPIEEV 315
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
729-938 |
2.88e-26 |
|
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: 114.23 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSS---PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISE 801
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 802 VHQNMGYCPQ--FDAIDELLTGREHLYLYARLRGV-PAEEIEKVANWSIKSLGLTV-YADCLAGTYSGGNKRKLSTAIAL 877
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 878 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDG 481
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
729-935 |
4.01e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.64 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSS--PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniSEVHQNM 806
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQFDAideLL---TGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 883
Cdd:COG1116 83 GVVFQEPA---LLpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50949876 884 VLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 935
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
754-938 |
5.03e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 107.13 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISE---VHQNMGYCPQFDAIDELLTGREHLYL--Y 828
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPPherARAGIGYVPEGRRIFPELTVEENLLLgaY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 ARLRGVPAEEIEKVanwsikslgltvYA---------DCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 899
Cdd:cd03224 102 ARRRAKRKARLERV------------YElfprlkerrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 50949876 900 MLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03224 170 EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
731-935 |
1.10e-25 |
|
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: 106.08 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 731 RLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVHQNMGYCP 810
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 811 QFDAIDEL--LTGRE--HLYLYAR---LRGVPAEEIEKVANwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 883
Cdd:cd03235 75 QRRSIDRDfpISVRDvvLMGLYGHkglFRRLSKADKAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 50949876 884 VLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIM 935
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
754-940 |
1.30e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.67 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQ----FDAidellTGREHLYLY 828
Cdd:COG4619 23 LEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQepalWGG-----TVRDNLPFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 ARLRGVPAEEiEKVANWsIKSLGLTvyADCL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVI 905
Cdd:COG4619 98 FQLRERKFDR-ERALEL-LERLGLP--PDILdkpVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELL 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 50949876 906 VSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAF 940
Cdd:COG4619 174 REYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
754-920 |
7.31e-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: 103.89 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTG---DTTVTSGDATVAGKSIltNISEVHQNMGYCPQFDAIDELLTGREHLYLYAR 830
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 LRG---VPAEEIEK-VANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPqarrMLWNVIV 906
Cdd:cd03234 108 LRLprkSSDAIRKKrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTALNLV 183
|
170
....*....|....*...
gi 50949876 907 SII----REGRAVVLTSH 920
Cdd:cd03234 184 STLsqlaRRNRIVILTIH 201
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
745-938 |
1.11e-24 |
|
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: 103.95 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 745 PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTNISEVhqnMGYCPQ--FDai 815
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrKKFLRRIGVV---FGQKTQlwWD-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 816 delLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 895
Cdd:cd03267 110 ---LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50949876 896 QARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03267 187 VAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
729-938 |
1.16e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISeVHQ-NMG 807
Cdd:COG3842 5 ALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLP-PEKrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 808 YCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNK-RklsTAIA--LIGCPPLV 884
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VALAraLAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 885 LLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
730-944 |
1.63e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 102.72 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISEVH 803
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 QNMGYCPQfdaidelLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPL 883
Cdd:cd03301 79 QNYALYPH-------MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 884 VLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMG 944
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
705-949 |
6.89e-24 |
|
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: 107.54 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 705 PIVDEDDDVAEERQRIITggNKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVT 784
Cdd:COG4987 311 ELLDAPPAVTEPAEPAPA--PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 785 SGDATVAGKSILT-NISEVHQNMGYCPQ----FDAidellTGREHLyLYARlrgvPA---EEIEKV------ANWsIKSL 850
Cdd:COG4987 389 SGSITLGGVDLRDlDEDDLRRRIAVVPQrphlFDT-----TLRENL-RLAR----PDatdEELWAAlervglGDW-LAAL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 851 --GLtvyaDCLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEE 924
Cdd:COG4987 458 pdGL----DTWLGeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAG 532
|
250 260
....*....|....*....|....*
gi 50949876 925 CEAlCTRLAIMVKGAFRCMGTIQHL 949
Cdd:COG4987 533 LER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
754-938 |
1.60e-23 |
|
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: 100.93 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSG-DATVAGKSI-LTNISEVHQNMGYC-----PQFD----AIDELLTGr 822
Cdd:COG1119 26 VKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLVspalqLRFPrdetVLDVVLSG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 823 ehlyLYA---RLRGVPAEEIEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 899
Cdd:COG1119 105 ----FFDsigLYREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50949876 900 MLWNVIVSIIREG-RAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG1119 180 LLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
729-923 |
1.67e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.13 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGtSSPAVDRLCVGVRPGE-CFgLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNIS--EVH-- 803
Cdd:COG2884 1 MIRFENVSKRYPG-GREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-LSRLKrrEIPyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 -QNMGYCPQfdaiD-ELLTGR---EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALI 878
Cdd:COG2884 78 rRRIGVVFQ----DfRLLPDRtvyENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 50949876 879 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 923
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
746-954 |
1.90e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 103.28 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTfkmlTGDTTVTSGDATVAGKSILT---NISEVHQNMG-YCPQFDAIDELLTG 821
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG----ALPAHV*GPDAGRRPWRF*TwcaNRRALRRTIG*HRPVR*GRRESFSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 822 REHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 901
Cdd:NF000106 104 RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50949876 902 WNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFG 954
Cdd:NF000106 184 WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
727-923 |
1.14e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 97.81 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 727 TDILRLHELTKIYP--GTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEV-- 802
Cdd:COG1136 2 SPLLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-SSLSERel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 803 ----HQNMGYCPQ-FDAIDELlTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIAL 877
Cdd:COG1136 81 arlrRRHIGFVFQfFNLLPEL-TALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 50949876 878 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSME 923
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
754-950 |
1.62e-22 |
|
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: 97.74 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISE-----VHQNMGYCPQFDAideLLTG------- 821
Cdd:COG1127 28 VPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI-TGLSEkelyeLRRRIGMLFQGGA---LFDSltvfenv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 822 ----REHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 897
Cdd:COG1127 104 afplREH-------TDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPIT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 898 RRmlwnVIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 950
Cdd:COG1127 177 SA----VIDELIRElrdelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
727-951 |
2.55e-22 |
|
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: 96.97 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 727 TDILRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE--VHQ 804
Cdd:COG0410 1 MPMLEVENLHAGYGG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 805 NMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVAnwsikslglTVYA---------DCLAGTYSGGNKRKLSTAI 875
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLE---------RVYElfprlkerrRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 876 ALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKS 951
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
754-950 |
3.09e-22 |
|
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: 96.80 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS----EVHQNMGYCPQFDAIDELLTGREH--LYL 827
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyRLRRRMGMLFQSGALFDSLTVFENvaFPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 828 YARLRGvPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNVIVS 907
Cdd:cd03261 103 REHTRL-SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS----GVIDD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 50949876 908 IIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLK 950
Cdd:cd03261 178 LIRSlkkelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
754-920 |
1.00e-21 |
|
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: 93.85 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTT--VTSGDATVAGKSILTNISEVhqnMGYCPQFDAIDELLTGREHLYLYARL 831
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 832 RGVPAEEiekvanwsikslgltvyadclagtysggnKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE 911
Cdd:cd03232 107 RGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
....*....
gi 50949876 912 GRAVVLTSH 920
Cdd:cd03232 158 GQAILCTIH 166
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
730-945 |
1.20e-21 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 92.88 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisevhqnmgyc 809
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 pQFDAIDElltgrehlylyARLRGVpaeeiekvanwsikslgLTVYadclagTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03216 65 -SFASPRD-----------ARRAGI-----------------AMVY------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 890 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafRCMGT 945
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
727-946 |
1.26e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 727 TDILRLHELTKIYPGTSSP--------------------AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSG 786
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 787 DATVAGK--SILtnisEVhqNMGYCPQfdaidelLTGREHLYLYARLRGVPAEEIEK----VANWSikslGLTVYADCLA 860
Cdd:COG1134 82 RVEVNGRvsALL----EL--GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEkfdeIVEFA----ELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 861 GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP--QAR---RMLwnvivSIIREGRAVVLTSHSMEECEALCTRLAIM 935
Cdd:COG1134 145 KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafQKKclaRIR-----ELRESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|.
gi 50949876 936 VKGAFRCMGTI 946
Cdd:COG1134 220 EKGRLVMDGDP 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
754-938 |
1.42e-21 |
|
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: 94.52 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGK-SILTNIsevhqNMGYCPQfdaidelLTGREHLYLYARLR 832
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvSSLLGL-----GGGFNPE-------LTGRENIYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 833 GVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREG 912
Cdd:cd03220 113 GLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQG 192
|
170 180
....*....|....*....|....*.
gi 50949876 913 RAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03220 193 KTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
754-983 |
1.58e-21 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 95.40 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------------NISEVHQNMGYCPQFDAIDELLTG 821
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelrelrrkKISMVFQSFALLPHRTVLENVAFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 822 REhlylyarLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 901
Cdd:cd03294 127 LE-------VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 902 WNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLkskfgdgyivtmkIKSPKDDLlpdlnpVEQF 980
Cdd:cd03294 200 QDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI-------------LTNPANDY------VREF 260
|
...
gi 50949876 981 FQG 983
Cdd:cd03294 261 FRG 263
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
729-945 |
2.50e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.19 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGK--SILTNISEVHQNM 806
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQFDAIDELLTGREHLYLYARLR-GVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 885
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 886 LDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
730-938 |
4.13e-21 |
|
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: 91.86 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILtnisevhqnmgyc 809
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 pqfDAIDELLTGREHL-YLYARLRGVPaeeiekvanwsikslGLTVYADCLAGtYSGGNKRKLSTAIALIGCPPLVLLDE 888
Cdd:cd03229 66 ---DLEDELPPLRRRIgMVFQDFALFP---------------HLTVLENIALG-LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 50949876 889 PTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
731-940 |
4.26e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 92.71 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 731 RLHELTKIYPGTSSpAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-----LTNISEVHQN 805
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCPQFDaidellTGREHLYLYARLRGVPAEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 885
Cdd:cd03226 80 VDYQLFTD------SVREELLLGLKELDAGNEQAETV----LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 886 LDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 940
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
745-920 |
4.73e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 92.04 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 745 PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREH 824
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 825 LYLYARLRGVPAEEIEKvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 904
Cdd:TIGR01189 94 LHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*.
gi 50949876 905 IVSIIREGRAVVLTSH 920
Cdd:TIGR01189 170 LRAHLARGGIVLLTTH 185
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
730-938 |
5.21e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 93.40 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----------N 798
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkalrqlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 799 ISEVHQNMGYCPQFDAIDELLTGR--EHLYLYARLRGVPAEEIEKvANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIA 876
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 877 LIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
731-938 |
6.14e-21 |
|
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: 91.34 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 731 RLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYC 809
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQfdaidelltgrehlylyarlrgvpaeeiekvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 50949876 890 TTGMDP--QARRMlwNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03214 125 TSHLDIahQIELL--ELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
739-938 |
6.49e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 92.27 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 739 YPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQNMGYCPQfDAidE 817
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRNIGYVPQ-DV--T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 818 LLTG--REHLYLYARLrgVPAEEIEKVANWSikslGLTVYADCLAGTY-----------SGGNKRKLSTAIALIGCPPLV 884
Cdd:cd03245 89 LFYGtlRDNITLGAPL--ADDERILRAAELA----GVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 885 LLDEPTTGMDPQARRMLWNVIVSIIReGRAVVLTSH--SMEEceaLCTRLAIMVKG 938
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHrpSLLD---LVDRIIVMDSG 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
754-940 |
6.86e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 91.34 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQN-MGYCPQfDAIDELLtgrehlylyarl 831
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAgIAYVPE-DRKREGL------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 832 rgvpaeeiekVANWSIKS-LGLTVYadclagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIR 910
Cdd:cd03215 90 ----------VLDLSVAEnIALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
170 180 190
....*....|....*....|....*....|
gi 50949876 911 EGRAVVLTSHSMEECEALCTRLAIMVKGAF 940
Cdd:cd03215 153 AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
730-938 |
1.67e-20 |
|
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: 90.30 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSPAVDRLCVGV----RPGECFGLLGVSGAGKTTTFKMLTGDTTV--TSGDATVAGKSIltNISEVH 803
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLLKNVsgkaKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL--DKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 QNMGYCPQFDAIDELLTGREHLYLYARLRGVpaeeiekvanwsikslgltvyadclagtySGGNKRKLSTAIALIGCPPL 883
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 884 VLLDEPTTGMDP-QARRmlwnvIVSIIR----EGRAVVLTSHSM-EECEALCTRLAIMVKG 938
Cdd:cd03213 133 LFLDEPTSGLDSsSALQ-----VMSLLRrladTGRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
754-952 |
3.51e-20 |
|
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: 90.86 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRG 833
Cdd:cd03299 22 VERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 834 VPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGR 913
Cdd:cd03299 101 VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50949876 914 AVVL-TSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSK 952
Cdd:cd03299 181 VTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
754-938 |
7.55e-20 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 95.95 E-value: 7.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTT---VTSGDATVAGKSILTNISevhQNMGYCPQFDAIDELLTGREHLYLYAR 830
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 LR---GVPAEE----IEKVanwsIKSLGLTVYADCLAGTYSGG----NKRKLSTAIALIGCPPLVL-LDEPTTGMDPQAR 898
Cdd:TIGR00956 863 LRqpkSVSKSEkmeyVEEV----IKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 50949876 899 rmlWnVIVSIIRE----GRAVVLTSHS-----MEECEalctRLAIMVKG 938
Cdd:TIGR00956 939 ---W-SICKLMRKladhGQAILCTIHQpsailFEEFD----RLLLLQKG 979
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
729-935 |
8.48e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISE------ 801
Cdd:COG1129 4 LLEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrFRSPRDaqaagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 802 --VHQNMGYCPQFDAIDELLTGRE----HLYLYARLRgvpaEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAI 875
Cdd:COG1129 82 aiIHQELNLVPNLSVAENIFLGREprrgGLIDWRAMR----RRAREL----LARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 876 ALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIM 935
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
704-954 |
1.35e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 94.52 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 704 EPIVDEDDDVAEERQRIITGGNKTDIlRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTV 783
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 784 TSGDATVAGKSILT-NISEVHQNMGYCPQfDaiDELLTG--REHLYLYArlRGVPAEEIEKVANWS-----IKSL--GL- 852
Cdd:COG2274 528 TSGRILIDGIDLRQiDPASLRRQIGVVLQ-D--VFLFSGtiRENITLGD--PDATDEEIIEAARLAglhdfIEALpmGYd 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 853 TVYADcLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIReGRAVVLTSHSMeECEALCTRL 932
Cdd:COG2274 603 TVVGE-GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRI 679
|
250 260
....*....|....*....|..
gi 50949876 933 AIMVKGAFRCMGTIQHLKSKFG 954
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKG 701
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
746-945 |
1.64e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.28 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFD---------AID 816
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQhvrlfremtVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 817 ELLTGrEHLYLYARL----------RGVPAEEIEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:PRK11300 100 NLLVA-QHQQLKTGLfsgllktpafRRAESEALDRAATW-LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
730-938 |
1.77e-19 |
|
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: 86.67 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGY 808
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQfdaidelltgreHLYLYARlrgvpaeeiekvanwSIKSLGLtvyadclagtySGGNKRKLSTAIALIGCPPLVLLDE 888
Cdd:cd03228 81 VPQ------------DPFLFSG---------------TIRENIL-----------SGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 50949876 889 PTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEaLCTRLAIMVKG 938
Cdd:cd03228 123 ATSALDPETEALILEALRA-LAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
755-956 |
2.06e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.57 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 755 RPGECFGLLGVSGAGKTT-----TFKMLTGdtTVTSGDATVAGKSIltNISEVHQNMGYCPQFDAIDELLTGREHLYLYA 829
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 830 RLR---GVPAEE-IEKVANwSIKSLGLTVYADCLAGT------YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 899
Cdd:TIGR00955 125 HLRmprRVTKKEkRERVDE-VLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 50949876 900 MLWNVIVSIIREGRAVVLTSH--SMEECEaLCTRLAIMVKGAFRCMGTIQHLKSKFGDG 956
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDL 261
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
674-940 |
2.28e-19 |
|
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: 92.94 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 674 MVVEGVVYFLLTLLVQRHFflSQWIAEPTKEPIVDEDDDVAE------------------ERQRIITGGNktDILRLHEL 735
Cdd:TIGR03269 210 ALEEAVKASGISMVLTSHW--PEVIEDLSDKAIWLENGEIKEegtpdevvavfmegvsevEKECEVEVGE--PIIKVRNV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 736 TKIYPGTSS---PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSG-----------DAT---VAGKSILTN 798
Cdd:TIGR03269 286 SKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvDMTkpgPDGRGRAKR 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 799 -ISEVHQNMGYCPQFDAIDELL--TGREHLYLYARLRGVpaeeiekvanWSIKSLGLT-VYA----DCLAGTYSGGNKRK 870
Cdd:TIGR03269 366 yIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAV----------ITLKMVGFDeEKAeeilDKYPDELSEGERHR 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 871 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAF 940
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
730-939 |
2.64e-19 |
|
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: 86.50 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQNMGY 808
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQfDaiDELLTgrehlylyarlrGVPAEEIekvanwsikslgltvyadclagtYSGGNKRKLSTAIALIGCPPLVLLDE 888
Cdd:cd03246 81 LPQ-D--DELFS------------GSIAENI-----------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 50949876 889 PTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGA 939
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
729-935 |
2.99e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 87.87 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYP-----GTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATV--AGKSI-LTNIS 800
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 801 EVH------QNMGYCPQF----------DAIDELLtgrehlylyaRLRGVPAEE-IEKVANWsIKSLGL-----TVYAdc 858
Cdd:COG4778 84 PREilalrrRTIGYVSQFlrviprvsalDVVAEPL----------LERGVDREEaRARAREL-LARLNLperlwDLPP-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 859 laGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwnVIVSIIRE----GRAVVLTSHSMEECEALCTRLAI 934
Cdd:COG4778 151 --ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA----VVVELIEEakarGTAIIGIFHDEEVREAVADRVVD 224
|
.
gi 50949876 935 M 935
Cdd:COG4778 225 V 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
733-938 |
8.01e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 733 HELTKIYPGTSSPA------VDRLCVG---------VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-L 796
Cdd:COG1129 239 RELEDLFPKRAAAPgevvleVEGLSVGgvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 797 TNISE-VHQNMGYCPQfdaiDELLTG-------REHLYL-----YARLRGVPAEEIEKVANWSIKSLGL-TVYADCLAGT 862
Cdd:COG1129 319 RSPRDaIRAGIAYVPE----DRKGEGlvldlsiRENITLasldrLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGN 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 863 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
748-920 |
1.00e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.63 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 748 DRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYL 827
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 828 YARLRGVPAEEiekvANWSI-KSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIV 906
Cdd:PRK13538 98 YQRLHGPGDDE----ALWEAlAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
170
....*....|....
gi 50949876 907 SIIREGRAVVLTSH 920
Cdd:PRK13538 174 QHAEQGGMVILTTH 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
730-920 |
1.04e-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: 84.67 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYC 809
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQfdaidelltgREHLYlyarlrgvpaeeiekvaNWSIKS-LGLtvyadclagTYSGGNKRKLSTAIALIGCPPLVLLDE 888
Cdd:cd03247 81 NQ----------RPYLF-----------------DTTLRNnLGR---------RFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190
....*....|....*....|....*....|..
gi 50949876 889 PTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 920
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWITHH 156
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
734-923 |
1.22e-18 |
|
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: 85.54 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 734 ELTKIYPGTSsPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISEVHQNMGYC 809
Cdd:cd03292 5 NVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....
gi 50949876 890 TTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 923
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
732-920 |
1.41e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 732 LHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsilTNISEVHQNMGYCPQ 811
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---LRIGYLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 812 FDAIDELLTGREHLY-LYARLR------GVPAEEIEKVAN----------WSIKS--------LGLT-VYADCLAGTYSG 865
Cdd:COG0488 76 LTVLDTVLDGDAELRaLEAELEeleaklAEPDEDLERLAElqeefealggWEAEAraeeilsgLGFPeEDLDRPVSELSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 866 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiiREGrAVVLTSH 920
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPG-TVLVVSH 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
704-952 |
1.76e-18 |
|
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: 90.59 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 704 EPIVDEDDDVAEERQRIITGGNKTDIlRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTV 783
Cdd:COG4988 312 FALLDAPEPAAPAGTAPLPAAGPPSI-ELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 784 TSGDATVAGKSiLTNISE--VHQNMGYCPQFDAideLLTG--REHLYLYArlRGVPAEEIEKVAnwsiKSLGLTVYADCL 859
Cdd:COG4988 390 YSGSILINGVD-LSDLDPasWRRQIAWVPQNPY---LFAGtiRENLRLGR--PDASDEELEAAL----EAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 860 AGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECeAL 928
Cdd:COG4988 460 PDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALL-AQ 537
|
250 260
....*....|....*....|....
gi 50949876 929 CTRLAIMVKGAFRCMGTIQHLKSK 952
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
743-938 |
2.37e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.53 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 743 SSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISEVHQNMGYC-------PQF 812
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVfqqfylfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 813 DAIDELLTGRehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 892
Cdd:PRK09493 93 TALENVMFGP------LRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50949876 893 MDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
735-946 |
3.98e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.87 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 735 LTKIY-PGT--SSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISEVHQNMG- 807
Cdd:PRK13637 8 LTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkVKLSDIRKKVGl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 808 ---YcPQFDAIDEllTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLT--VYADCLAGTYSGGNKRKLSTAIALIGCPP 882
Cdd:PRK13637 88 vfqY-PEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 883 LVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTI 946
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
729-969 |
5.40e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.75 E-value: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE---VHQN 805
Cdd:PRK11248 1 MLQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCPQFDAIDELLTGREhlylyarLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 885
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQ-------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 886 LDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMgtiQHLKSKFGDGYIVTMKIK 964
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRFVAGESSR 228
|
....*
gi 50949876 965 SPKDD 969
Cdd:PRK11248 229 SIKSD 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
725-947 |
5.99e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 725 NKTDILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTN---- 798
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHklaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 799 ---ISEVHQnmgycpQFDAIDELlTGREHLY----LYARLRGVPA---EEIEKVANWSIKSLGLTVYADCLAGTYSGGNK 868
Cdd:PRK09700 79 qlgIGIIYQ------ELSVIDEL-TVLENLYigrhLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949876 869 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQ 947
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
739-924 |
6.41e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 739 YPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILtnisevhqnmGYCPQFDAIDEL 818
Cdd:NF040873 2 YGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV----------AYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 819 L--TGRE--------HLYLYARLRGVPAEEIEKvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 888
Cdd:NF040873 70 LplTVRDlvamgrwaRRGLWRRLTRDDRAAVDD----ALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 50949876 889 PTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEE 924
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
725-949 |
6.47e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.07 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 725 NKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKS--------IL 796
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 797 TNISEVHQNmgycP--QF---DAIDELLTGREHlylyarlRGVPAEE-IEKVaNWSIKSLGLTVYADCLAGTYSGGNKRK 870
Cdd:PRK13635 81 RQVGMVFQN----PdnQFvgaTVQDDVAFGLEN-------IGVPREEmVERV-DQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 871 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLT-SHSMEECeALCTRLAIMVKGAFRCMGTIQHL 949
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
727-958 |
1.30e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.04 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 727 TDILRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEVHQNM 806
Cdd:PRK11607 17 TPLLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949876 887 DEPTTGMDPQAR-RMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT----IQHLKSKFGDGYI 958
Cdd:PRK11607 174 DEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
730-935 |
1.57e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.76 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSS--PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE---VHQ 804
Cdd:COG4525 4 LTVRHVSVRYPGGGQpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgvVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 805 NMGYCPQFDAIDELLTGrehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLV 884
Cdd:COG4525 84 KDALLPWLNVLDNVAFG-------LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 885 LLDEPTTGMDPQAR-RM------LWNvivsiiREGRAVVLTSHSMEECEALCTRLAIM 935
Cdd:COG4525 157 LMDEPFGALDALTReQMqellldVWQ------RTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
754-938 |
1.65e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.19 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISEVHQNMGYCPQfdaidelltgreHLYLYAR 830
Cdd:cd03262 23 VKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVGMVFQ------------QFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 L-------------RGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 897
Cdd:cd03262 91 LtvlenitlapikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 50949876 898 RRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03262 171 VGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
730-921 |
2.58e-17 |
|
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: 86.65 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGY 808
Cdd:TIGR02868 335 LELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQ----FDAidellTGREHLYLyARlRGVPAEEIEKV------ANWsIKSL--GLTVYADCLAGTYSGGNKRKLSTAIA 876
Cdd:TIGR02868 414 CAQdahlFDT-----TVRENLRL-AR-PDATDEELWAAlervglADW-LRALpdGLDTVLGEGGARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 50949876 877 LIGCPPLVLLDEPTTGMDPQAR----RMLWNVIvsiirEGRAVVLTSHS 921
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETAdellEDLLAAL-----SGRTVVLITHH 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
730-923 |
4.54e-17 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 85.80 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSsPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISE--VHQNMG 807
Cdd:TIGR02857 322 LEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADADAdsWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 808 YCPQ----FDAidellTGREHLYLYArlRGVPAEEIEKV-----ANWSIKSLGL---TVYADCLAGtYSGGNKRKLSTAI 875
Cdd:TIGR02857 400 WVPQhpflFAG-----TIAENIRLAR--PDASDAEIREAleragLDEFVAALPQgldTPIGEGGAG-LSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 50949876 876 ALIGCPPLVLLDEPTTGMDPQARrmlwNVIVSIIRE---GRAVVLTSHSME 923
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETE----AEVLEALRAlaqGRTVLLVTHRLA 518
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
757-920 |
6.34e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.23 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGvpA 836
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHS--D 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 837 EEIEKvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVV 916
Cdd:cd03231 104 EQVEE----ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVV 179
|
....
gi 50949876 917 LTSH 920
Cdd:cd03231 180 LTTH 183
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
744-960 |
1.18e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.54 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 744 SPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------------NISEVHQNMGYCPQ 811
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrevrrkKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 812 FDAIDELLTGREhlylyarLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 891
Cdd:PRK10070 121 MTVLDNTAFGME-------LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 892 GMDPQARRMLWNVIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGDGYIVT 960
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
754-946 |
2.09e-16 |
|
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: 79.82 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE---VHQNMGYCPqfdaideLLTGREHLYLYAR 830
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvVFQNYSLLP-------WLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 --LRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI 908
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 50949876 909 IREGR-AVVLTSHSMEECEALCTRLAIMVKGAFRCMGTI 946
Cdd:TIGR01184 161 WEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
730-938 |
2.69e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 79.15 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKiYPGTSSpAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILT---NISE 801
Cdd:cd03260 1 IELRDLNV-YYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldvDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 802 VHQNMGYCPQ----FDAidellTGREHLYLYARLRGV-PAEEIEKVANWSIKSLGLT--VYADCLAGTYSGGNKRKLSTA 874
Cdd:cd03260 79 LRRRVGMVFQkpnpFPG-----SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWdeVKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50949876 875 IALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
741-945 |
2.89e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.52 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 741 GTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAG--KSILTNISEVHQNMGYCPQ------F 812
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDIRNKAGMVFQnpdnqiV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 813 DAIDE--LLTGREHLylyarlrGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 890
Cdd:PRK13633 100 ATIVEedVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 891 TGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECeALCTRLAIMVKGAFRCMGT 945
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
729-935 |
3.61e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 80.87 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTG---DTTVTSGDATVAGKSILT------ 797
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 798 ------NISEVHQN-MGYC-PQF---DAIDELLtgREHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADcLAGTY--- 863
Cdd:COG0444 81 rkirgrEIQMIFQDpMTSLnPVMtvgDQIAEPL--RIH-------GGLSKAEARERAIELLERVGLPDPER-RLDRYphe 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 864 -SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP--QARRMlwNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 935
Cdd:COG0444 151 lSGGMRQRVMIARALALEPKLLIADEPTTALDVtiQAQIL--NLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
735-945 |
4.16e-16 |
|
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: 78.92 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 735 LTKIYPgtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEVHQNMGYCPQFDA 814
Cdd:cd03296 8 VSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 815 IDELLTGREH----LYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 890
Cdd:cd03296 85 LFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 891 TGMDPQARRML--WnvivsiIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:cd03296 165 GALDAKVRKELrrW------LRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
707-939 |
9.54e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 707 VDEDDDVAE-ERQRIIT---GGNKTDI------------LRLHELTKiyPGTSSPAvdrlCVGVRPGECFGLLGVSGAGK 770
Cdd:PRK11288 219 VATFDDMAQvDRDQLVQamvGREIGDIygyrprplgevrLRLDGLKG--PGLREPI----SFSVRAGEIVGLFGLVGAGR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 771 TTTFKMLTGDTTVTSGDATVAGKSILTN--ISEVHQNMGYCPQ---FDAIDELLTGREHLYLYARLRGVPAEEI------ 839
Cdd:PRK11288 293 SELMKLLYGATRRTAGQVYLDGKPIDIRspRDAIRAGIMLCPEdrkAEGIIPVHSVADNINISARRHHLRAGCLinnrwe 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 840 EKVANWSIKSLGL-TVYADCLAGTYSGGNKRK------LSTAIALIgcpplvLLDEPTTGMDPQARRMLWNVIVSIIREG 912
Cdd:PRK11288 373 AENADRFIRSLNIkTPSREQLIMNLSGGNQQKailgrwLSEDMKVI------LLDEPTRGIDVGAKHEIYNVIYELAAQG 446
|
250 260
....*....|....*....|....*..
gi 50949876 913 RAVVLTSHSMEECEALCTRLAIMVKGA 939
Cdd:PRK11288 447 VAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
729-938 |
1.16e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTNI 799
Cdd:COG3845 5 ALELRGITKRFGGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 800 SEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVAnwsiKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 879
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELS----ERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 50949876 880 CPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
754-945 |
1.70e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTNISEVHQNMGYCPQF--------DAIDELLT 820
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpesqlfeeTVLKDVAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 821 GREHLylyarlrGVPAEEIEKVANWSIKSLGLTV-YADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 899
Cdd:PRK13643 109 GPQNF-------GIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50949876 900 MLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
729-932 |
1.78e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.43 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTkiYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTniSEVHQNMGY 808
Cdd:PRK13543 11 LLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--GDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVAnwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 888
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50949876 889 PTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRL 932
Cdd:PRK13543 164 PYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
730-945 |
2.18e-15 |
|
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: 80.56 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGY 808
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQfdaiD-ELLTG--REHLylyARLRGVPAEEIEKVAnwsiKSLGL------------TVYADclAGTY-SGGNKRKLS 872
Cdd:COG4618 411 LPQ----DvELFDGtiAENI---ARFGDADPEKVVAAA----KLAGVhemilrlpdgydTRIGE--GGARlSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 873 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMeecEAL--CTRLAIMVKGAFRCMGT 945
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFGP 549
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
731-938 |
3.76e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.92 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 731 RLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISE-----VH 803
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQD-LTALSEkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 QNMGYCPQ-FDaideLLTGR---EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADclagTY----SGGNKRKLSTAI 875
Cdd:PRK11153 82 RQIGMIFQhFN----LLSSRtvfDNVALPLELAGTPKAEIKARVTELLELVGLSDKAD----RYpaqlSGGQKQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 876 ALiGCPPLVLL-DEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK11153 154 AL-ASNPKVLLcDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
730-934 |
4.23e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTNIS 800
Cdd:PRK11288 5 LSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 801 EVHQNMGYCPQFDAIDELLTGRehlyLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 880
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQ----LPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 50949876 881 PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAI 934
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
729-945 |
6.87e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 76.27 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYP-GTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS---EVHQ 804
Cdd:PRK13639 1 ILETRDLKYSYPdGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 805 NMGYCPQfDAIDELL--TGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPP 882
Cdd:PRK13639 79 TVGIVFQ-NPDDQLFapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 883 LVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
756-938 |
1.09e-14 |
|
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: 74.25 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 756 PGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAG-------KSIltNISEVHQNMGYCPQFDAIDELLTGREHLyLY 828
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKI--NLPPQQRKIGLVFQQYALFPHLNVRENL-AF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 ArLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI 908
Cdd:cd03297 99 G-LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|.
gi 50949876 909 IRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03297 178 KKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
729-951 |
1.43e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPgTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISEVHQNM 806
Cdd:PRK13644 1 MIRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYC---PQFDAI-----DELLTGREHLYLyarlrgvPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALI 878
Cdd:PRK13644 80 GIVfqnPETQFVgrtveEDLAFGPENLCL-------PPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 879 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFRCMGTIQHLKS 951
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
743-938 |
1.80e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 743 SSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------------ISE--------- 801
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangivyISEdrkrdglvl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 802 ---VHQNMGYCpqfdAIDELLtgrehlYLYARLRGvpAEEIEKVANW----SIKslglTVYADCLAGTYSGGNKRKLSTA 874
Cdd:PRK10762 344 gmsVKENMSLT----ALRYFS------RAGGSLKH--ADEQQAVSDFirlfNIK----TPSMEQAIGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50949876 875 IALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
729-938 |
2.18e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.19 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYpgtsspAVDRLCVGV----RPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKS----ILTNIS 800
Cdd:PRK11701 6 LLSVRGLTKLY------GPRKGCRDVsfdlYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 801 E-------------VHQN--MGYCPQFDA---IDELL--TGREHlylYARLRGVPAEEIEKVanwSIKSLGLtvyaDCLA 860
Cdd:PRK11701 80 EaerrrllrtewgfVHQHprDGLRMQVSAggnIGERLmaVGARH---YGDIRATAGDWLERV---EIDAARI----DDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 861 GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD--PQARrmLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVK 937
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR--LLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
.
gi 50949876 938 G 938
Cdd:PRK11701 228 G 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
728-932 |
2.49e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 728 DILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisevhqNMG 807
Cdd:COG0488 314 KVLELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 808 YCPQ-FDAIDELLTGREHLYLYAR------LRGV------PAEEIEKvanwSIKSLgltvyadclagtySGGNKRKLSTA 874
Cdd:COG0488 382 YFDQhQEELDPDKTVLDELRDGAPggteqeVRGYlgrflfSGDDAFK----PVGVL-------------SGGEKARLALA 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 875 IALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIirEGrAVVLTSHSMEECEALCTRL 932
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRI 499
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
761-926 |
2.65e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 761 GLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILtniSEVHQN-----MGYCPQfdaidEL-------LTGREHLYLY 828
Cdd:NF033858 31 GLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DARHRRavcprIAYMPQ-----GLgknlyptLSVFENLDFF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 ARLRGVPAEEIEkvanWSIKSL----GLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 904
Cdd:NF033858 103 GRLFGQDAAERR----RRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWEL 178
|
170 180
....*....|....*....|....*.
gi 50949876 905 IVSiIREGRA----VVLTSHsMEECE 926
Cdd:NF033858 179 IDR-IRAERPgmsvLVATAY-MEEAE 202
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
726-945 |
2.70e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.75 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 726 KTDILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEVHQN 805
Cdd:PRK09452 11 LSPLVELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVL 885
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 886 LDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
762-949 |
3.74e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 762 LLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISEVHQNMGYCPQfDAIDELL--TGREHLYLYARLRGVPAEE 838
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVGLVFQ-NPDDQIFspTVEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 839 IEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVL 917
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIF 193
|
170 180 190
....*....|....*....|....*....|..
gi 50949876 918 TSHSMEECEALCTRLAIMVKGAFRCMGTIQHL 949
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
754-938 |
4.23e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISEVHQNMGYCPQfdaiDELLTGrehLYLYARL 831
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPE----DRQSSG---LYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 832 R-----------GV---PAEEIEKVANWSiKSLGLTV-YADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 896
Cdd:PRK15439 359 AwnvcalthnrrGFwikPARENAVLERYR-RALNIKFnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 50949876 897 ARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
729-940 |
7.42e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 7.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---------I 799
Cdd:PRK10762 4 LLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkssqeagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 800 SEVHQNMGYCPQFDAIDELLTGREhlyLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 879
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGRE---FVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 880 CPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 940
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
743-978 |
8.33e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 743 SSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQNMGYCPQFDAIDELLTG 821
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 822 RE--------HLYLYARLrgvpAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 893
Cdd:PRK09536 95 RQvvemgrtpHRSRFDTW----TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 894 D-PQARRMLwNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMG------TIQHLKSKFGDGYIVTMK--IK 964
Cdd:PRK09536 171 DiNHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAFDARTAVGTDpaTG 249
|
250
....*....|....
gi 50949876 965 SPKDDLLPDLNPVE 978
Cdd:PRK09536 250 APTVTPLPDPDRTE 263
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
729-945 |
1.59e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS--EVHQNM 806
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI-SMLSsrQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQFDAIDELLTGRE--------HLYLYARLrgvpAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALI 878
Cdd:PRK11231 79 ALLPQHHLTPEGITVRElvaygrspWLSLWGRL----SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949876 879 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
729-972 |
1.73e-13 |
|
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: 74.48 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTG--DTTVTSGDATVAGKSILTN-------- 798
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASnirdtera 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 799 -ISEVHQNMGYCPQFDAIDELLTGREhLYLYARLRGVP-----AEEIEKVANWSIKSLGLTVyadclaGTYSGGNKRKLS 872
Cdd:TIGR02633 79 gIVIIHQELTLVPELSVAENIFLGNE-ITLPGGRMAYNamylrAKNLLRELQLDADNVTRPV------GDYGGGQQQLVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 873 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafrcmgtiQHLKSK 952
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--------QHVATK 223
|
250 260
....*....|....*....|....
gi 50949876 953 FGDGY----IVTMKIKSPKDDLLP 972
Cdd:TIGR02633 224 DMSTMseddIITMMVGREITSLYP 247
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
729-938 |
2.04e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.80 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISE----- 801
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSErelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 802 VHQNMGYCPQfdaidelltgreHLYLYAR----------LR--GVPAEEIEKVANWSIKSLGLTVYADclagTY----SG 865
Cdd:COG1135 80 ARRKIGMIFQ------------HFNLLSSrtvaenvalpLEiaGVPKAEIRKRVAELLELVGLSDKAD----AYpsqlSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50949876 866 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENG 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
750-921 |
2.46e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 750 LCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIltNISEVHQNMGYCPQFDAIDELLTGREHLYLYA 829
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 830 RLRGVPAEEIEKvanwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 909
Cdd:PRK13539 99 AFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHL 174
|
170
....*....|..
gi 50949876 910 REGRAVVLTSHS 921
Cdd:PRK13539 175 AQGGIVIAATHI 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
726-926 |
2.48e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.75 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 726 KTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTG--------DTTVTSGDATVAGKSILt 797
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVW- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 798 NISE----VHQNmgycP--QFDAI---DELLTGREHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNK 868
Cdd:PRK13640 81 DIREkvgiVFQN----PdnQFVGAtvgDDVAFGLEN-------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 869 RKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNVIVSIIRE-----GRAVVLTSHSMEECE 926
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKlkkknNLTVISITHDIDEAN 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
729-938 |
8.86e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 8.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKI-YPGTSS--PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTN------- 798
Cdd:COG1101 1 MLELKNLSKTfNPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKlpeykra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 799 --ISEVHQN--MGYCPQfdaidelLTGREHLYL-YAR-----LR-GVPAEEIEKVANW-SIKSLGLTVYADCLAGTYSGG 866
Cdd:COG1101 80 kyIGRVFQDpmMGTAPS-------MTIEENLALaYRRgkrrgLRrGLTKKRRELFRELlATLGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 867 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRavvLTS----HSMEECEALCTRLAIMVKG 938
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEG 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
754-941 |
8.99e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEVH------QNMGYCPQFDAIDELLTGREHLYL 827
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 828 YARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVS 907
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 50949876 908 IIRE-GRAVVLTSHSmEECEALCTRLAIMVKGAFR 941
Cdd:PRK10584 192 LNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
745-938 |
1.07e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 745 PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTN-------------ISEVHQNMGYCPQ 811
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGlsprerrrlgvayIPEDRLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 812 FDAIDELLTGREHLYLYAR---LRGVPAEEI--EKVANWSIKSLGltvyADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:COG3845 351 MSVAENLILGRYRRPPFSRggfLDRKAIRAFaeELIEEFDVRTPG----PDTPARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
755-938 |
1.16e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 72.57 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 755 RPGECFGLLGVSGAGKTTTFKMLTGDTT--VTSGDATVAG----KSILTNISevhqnmGYCPQFDAIDELLTGREHLYLY 828
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkQETFARIS------GYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 ARLR---GVPAEEIEKVANWSIKSLGLTVYADCLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 900
Cdd:PLN03140 978 AFLRlpkEVSKEEKMMFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50949876 901 LWNVIVSIIREGRAVVLTSH--SMEECEALcTRLAIMVKG 938
Cdd:PLN03140 1058 VMRTVRNTVDTGRTVVCTIHqpSIDIFEAF-DELLLMKRG 1096
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
761-951 |
1.19e-12 |
|
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: 70.53 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 761 GLLGVSGAGKTTTFKMLTGDTTVTSGDATVAG-------KSILTNIsevHQN-MGYCPQFDAIDELLTGREHLyLYARLR 832
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPP---EKRrIGYVFQEARLFPHLSVRGNL-RYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 833 GVPAEeieKVANWS--IKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIR 910
Cdd:TIGR02142 103 ARPSE---RRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 50949876 911 E-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKS 951
Cdd:TIGR02142 180 EfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
729-952 |
1.30e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.49 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYP-GTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI---LTNISEVHQ 804
Cdd:PRK13636 5 ILKVEELNYNYSdGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 805 NMGYCPQfDAIDELLTGR--EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPP 882
Cdd:PRK13636 83 SVGMVFQ-DPDNQLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 883 LVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSK 952
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
757-948 |
1.37e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAG-----------KSILT---NISEVHQNMGYCPQFDAIDELLTGR 822
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRElrrNVGMVFQQYNLWPHLTVQQNLIEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 823 ehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQarrmLW 902
Cdd:PRK11124 108 ------CRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----IT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 50949876 903 NVIVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQH 948
Cdd:PRK11124 178 AQIVSIIRElaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
727-955 |
2.22e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.60 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 727 TDILRLHELT-KIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGK--------SILT 797
Cdd:PRK13650 2 SNIIEVKNLTfKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 798 NISEVHQNmgycP--QFDAI---DELLTGREHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLS 872
Cdd:PRK13650 82 KIGMVFQN----PdnQFVGAtveDDVAFGLEN-------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 873 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECeALCTRLAIMVKGAFRCMGTIQHLKS 951
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFS 229
|
....
gi 50949876 952 KFGD 955
Cdd:PRK13650 230 RGND 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
756-920 |
3.21e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 756 PGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATvagksILTN----ISEVHQNMGYCPQFDAIDELLTGREHLYLYARL 831
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGT-----ILANnrkpTKQILKRTGFVTQDDILYPHLTVRETLVFCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 832 R---GVPAEEIEKVANWSIKSLGLTVYADCLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 903
Cdd:PLN03211 168 RlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170
....*....|....*..
gi 50949876 904 VIVSIIREGRAVVLTSH 920
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMH 264
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
725-923 |
3.98e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 725 NKTDILRLHELTKIY-PGTSSPAVDR-LCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEV 802
Cdd:PRK11629 1 MNKILLQCDNLCKRYqEGSVQTDVLHnVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-MSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 803 ------HQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIA 876
Cdd:PRK11629 80 akaelrNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 50949876 877 LIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI-IREGRAVVLTSHSME 923
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
729-923 |
4.00e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.84 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYP-GTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVHQNM 806
Cdd:PRK13647 4 IIEVEDLHFRYKdGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 807 GYCPQfDAIDELLTGR--EHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLV 884
Cdd:PRK13647 82 GLVFQ-DPDDQVFSSTvwDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 50949876 885 LLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 923
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVD 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
749-938 |
4.76e-12 |
|
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: 66.36 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 749 RLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------ISEVHQNMGYCPQFDAIDELLTGR 822
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppadrpVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 823 EHlylYARLRGVPAEEIEKVAnwsiKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 902
Cdd:cd03298 96 SP---GLKLTAEDRQAIEVAL----ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 50949876 903 NVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:cd03298 169 DLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
754-938 |
5.80e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE----------------VHQNMGYCPQFDAIDE 817
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirqlrqhvgfVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 818 LLTGRehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 897
Cdd:PRK11264 106 IIEGP------VIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 50949876 898 RRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK11264 180 VGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
757-938 |
6.02e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSilTNiSEVHQNM-GYCPQFDAID---------ELLTGRehlY 826
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP--TR-QALQKNLvAYVPQSEEVDwsfpvlvedVVMMGR---Y 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 827 LYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRK--LSTAIALIGcpPLVLLDEPTTGMDPQ--ARrmlw 902
Cdd:PRK15056 107 GHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRvfLARAIAQQG--QVILLDEPFTGVDVKteAR---- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50949876 903 nvIVSIIR----EGRAVVLTSHSMEECEALCTrLAIMVKG 938
Cdd:PRK15056 181 --IISLLRelrdEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
729-949 |
9.93e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYpgTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFK----MLTGDTTVTS-----GDATVAGKSILTNI 799
Cdd:PRK09984 4 IIRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 800 SEVHQNMGYC-PQFDAIDELlTGREHLYLYArLRGVP---------AEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKR 869
Cdd:PRK09984 82 RKSRANTGYIfQQFNLVNRL-SVLENVLIGA-LGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 870 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQH 948
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
.
gi 50949876 949 L 949
Cdd:PRK09984 240 F 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
756-951 |
1.36e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.80 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 756 PGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-------LTNISEVHQNMGYC-------PQFDAIDELLTG 821
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVfqqynlwPHLTVMENLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 822 RehlylyARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQarrmL 901
Cdd:COG4161 107 P------CKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----I 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 50949876 902 WNVIVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKS 951
Cdd:COG4161 177 TAQVVEIIRElsqtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
730-954 |
2.27e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISE--VHQNMG 807
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 808 YCPQ----FDAidellTGREHLYLYA------RLRGVpaeeIEKVanwsikslGLTVYADCLAG----------TYSGGN 867
Cdd:PRK11160 418 VVSQrvhlFSA-----TLRDNLLLAApnasdeALIEV----LQQV--------GLEKLLEDDKGlnawlgeggrQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 868 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMlwnvIVSIIRE---GRAVVLTSH---SMEECEALCtrlaIMVKGAFR 941
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQ----ILELLAEhaqNKTVLMITHrltGLEQFDRIC----VMDNGQII 552
|
250
....*....|...
gi 50949876 942 CMGTIQHLKSKFG 954
Cdd:PRK11160 553 EQGTHQELLAQQG 565
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
752-952 |
2.38e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.81 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 752 VGVRPGECFGLLGVSGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDaidelltgrEH-L 825
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFP---------EHqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 826 YLYARLR---------GVPAEEIEKVANWSIKSLGLTvyADCLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 893
Cdd:PRK13634 99 FEETVEKdicfgpmnfGVSEEDAKQKAREMIELVGLP--EELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 894 DPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSK 952
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
746-986 |
2.50e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.57 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTNISEVHQNMGYCPQF-------D 813
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllkptTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFpesqlfeD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 814 AID-ELLTGREHLylyarlrGVPAEEIEKVANWSIKSLGLTvyADCLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:PRK13646 102 TVErEIIFGPKNF-------KMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 890 TTGMDPQARRMLWNVIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLkskFGDG-YIVTMKIKSPk 967
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL---FKDKkKLADWHIGLP- 248
|
250
....*....|....*....
gi 50949876 968 dDLLPDLNPVEQFFQGNFP 986
Cdd:PRK13646 249 -EIVQLQYDFEQKYQTKLK 266
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
738-924 |
4.47e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 738 IY-PGTS--SPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-----EVHQNMGYC 809
Cdd:PRK13641 11 IYsPGTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlkKLRKKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFDAIdELL--TGREHLYLYARLRGVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:PRK13641 91 FQFPEA-QLFenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEE 924
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDD 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
725-966 |
5.76e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.24 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 725 NKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEVH 803
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIsKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 QNMGYC---P--QFDAI---DELLTGREHlylyarlRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAI 875
Cdd:PRK13632 83 KKIGIIfqnPdnQFIGAtveDDIAFGLEN-------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 876 ALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLT-SHSMEECeALCTRLAIMVKGAFRCMGTIQH-LKSKf 953
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK- 233
|
250
....*....|...
gi 50949876 954 gdGYIVTMKIKSP 966
Cdd:PRK13632 234 --EILEKAKIDSP 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
762-938 |
6.69e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.38 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 762 LLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-----NISEVHQNMGYCPQF--------DAIDELLTGREHLyly 828
Cdd:PRK13649 38 FIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQFpesqlfeeTVLKDVAFGPQNF--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 arlrGVPAEEIEKVANwsiKSLGLTVYADCLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 904
Cdd:PRK13649 115 ----GVSQEEAEALAR---EKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTL 187
|
170 180 190
....*....|....*....|....*....|....
gi 50949876 905 IVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK13649 188 FKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
729-938 |
7.67e-11 |
|
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: 64.06 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTS-------SPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAG--------- 792
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 793 --KSILTNISEVHQNmgyCPqfDAIDELLTGR----EHLYLYARLRgvPAEEIEKVANWsIKSLGL-TVYADCLAGTYSG 865
Cdd:TIGR02769 82 qrRAFRRDVQLVFQD---SP--SAVNPRMTVRqiigEPLRHLTSLD--ESEQKARIAEL-LDMVGLrSEDADKLPRQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 866 GNKRKLSTAIALIGCPPLVLLDEPTTGMDpqarRMLWNVIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
729-929 |
1.27e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGdttVT-----SGDATVAGKSI-LTNISE- 801
Cdd:PRK13549 5 LLEMKNITKTFGGV--KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG---VYphgtyEGEIIFEGEELqASNIRDt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 802 -------VHQNMGYCPQFDAIDELLTGREHLY--------LYARlrgvpAEEIekvanwsIKSLGLTVYADCLAGTYSGG 866
Cdd:PRK13549 80 eragiaiIHQELALVKELSVLENIFLGNEITPggimdydaMYLR-----AQKL-------LAQLKLDINPATPVGNLGLG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 867 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALC 929
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAIS 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
761-949 |
1.40e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 64.35 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 761 GLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISE-----VHQ-NMGYCPQfDAidEL---LTGREHLyLYARL 831
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARgiflpPHRrRIGYVFQ-EA--RLfphLSVRGNL-LYGRK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 832 RGVPAE---EIEKVANWsiksLGLtvyADCLA---GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVI 905
Cdd:COG4148 104 RAPRAErriSFDEVVEL----LGI---GHLLDrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 50949876 906 VSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHL 949
Cdd:COG4148 177 ERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
739-901 |
2.08e-10 |
|
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: 62.25 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 739 YPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQfdaiDE 817
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQ----DV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 818 LL---TGREHLyLYARlRGVPAEEIEKVANWS-----IKSL--GL-TVYADcLAGTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:cd03251 86 FLfndTVAENI-AYGR-PGATREEVEEAARAAnahefIMELpeGYdTVIGE-RGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170
....*....|....*
gi 50949876 887 DEPTTGMDPQARRML 901
Cdd:cd03251 163 DEATSALDTESERLV 177
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
739-954 |
2.60e-10 |
|
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: 61.73 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 739 YPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISE-VHQNMGYCPQfdaiDE 817
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQVGVVLQ----EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 818 LL---TGREHLYLYArlRGVPAEEIEKVANWS-----IKSLGL---TVYADCLAGtYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:cd03252 86 VLfnrSIRDNIALAD--PGMSMERVIEAAKLAgahdfISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFRCMGTIQHLKSKFG 954
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
679-920 |
3.57e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.83 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 679 VVYF--LLTLLVQR-----HFFLSQWIAEPTKEPIVDEDDDVA--EERQRIITGGNKTDILRLHELTKIYPGtSSPAVDR 749
Cdd:PRK13657 275 VVAFvgFATLLIGRldqvvAFINQVFMAAPKLEEFFEVEDAVPdvRDPPGAIDLGRVKGAVEFDDVSFSYDN-SRQGVED 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 750 LCVGVRPGECFGLLGVSGAGKTTTFKML-------TGDTTVTSGD-ATVAGKSILTNISEVHQNMGYcpqFD-AI-DELL 819
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDiRTVTRASLRRNIAVVFQDAGL---FNrSIeDNIR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 820 TGR-----EHLYLYARlRGVPAEEIEKvanwsiKSLGLtvyaDCLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPT 890
Cdd:PRK13657 431 VGRpdatdEEMRAAAE-RAQAHDFIER------KPDGY----DTVVGergrQLSGGERQRLAIARALLKDPPILILDEAT 499
|
250 260 270
....*....|....*....|....*....|
gi 50949876 891 TGMDPQARRMLwNVIVSIIREGRAVVLTSH 920
Cdd:PRK13657 500 SALDVETEAKV-KAALDELMKGRTTFIIAH 528
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
739-920 |
3.93e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 63.65 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 739 YPGtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQfDAIde 817
Cdd:COG1132 349 YPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQ-DTF-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 818 LLTG--REHLyLYARLrGVPAEEIEKVANWS-----IKSL--GL-TVYADclAGTY-SGGNKRKLSTAIALIGCPPLVLL 886
Cdd:COG1132 425 LFSGtiRENI-RYGRP-DATDEEVEEAAKAAqahefIEALpdGYdTVVGE--RGVNlSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190
....*....|....*....|....*....|....
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSH 920
Cdd:COG1132 501 DEATSALDTETEALIQEALER-LMKGRTTIVIAH 533
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
735-938 |
6.42e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 735 LTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------LTN-ISEVHQN 805
Cdd:PRK10982 4 ISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskeaLENgISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCPQFDAIDELLTGR--------EHLYLYARLRGVPAE-EI-----EKVANWSIKSLGLTVyadcLAGTYSGGNKrkl 871
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRyptkgmfvDQDKMYRDTKAIFDElDIdidprAKVATLSVSQMQMIE----IAKAFSYNAK--- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949876 872 staialigcppLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK10982 155 -----------IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
754-939 |
6.55e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI------------LTNISEVHQNMGYCPQFD-----AID 816
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspldavkkgMAYITESRRDNGFFPNFSiaqnmAIS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 817 ELL-TGRehlylYARLRGVPAEEIE-KVANWSIKSLGLTVYA-DCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 893
Cdd:PRK09700 366 RSLkDGG-----YKGAMGLFHEVDEqRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50949876 894 DPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 939
Cdd:PRK09700 441 DVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
744-923 |
6.84e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 744 SPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGK----------SILTNISEVHQNMGYCPQFD 813
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllALRQQVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 814 AIDElltgreHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 893
Cdd:PRK13638 94 DIDS------DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190
....*....|....*....|....*....|
gi 50949876 894 DPQARRMLWNVIVSIIREGRAVVLTSHSME 923
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
726-938 |
1.24e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.15 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 726 KTDILRLHELTKIYP-GTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGD-TTVTSGDATVAGKSILTN----- 798
Cdd:TIGR02633 254 GDVILEARNLTCWDViNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRnpaqa 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 799 -------ISEVHQNMGYCPQFdAIDELLTgREHLYLYARLRGVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSGGNKRK 870
Cdd:TIGR02633 334 iragiamVPEDRKRHGIVPIL-GVGKNIT-LSVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQK 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 871 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
730-923 |
1.45e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIY-PGTSS--PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSG-------------------- 786
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 787 --DATVAGKSI---LTNISEVHQNMGYCPQFdAIDELL--TGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTV-YADC 858
Cdd:PRK13651 83 vlEKLVIQKTRfkkIKKIKEIRRRVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 859 LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 923
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
833-945 |
2.08e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 833 GVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE 911
Cdd:PRK13631 146 GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN 225
|
90 100 110
....*....|....*....|....*....|....
gi 50949876 912 GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:PRK13631 226 NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
728-938 |
2.35e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.33 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 728 DILRLHELTkIYpgTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTT----FKMLTGDTTVTSGDATVAGKSILTN----- 798
Cdd:PRK10418 3 QQIELRNIA-LQ--AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCalrgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 799 -ISEVHQNmgycPQfDAIDELLTGREHLYLYARLRGVPAEEIEKVAnwSIKSLGLTvYADCLAGTY----SGGNKRKLST 873
Cdd:PRK10418 80 kIATIMQN----PR-SAFNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLE-NAARVLKLYpfemSGGMLQRMMI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 874 AIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
754-920 |
2.35e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 58.31 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTG--DTTVTSGDATVAGKSIlTNISevhqnmgycpqfdaIDEllTGREHLYLY--- 828
Cdd:cd03217 23 IKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDI-TDLP--------------PEE--RARLGIFLAfqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 -ARLRGVpaeeieKVANWsIKSLGLTvyadclagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVS 907
Cdd:cd03217 86 pPEIPGV------KNADF-LRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170
....*....|...
gi 50949876 908 IIREGRAVVLTSH 920
Cdd:cd03217 150 LREEGKSVLIITH 162
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
754-894 |
2.65e-09 |
|
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: 58.04 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVT---SGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYAR 830
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50949876 831 LRGvpaeeiekvaNWSIKSLgltvyadclagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 894
Cdd:cd03233 110 CKG----------NEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
730-920 |
2.67e-09 |
|
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: 56.69 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGtsSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisevhQNMGYC 809
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQFdaidelltgrehlylyarlrgvpaeeiekvanwsikslgltvyadclagtySGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:cd03221 69 EQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 50949876 890 TTGMDPQARRMLwnvIVSIIREGRAVVLTSH 920
Cdd:cd03221 98 TNHLDLESIEAL---EEALKEYPGTVILVSH 125
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
746-944 |
2.74e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISEVHQNMGYCPQ--FDAIDELL 819
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 820 TGREHLYLYARLRGV-PAEEIEKVANWSIKSLGLTV-YADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 897
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 50949876 898 RRMLWNVIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMG 944
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
725-947 |
3.41e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.99 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 725 NKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVH 803
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 QNMGYCpqFDAIDELLTGREHLYLYA---RLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 880
Cdd:PRK13648 83 KHIGIV--FQNPDNQFVGSIVKYDVAfglENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 881 PPLVLLDEPTTGMDPQARRMLWNvIVSIIREGRAVVLTSHSMEECEAL-CTRLAIMVKGAFRCMGTIQ 947
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLD-LVRKVKSEHNITIISITHDLSEAMeADHVIVMNKGTVYKEGTPT 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
746-938 |
3.44e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL--TNISEVHQNMGYCPQFDAIDELLTGRE 823
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 824 HLYL--YARLRGVPAEEIEKVANWSIKSLGLTVYAdclAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 901
Cdd:PRK11614 100 NLAMggFFAERDQFQERIKWVYELFPRLHERRIQR---AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 50949876 902 WNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK11614 177 FDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
754-954 |
3.56e-09 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 58.32 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQ----FDAidellTGREHLyLY 828
Cdd:cd03249 26 IPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQepvlFDG-----TIAENI-RY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 ARLRGVPAEEIE--KVANWS--IKSL--GLtvyaDCLAGTY----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 898
Cdd:cd03249 100 GKPDATDEEVEEaaKKANIHdfIMSLpdGY----DTLVGERgsqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 899 RMLWNVIVSiIREGRAVVLTSHSmeeceaLCT-----RLAIMVKGAFRCMGTIQHLKSKFG 954
Cdd:cd03249 176 KLVQEALDR-AMKGRTTIVIAHR------LSTirnadLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
754-920 |
3.61e-09 |
|
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: 58.39 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQfdaiDELL---TGREHLyLYA 829
Cdd:cd03254 26 IKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ----DTFLfsgTIMENI-RLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 830 RLRgVPAEEIEKV-----ANWSIKSL--GLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 902
Cdd:cd03254 101 RPN-ATDEEVIEAakeagAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQ 179
|
170
....*....|....*...
gi 50949876 903 NVIVSiIREGRAVVLTSH 920
Cdd:cd03254 180 EALEK-LMKGRTSIIIAH 196
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
759-946 |
3.65e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 759 CFGLLGVSGAGKTT---TFKMLT--GDTTVTSGDATVAGKSILT---NISEVHQNMGYCPQFDAIDELLTGREHLYLYAR 830
Cdd:PRK14267 32 VFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 LRGV--PAEEIEKVANWSIKSLGL-TVYADCL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNV 904
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 50949876 905 IVSiIREGRAVVLTSHSmeecEALCTRLAIMVkgAFRCMGTI 946
Cdd:PRK14267 192 LFE-LKKEYTIVLVTHS----PAQAARVSDYV--AFLYLGKL 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
729-894 |
5.14e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 57.83 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTSSP--AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISE----- 801
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD-LFALDEdarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 802 -VHQNMGYCPQ-FDAIDELlTGREHLYLYARLRGVP------AEEIEKVanwsikslGLTVYADCLAGTYSGGNKRKLST 873
Cdd:COG4181 87 lRARHVGFVFQsFQLLPTL-TALENVMLPLELAGRRdararaRALLERV--------GLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180
....*....|....*....|.
gi 50949876 874 AIALIGCPPLVLLDEPTTGMD 894
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLD 178
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
762-920 |
5.61e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 762 LLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEK 841
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITEL 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949876 842 VANWSIKSlgltvYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 920
Cdd:PRK13540 112 CRLFSLEH-----LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
754-939 |
7.45e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEVH-QNMG-Y-CPQFDAIDELLTGREHLylyar 830
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP-CARLTPAKaHQLGiYlVPQEPLLFPNLSVKENI----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 LRGVPAEE--IEKVANWsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI 908
Cdd:PRK15439 108 LFGLPKRQasMQKMKQL-LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL 186
|
170 180 190
....*....|....*....|....*....|.
gi 50949876 909 IREGRAVVLTSHSMEECEALCTRLAIMVKGA 939
Cdd:PRK15439 187 LAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
730-927 |
9.22e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.72 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTssPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTT---VTSGDATVAGKSILTniSEVHQ-N 805
Cdd:COG4136 2 LSLENLTITLGGR--PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTA--LPAEQrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCPQfdaiDELLTgrEHLYLYARL-----RGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 880
Cdd:COG4136 78 IGILFQ----DDLLF--PHLSVGENLafalpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 50949876 881 PPLVLLDEPTTGMDP----QARRMLWNvivSIIREGRAVVLTSHSMEECEA 927
Cdd:COG4136 152 PRALLLDEPFSKLDAalraQFREFVFE---QIRQRGIPALLVTHDEEDAPA 199
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
747-951 |
9.27e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.80 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 747 VDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTG-DTTVT----SGDATVAGKSILT--NISEVHQNMGYCPQ------FD 813
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSIFNyrDVLEFRRRVGMLFQrpnpfpMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 814 AIDELLTG-REHlylyarlRGVPAEEIEKVANWSIKSLGL-TVYADCLAGT---YSGGNKRKLSTAIALIGCPPLVLLDE 888
Cdd:PRK14271 117 IMDNVLAGvRAH-------KLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 889 PTTGMDPQARRMLWNVIVSIIrEGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKS 951
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
757-931 |
1.90e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.61 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDaTVAGKSILTNISE----VHQNMGYCPQFDAIDELLTGrehlylyarLR 832
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREdtrlMFQDARLLPWKKVIDNVGLG---------LK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 833 GvpaeeiekvaNW------SIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIV 906
Cdd:PRK11247 108 G----------QWrdaalqALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180
....*....|....*....|....*.
gi 50949876 907 SIIRE-GRAVVLTSHSMEECEALCTR 931
Cdd:PRK11247 178 SLWQQhGFTVLLVTHDVSEAVAMADR 203
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
741-894 |
2.23e-08 |
|
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: 58.21 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 741 GTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS--EVHQNMGYCPQFDAIdel 818
Cdd:TIGR01193 484 GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-KDIDrhTLRQFINYLPQEPYI--- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 819 LTGR--EHLYLYARlRGVPAEEIEKVANWS-IK------SLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 889
Cdd:TIGR01193 560 FSGSilENLLLGAK-ENVSQDEIWAACEIAeIKddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
....*
gi 50949876 890 TTGMD 894
Cdd:TIGR01193 639 TSNLD 643
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
754-947 |
2.49e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.32 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNIS--EVHQNMGYCPQ-------FDAIDELLTGREH 824
Cdd:PRK13548 25 LRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSpaELARRRAVLPQhsslsfpFTVEEVVAMGRAP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 825 LYL-YARLRGVPAEEIEKVanwsikslGLTVYADCLAGTYSGGNKRKLSTAIALI------GCPPLVLLDEPTTGMDPQ- 896
Cdd:PRK13548 104 HGLsRAEDDALVAAALAQV--------DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAh 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 897 -------ARRMlwnvivsIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQ 947
Cdd:PRK13548 176 qhhvlrlARQL-------AHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
746-955 |
3.66e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEvhqnmgycpqfdAIDELLTGREHL 825
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS------------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 826 YLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVI 905
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 50949876 906 VSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGD 955
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
754-938 |
3.81e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.87 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCpqFDAIDELLTG---REHLYLYA 829
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNLRRKIGMV--FQNPDNQFVGatvEDDVAFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 830 RLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 909
Cdd:PRK13642 108 ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIK 187
|
170 180 190
....*....|....*....|....*....|
gi 50949876 910 REGRAVVLT-SHSMEECeALCTRLAIMVKG 938
Cdd:PRK13642 188 EKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
730-938 |
4.59e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSpavdRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGK------------SIL- 796
Cdd:PRK10771 2 LKLTDITWLYHHLPM----RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpvSMLf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 797 --TNISE---VHQNMGYcpqfdAIDELLtgrehlylyaRLRGVPAEEIEKVAnwsiKSLGLTVYADCLAGTYSGGNKRKL 871
Cdd:PRK10771 78 qeNNLFShltVAQNIGL-----GLNPGL----------KLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 872 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKG 938
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLmVSHSLEDAARIAPRSLVVADG 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
742-920 |
5.56e-08 |
|
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: 54.93 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 742 TSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVHQN-----MGYCPQ----F 812
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ----DIREVTLDslrraIGVVPQdtvlF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 813 -DAIdelltgrEHLYLYARLrGVPAEEIEKVA-----NWSIKSL--GltvYADCLA--GTY-SGGNKRKLSTAIALIGCP 881
Cdd:cd03253 88 nDTI-------GYNIRYGRP-DATDEEVIEAAkaaqiHDKIMRFpdG---YDTIVGerGLKlSGGEKQRVAIARAILKNP 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 50949876 882 PLVLLDEPTTGMDPQARRMLWNVIVSIIReGRAVVLTSH 920
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
739-954 |
7.03e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 56.65 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 739 YPGTSS-PAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQfdaiD 816
Cdd:TIGR00958 488 YPNRPDvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQ----E 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 817 ELLTGR--EHLYLYArLRGVPAEEIEKVANWS-----IKSLGLTVYADC-LAGTY-SGGNKRKLSTAIALIGCPPLVLLD 887
Cdd:TIGR00958 564 PVLFSGsvRENIAYG-LTDTPDEEIMAAAKAAnahdfIMEFPNGYDTEVgEKGSQlSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949876 888 EPTTGMDPQARRMLWNvivSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFRCMGTIQHLKSKFG 954
Cdd:TIGR00958 643 EATSALDAECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
757-947 |
7.56e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.86 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVH---QNMGYCPQFDAIDELLTGREH----LYLYA 829
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHardRKVGFVFQHYALFRHMTVFDNiafgLTVLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 830 RLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 909
Cdd:PRK10851 104 RRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLH 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 50949876 910 REGR-AVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQ 947
Cdd:PRK10851 184 EELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
747-940 |
7.78e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 747 VDRLCVGVRPGECFGLLGVSGAGKTTtFKM-LTGDT--TVTSGDATVAGKSIltNISEVHqnmgycpqfDAIDELLT--- 820
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsVFGRSygRNISGTVFKDGKEV--DVSTVS---------DAIDAGLAyvt 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 821 -GREHLYL-----------YARLRGV-------PAEEIeKVANWSIKSLGL---TVYAdcLAGTYSGGNKRKLSTAIALI 878
Cdd:NF040905 344 eDRKGYGLnliddikrnitLANLGKVsrrgvidENEEI-KVAEEYRKKMNIktpSVFQ--KVGNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 879 GCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 940
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
746-968 |
7.81e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGksiltNISEVHQNMGYCPQfdaidelLTGREHL 825
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 826 YLYARLRGVPAEEIEKVANWSIK--SLGLTVYADclAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 903
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEfsELGEFIYQP--VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 904 VIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFgDGYIVTMKIKSPKD 968
Cdd:PRK13546 185 KIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
757-923 |
1.17e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.20 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISEVHQNMGYCPQFDAID-ELLTGR-----EHLYLYAR 830
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQ----TINLVRDKDGQLKVADKNQlRLLRTRltmvfQHFNLWSH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 LrgvpaEEIEKVANWSIKSLGLT---------VYADCLA------GTY----SGGNKRKLSTAIALIGCPPLVLLDEPTT 891
Cdd:PRK10619 107 M-----TVLENVMEAPIQVLGLSkqeareravKYLAKVGideraqGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190
....*....|....*....|....*....|..
gi 50949876 892 GMDPQARRMLWNVIVSIIREGRAVVLTSHSME 923
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
747-918 |
1.74e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 747 VDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTT--VTSGDATVAGKSILT-------NISEVHQNMGYCPQ------ 811
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVTLNgeplaaiDAPRLARLRAVLPQaaqpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 812 -FDAIDELLTGRehlYLYARLRGVPAEEIEKVANWSIKSLGltvyADCLAG----TYSGGNKRKLSTAIAL--------- 877
Cdd:PRK13547 97 aFSAREIVLLGR---YPHARRAGALTHRDGEIAWQALALAG----ATALVGrdvtTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 50949876 878 IGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLT 918
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLA 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
726-899 |
2.06e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.34 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 726 KTDILRLHELTKIYpGTSSpAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISEvhQN 805
Cdd:PRK11432 3 QKNFVVLKNITKRF-GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSI--QQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCPQFDAIDELltgrEHLYLYA------RLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 879
Cdd:PRK11432 78 RDICMVFQSYALF----PHMSLGEnvgyglKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180
....*....|....*....|
gi 50949876 880 CPPLVLLDEPTTGMDPQARR 899
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRR 173
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
739-905 |
2.25e-07 |
|
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: 52.88 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 739 YPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTT----FKMLtgdtTVTSGDATVAGKSILT-NISEVHQNMGYCPQfD 813
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKiGLHDLRSRISIIPQ-D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 814 AIdeLLTG--REHL-----YLYARLRGVpaeeIEKVANWS-IKSLGLTVYADCLAG--TYSGGNKRKLSTAIALIGCPPL 883
Cdd:cd03244 87 PV--LFSGtiRSNLdpfgeYSDEELWQA----LERVGLKEfVESLPGGLDTVVEEGgeNLSVGQRQLLCLARALLRKSKI 160
|
170 180
....*....|....*....|..
gi 50949876 884 VLLDEPTTGMDPQARRMLWNVI 905
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTI 182
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
740-938 |
2.40e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 52.47 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 740 PGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisevhqnMGYCPQFDAIdelL 819
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWI---Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 820 TG--REHLylyarLRGVP--AEEIEKVanwsIKSLGLTVYADCLAG-----------TYSGGNKRKLSTAIALIGCPPLV 884
Cdd:cd03250 79 NGtiRENI-----LFGKPfdEERYEKV----IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 885 LLDEPTTGMDPQARRMLW-NVIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKG 938
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
747-941 |
2.71e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 747 VDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGD-TTVTSGDATVAGKSILTNISE--VHQNMGYCPQ---FDAIDELLT 820
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQqaIAQGIAMVPEdrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 821 GREHLYL-----YARLRGVPAEEIEKVANWSIKSLGLTVYADCLA-GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 894
Cdd:PRK13549 358 VGKNITLaaldrFTGGSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 50949876 895 PQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFR 941
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
754-917 |
3.50e-07 |
|
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: 52.80 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisevhqnmGYCPQFDAIDELLTGREHLYLYARLRG 833
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 834 VPAEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGR 913
Cdd:cd03237 91 THPYFKTEI----AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
....
gi 50949876 914 AVVL 917
Cdd:cd03237 167 KTAF 170
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
762-980 |
4.96e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.70 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 762 LLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQ------NMGYCPQF-------DAID-ELLTGREHLyl 827
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlrkEIGLVFQFpeyqlfqETIEkDIAFGPVNL-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 828 yarlrGVPAEEIEKVANWSIKSLGLTV-YADCLAGTYSGGNKRKLSTA--IALIGcpPLVLLDEPTTGMDPQARRMLWNV 904
Cdd:PRK13645 120 -----GENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAgiIAMDG--NTLVLDEPTGGLDPKGEEDFINL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 905 IVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTI------QHLKSKFG----DGYIVTMKIKSPKDDLL-P 972
Cdd:PRK13645 193 FERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfeifsnQELLTKIEidppKLYQLMYKLKNKGIDLLnK 272
|
....*...
gi 50949876 973 DLNPVEQF 980
Cdd:PRK13645 273 NIRTIEEF 280
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
732-924 |
5.34e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 732 LHELTKI-YPGTSSPAVDRLCVGVRPGEcFGLL-GVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVH-QNMGY 808
Cdd:PRK10247 7 LLQLQNVgYLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYrQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQFDAI--DellTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAgTYSGGNKRKLSTAIALIGCPPLVLL 886
Cdd:PRK10247 86 CAQTPTLfgD---TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIA-ELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 50949876 887 DEPTTGMDPQARRMLWNVIVSIIRE-GRAVVLTSHSMEE 924
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDE 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
726-938 |
5.86e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 726 KTDILRLHELTKIypgtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQN 805
Cdd:PRK10982 247 GEVILEVRNLTSL----RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 806 MGYCpqfdaideLLTG-REHLYLYARL------------------RGVPAEEIEKVANWSIKSLGL-TVYADCLAGTYSG 865
Cdd:PRK10982 323 HGFA--------LVTEeRRSTGIYAYLdigfnslisnirnyknkvGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 866 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
730-894 |
7.88e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYpGTSSPAVDrLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-EVHQNMGY 808
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAEN-LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQFDA------IDELLT-GR-EHLYLYARLRgvpaEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGC 880
Cdd:PRK10253 86 LAQNATtpgditVQELVArGRyPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....
gi 50949876 881 PPLVLLDEPTTGMD 894
Cdd:PRK10253 162 TAIMLLDEPTTWLD 175
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
754-917 |
8.46e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnISevhqnmgYCPQFDAIDELLTgrehlyLYARLRG 833
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----IS-------YKPQYIKPDYDGT------VEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 834 VPA--------EEIekvanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVI 905
Cdd:PRK13409 424 ITDdlgssyykSEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170
....*....|..
gi 50949876 906 VSIIREGRAVVL 917
Cdd:PRK13409 497 RRIAEEREATAL 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
730-953 |
1.02e-06 |
|
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: 52.50 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSspAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGdttvTSGDATVAGKSILtnisevhqNMGYC 809
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG----MDQYEPTSGRIIY--------HVALC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 810 PQ---------------------------FDAIDELLTGR----------EHLYLYARLR------------GVPAEEIE 840
Cdd:TIGR03269 67 EKcgyverpskvgepcpvcggtlepeevdFWNLSDKLRRRirkriaimlqRTFALYGDDTvldnvlealeeiGYEGKEAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 841 KVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVS-IIREGRAVVLTS 919
Cdd:TIGR03269 147 GRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTS 226
|
250 260 270
....*....|....*....|....*....|....
gi 50949876 920 HSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKF 953
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
760-959 |
1.09e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 760 FGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-------TNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLR 832
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 833 GVPAE-EIEKVANWSIKSLGL--TVY--ADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVS 907
Cdd:PRK14246 119 GIKEKrEIKKIVEECLRKVGLwkEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 908 IIREgRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHL----KSKFGDGYIV 959
Cdd:PRK14246 199 LKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
754-922 |
1.98e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGdatvagksilTNISEVHQNMGYCPQ---FDAIDELLTGRehlylYAR 830
Cdd:PRK09544 27 LKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLRIGYVPQklyLDTTLPLTVNR-----FLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 LR-GVPAEEIEKVanwsIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 909
Cdd:PRK09544 92 LRpGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
170
....*....|....
gi 50949876 910 RE-GRAVVLTSHSM 922
Cdd:PRK09544 168 RElDCAVLMVSHDL 181
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
739-899 |
2.05e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 739 YPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAG--------KSILTNISEVHQNMgycp 810
Cdd:PRK11176 351 YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlASLRNQVALVSQNV---- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 811 qfdaidelltgreHLY--------LYARLRGVPAEEIEKVANWS-----IKSL--GLtvyaDCLAG----TYSGGNKRKL 871
Cdd:PRK11176 427 -------------HLFndtianniAYARTEQYSREQIEEAARMAyamdfINKMdnGL----DTVIGengvLLSGGQRQRI 489
|
170 180
....*....|....*....|....*...
gi 50949876 872 STAIALIGCPPLVLLDEPTTGMDPQARR 899
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESER 517
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
757-924 |
2.22e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.53 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI----LTNISEVHQNMGYCPQFDAIDELLTG--------REH 824
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVfdnvayplREH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 825 LYLyarlrgvPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRK--LSTAIALIgcPPLVLLDEPTTGMDPqarrMLW 902
Cdd:PRK11831 113 TQL-------PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRaaLARAIALE--PDLIMFDEPFVGQDP----ITM 179
|
170 180
....*....|....*....|....*..
gi 50949876 903 NVIVSIIRE-----GRAVVLTSHSMEE 924
Cdd:PRK11831 180 GVLVKLISElnsalGVTCVVVSHDVPE 206
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
727-920 |
3.62e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.88 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 727 TDILRLHELTKIYP-GTSSPAV-DRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEV-- 802
Cdd:PRK10535 2 TALLELKDIRRSYPsGEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 803 ---HQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIG 879
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 50949876 880 CPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 920
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
756-894 |
4.66e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.40 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 756 PGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVH-QNMGYCPQFDAIDELLTGREHLYL-----YA 829
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPAAEGMTVRELVAIgrypwHG 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 830 RLRGVPAEEIEKVANwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 894
Cdd:PRK10575 116 ALGRFGAADREKVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
729-926 |
1.01e-05 |
|
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: 47.85 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYPGTS-SPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisEVHQNMG 807
Cdd:cd03248 11 IVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-----SQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 808 YCPQFDAIdelltGREHLyLYAR---------LRGVPAEEIEKVA-------NWSIKSLGLTVYADCLAGTYSGGNKRKL 871
Cdd:cd03248 86 LHSKVSLV-----GQEPV-LFARslqdniaygLQSCSFECVKEAAqkahahsFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 872 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIvSIIREGRAVVLTSHSMEECE 926
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQAL-YDWPERRTVLVIAHRLSTVE 213
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
864-923 |
1.09e-05 |
|
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: 48.54 E-value: 1.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 864 SGGNKRKLSTAIALIGCPP---LVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 923
Cdd:pfam13304 238 SDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
754-917 |
1.37e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnISevhqnmgYCPQFDAIDELLTGREHlylyarLRG 833
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----IS-------YKPQYISPDYDGTVEEF------LRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 834 VPAEEIEkvANWS----IKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSII 909
Cdd:COG1245 425 ANTDDFG--SSYYkteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
....*...
gi 50949876 910 REGRAVVL 917
Cdd:COG1245 503 ENRGKTAM 510
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
754-902 |
2.09e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILtniSEVHQNMgycPQFD--AIDELLTG-REHLYLYAR 830
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQL---AWVNQET---PALPqpALEYVIDGdREYRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 831 LRGVPAE-----------EIEKVANWSIKSL------GLTVYADCL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 890
Cdd:PRK10636 98 LHDANERndghaiatihgKLDAIDAWTIRSRaasllhGLGFSNEQLerpVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170
....*....|..
gi 50949876 891 TGMDPQArrMLW 902
Cdd:PRK10636 178 NHLDLDA--VIW 187
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
729-938 |
2.13e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.46 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 729 ILRLHELTKIYpgTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLT--GD---TTVTSGDATVAGKSIltnisevh 803
Cdd:PRK14239 5 ILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNI-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 qnmgYCPQFDAID---EL-----------LTGREHLYLYARLRGVPAEEI-EKVANWSIKslGLTVY---ADCL---AGT 862
Cdd:PRK14239 75 ----YSPRTDTVDlrkEIgmvfqqpnpfpMSIYENVVYGLRLKGIKDKQVlDEAVEKSLK--GASIWdevKDRLhdsALG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 863 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
864-920 |
2.75e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 2.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949876 864 SGGNKRKLSTAIALIGCP----PLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSH 920
Cdd:cd03227 79 SGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
860-921 |
3.41e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 3.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50949876 860 AGTYSGGNKRKLSTAIALIGCPP--LVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHS 921
Cdd:cd03238 85 LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
730-945 |
4.92e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGtSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISEVH 803
Cdd:PRK11650 4 LKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepadrDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 QNMGYCPQfdaidelLTGREHLYlYA-RLRGVPAEEIEK-VANwSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCP 881
Cdd:PRK11650 83 QNYALYPH-------MSVRENMA-YGlKIRGMPKAEIEErVAE-AARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949876 882 PLVLLDEPTTGMDPQAR-RMLwnviVSIIREGRAVVLTS----HSMEECEALCTRLAIMVKGAFRCMGT 945
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRvQMR----LEIQRLHRRLKTTSlyvtHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
754-938 |
5.44e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.06 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTV-----TSGDATVAGKSILT-NISEVHQNMGYCPQFDAIDELLTGREHLYL 827
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNPIPNLSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 828 YARL-RGVPAE-EIEKVANWSIKSLGL----TVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 901
Cdd:PRK14247 106 GLKLnRLVKSKkELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 50949876 902 WNVIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK14247 186 ESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
724-920 |
5.56e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 47.24 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 724 GNKtdILRLHELTKIYpgTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisevh 803
Cdd:TIGR03719 319 GDK--VIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 qNMGYCPQF-DAID-------ELLTGREHLylyarlrgvpaeeieKVANWSIKSlgltvYADC------------LAGTY 863
Cdd:TIGR03719 386 -KLAYVDQSrDALDpnktvweEISGGLDII---------------KLGKREIPS-----RAYVgrfnfkgsdqqkKVGQL 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 50949876 864 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIirEGRAVVLtSH 920
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVI-SH 498
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
735-991 |
8.83e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 735 LTKIYPGTSSPAVDRL--CVGV-RPGECFGLLGVSGAGKTTTFKMLTGDT--TVTSGDATVAGKSILTNISEVH--QNMG 807
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILkpMDGLiKPGELTVVLGRPGSGCSTLLKTIASNTdgFHIGVEGVITYDGITPEEIKKHyrGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 808 YCPQFDAIDELLTGREHLYLYARLR-------GVPAEE-IEKVANWSIKSLGLTVYADCLAGT-----YSGGNKRKLSTA 874
Cdd:TIGR00956 142 YNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 875 IALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTS--HSMEECEALCTRLAIMVKGAFRCMGTIQHLKSk 952
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQ- 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 50949876 953 fgdgYIVTMKIKSPKDDLLPDL-----NPVEQFFQGNFPGSVQR 991
Cdd:TIGR00956 301 ----YFEKMGFKCPDRQTTADFltsltSPAERQIKPGYEKKVPR 340
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
757-920 |
1.08e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISEvhqnmgYCPQFDAI-------DELLTGrehlyly 828
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPED------YRKLFSAVftdfhlfDQLLGP------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 arlRGVPAEEiEKVANWsIKSLG----LTVYADCLAGT-YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 903
Cdd:PRK10522 416 ---EGKPANP-ALVEKW-LERLKmahkLELEDGRISNLkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170
....*....|....*...
gi 50949876 904 VIVSIIRE-GRAVVLTSH 920
Cdd:PRK10522 491 VLLPLLQEmGKTIFAISH 508
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
740-920 |
1.31e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 45.83 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 740 PGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTF----KMLTGDTTVTSGDATVAGKSILT------------NISEVH 803
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDLLGlserelrrirgnRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 804 QN-MgycpqfDAIDELLT-GR---EHLYLYARLRGVPAEE-----IEKVanwsikslGLTVYADCLaGTY----SGGNKR 869
Cdd:COG4172 99 QEpM------TSLNPLHTiGKqiaEVLRLHRGLSGAAARAralelLERV--------GIPDPERRL-DAYphqlSGGQRQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949876 870 KLSTAIALIGCPPLVLLDEPTTGMDP--QARrmlwnvIVSIIRE-----GRAVVLTSH 920
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVtvQAQ------ILDLLKDlqrelGMALLLITH 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
864-924 |
1.46e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 44.64 E-value: 1.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 864 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSI-IREGRAVVLTSHSMEE 924
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
734-952 |
3.58e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.69 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 734 ELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTF----KMLTgdttvTSGDATVAGKSILT-NISEVHQNMGY 808
Cdd:cd03289 7 DLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQFDAIdelLTG--REHLYLYARLRGvpaEEIEKVANwsikSLGLTVYADCLAG-----------TYSGGNKRKLSTAI 875
Cdd:cd03289 82 IPQKVFI---FSGtfRKNLDPYGKWSD---EEIWKVAE----EVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 876 ALIGCPPLVLLDEPTTGMDPqarrMLWNVIVSIIREGRA---VVLTSHSMeecEAL--CTRLAIMVKGAFRCMGTIQHLK 950
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDP----ITYQVIRKTLKQAFAdctVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLL 224
|
..
gi 50949876 951 SK 952
Cdd:cd03289 225 NE 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
762-897 |
5.66e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 762 LLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHqnmgycpqFDAIDelLTGREHLYLYARLRGVPAEEIEK 841
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHH--------VDGLD--LSSNPLLYMMRCFPGVPEQKLRA 609
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50949876 842 vanwSIKSLGLT-------VYadclagTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 897
Cdd:PLN03073 610 ----HLGSFGVTgnlalqpMY------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
746-938 |
7.79e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 746 AVDRLCVGVRPGECFGLLGVSGAGKTTT----FKMLTgdttvTSGDATVAGKSILT-----------NISEVHQ--NMGY 808
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNlnrrqllpvrhRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQFDAIDELLTGrehlyLYARLRGVPAEEIEKVANWSIKSLGLTV-----YAdclaGTYSGGNKRKLSTAIALIGCPPL 883
Cdd:PRK15134 376 NPRLNVLQIIEEG-----LRVHQPTLSAAQREQQVIAVMEEVGLDPetrhrYP----AEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50949876 884 VLLDEPTTGMDPQARRMLWNVIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 938
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
738-787 |
8.13e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.16 E-value: 8.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 50949876 738 IYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGD 787
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
861-920 |
9.25e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 9.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 861 GTYSGGNKRKLSTAIAL-------IGCPPLVLlDEPTTGMDPQARRmlwNVIVSIIRE-----GRAVVLTSH 920
Cdd:cd03240 114 GRCSGGEKVLASLIIRLalaetfgSNCGILAL-DEPTTNLDEENIE---ESLAEIIEErksqkNFQLIVITH 181
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
757-898 |
1.33e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 42.32 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 757 GECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPA 836
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR-MNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKK 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949876 837 EEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 898
Cdd:PRK11000 108 EEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
881-923 |
1.43e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 1.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 50949876 881 PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSME 923
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
735-926 |
2.25e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.20 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 735 LTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTgDTTVTSGDATVAGKSILT-NISEVHQNMGYCPQFD 813
Cdd:TIGR01271 1223 LTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSvTLQTWRKAFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 814 AIdelLTG--REHLYLYARLRGvpaEEIEKVAN-WSIKSLgLTVYADCLA-----GTY--SGGNKRKLSTAIALIGCPPL 883
Cdd:TIGR01271 1302 FI---FSGtfRKNLDPYEQWSD---EEIWKVAEeVGLKSV-IEQFPDKLDfvlvdGGYvlSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50949876 884 VLLDEPTTGMDPqarrmlwnVIVSIIREGR-------AVVLTSHSME---ECE 926
Cdd:TIGR01271 1375 LLLDEPSAHLDP--------VTLQIIRKTLkqsfsncTVILSEHRVEallECQ 1419
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
862-922 |
2.37e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50949876 862 TYSGGNKRKLSTAIALIGC---PPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSM 922
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
756-894 |
3.15e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 756 PGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisevhqNMGYCPQF-DAID-------ELLTGREHLyl 827
Cdd:PRK11819 349 PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV---------KLAYVDQSrDALDpnktvweEISGGLDII-- 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949876 828 yarlrgvpaeeieKVANWSIKSlgltvYADC------------LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 894
Cdd:PRK11819 417 -------------KVGNREIPS-----RAYVgrfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
730-938 |
4.39e-03 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 39.70 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 730 LRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISEVHQNMGY 808
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 809 CPQfDAIdeLLTG--REHLYLYARLrgvpaEEIEKVANWSIKSLGLTVyadclagtySGGNKRKLSTAIALIGCPPLVLL 886
Cdd:cd03369 87 IPQ-DPT--LFSGtiRSNLDPFDEY-----SDEEIYGALRVSEGGLNL---------SQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 887 DEPTTGMDPQARRMlwnvIVSIIRE---GRAVVLTSHSMEECeALCTRLAIMVKG 938
Cdd:cd03369 150 DEATASIDYATDAL----IQKTIREeftNSTILTIAHRLRTI-IDYDKILVMDAG 199
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
754-899 |
5.81e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 40.57 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 754 VRPGECFGLLGVSGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISeVHQNMGYCPQfdaiDELL---TGREHLyLY 828
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdVTQAS-LRAAIGIVPQ----DTVLfndTIAYNI-AY 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949876 829 ARLrGVPAEEIEKVANWS-----IKSL-----------GLTVyadclagtySGGNKRKLSTAIALIGCPPLVLLDEPTTG 892
Cdd:COG5265 455 GRP-DASEEEVEAAARAAqihdfIESLpdgydtrvgerGLKL---------SGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
....*..
gi 50949876 893 MDPQARR 899
Cdd:COG5265 525 LDSRTER 531
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
864-918 |
5.84e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 5.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 50949876 864 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLT 918
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
|
| |
