|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
478-701 |
2.27e-85 |
|
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: 272.84 E-value: 2.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKneTVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT--DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSSIFLK 701
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
107-809 |
2.11e-82 |
|
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: 292.30 E-value: 2.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 107 EEYASEKELLASSLS--KPSNF-VGVVFKDV----------MSYELRFFPDMV----PVSSVYMDSRAGCSKSCDAAQYW 169
Cdd:TIGR01257 526 ESYDDEVQLTQRALSllEENRFwAGVVFPDMypwtsslpphVKYKIRMDIDVVektnKIKDRYWDSGPRADPVEDFRYIW 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 170 SsGFTALQASIDAAI----IQLKTNVSLWRELESTKAVIMGEAAVVEIDTFPrgvilIYLVIAFSPFGYFLAIHIVAEKE 245
Cdd:TIGR01257 606 G-GFAYLQDMVEQGItrsqMQAEPPVGIYLQQMPYPCFVDDSFMIILNRCFP-----IFMVLAWIYSVSMTVKSIVLEKE 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 246 KRLKEFLKIMGLHDTAFWLSWVLLYTSLIFLMSLLMAVIATASSLFPQSSSIVIFLLFFLYGLSSVFFALMLTPLFKKSK 325
Cdd:TIGR01257 680 LRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKAS 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 326 HVGVVEFFVTVVFGFVGLLIVL----VESFPRSLVWLFSPLcqcAFLIGIAQVMHLEDFNEGALFSSLTEGP-----YPL 396
Cdd:TIGR01257 760 LAAACSGVIYFTLYLPHILCFAwqdrMTADLKTAVSLLSPV---AFGFGTEYLVRFEEQGLGLQWSNIGNSPlegdeFSF 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 397 IITLTMLALDSVFYALLAVYLDQVIPGEFGLRRSSLYFLKPSYW------SKNKRNYKELSEgNINGNISLNEIVEPVSS 470
Cdd:TIGR01257 837 LLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWlggegcSTREERALEKTE-PLTEEMEDPEHPEGIND 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 471 EFIGKE------AIRISGIQKAYRKKNETVEALRNLSFdiYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhr 544
Cdd:TIGR01257 916 SFFERElpglvpGVCVKNLVKIFEPSGRPAVDRLNITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-- 991
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 545 vSEIDEMFEA-RKMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKL 623
Cdd:TIGR01257 992 -KDIETNLDAvRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKL 1070
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 624 SLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSSIFLKSK 703
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNC 1150
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 704 WGIGYRLSMY------------IDRYCATES--------------------------LSSLVRQHIPAAALLQQNDQQIV 745
Cdd:TIGR01257 1151 FGTGFYLTLVrkmkniqsqrggCEGTCSCTSkgfstrcparvdeitpeqvldgdvneLMDLVYHHVPEAKLVECIGQELI 1230
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 746 YSLPFKDMDK--FSGLFSAL-DIHSNLGVISYGVSMTTLEDVFLKLEVEAEIDQAdYSVFTQQPREE 809
Cdd:TIGR01257 1231 FLLPNKNFKQraYASLFRELeETLADLGLSSFGISDTPLEEIFLKVTEDADSGSL-FAGGAQQKREN 1296
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
478-696 |
2.53e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 227.25 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLlSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
478-691 |
8.03e-56 |
|
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: 190.30 E-value: 8.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVseIDEMFEARKM 557
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--KKEPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLsilasvkgipanniiqevqkvlldldmqaikdnqakKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQGML 691
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILlSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
478-696 |
1.86e-50 |
|
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: 177.74 E-value: 1.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:COG4555 2 IEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRaLKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
478-695 |
1.04e-49 |
|
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: 174.69 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGqITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--QPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
489-701 |
8.50e-49 |
|
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: 172.55 E-value: 8.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKMIGICPQSDMNF 568
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR--EPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:cd03265 86 DELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 649 SRHIVWNLL-KYRKANRVTVF-STHFMDEADILADRKAVISQGMLKCVGSSIFLK 701
Cdd:cd03265 166 TRAHVWEYIeKLKEEFGMTILlTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
478-695 |
1.38e-44 |
|
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: 160.23 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRqLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
478-687 |
9.94e-43 |
|
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: 154.94 E-value: 9.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemfEARKM 557
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVIS 687
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLdiWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
487-689 |
1.30e-42 |
|
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: 154.55 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 487 YRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQ-SD 565
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKVGLVFQnPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 566 MNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03225 86 DQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29170396 646 DPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03225 166 DPAGRRELLELLKKLKAEGKTiIIVTHDLDLLLELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
478-696 |
1.83e-42 |
|
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: 154.80 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKM 557
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQS--DMNFDvLTVEE-------NLsilasvkGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GI 627
Cdd:COG1122 77 VGLVFQNpdDQLFA-PTVEEdvafgpeNL-------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIaGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 628 AVLgNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG1122 149 LAM-EPEVLVLDEPTAGLDPRGRRELLELLKrLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
478-689 |
5.72e-41 |
|
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: 149.95 E-value: 5.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--- 554
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIGICPQSdmnF---DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:cd03255 81 RRHIGFVFQS---FnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 632 NPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
478-691 |
1.05e-40 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 148.90 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNetveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKM 557
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIiqevQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQGML 691
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLiSSHLLSEIQKVADRIGIINKGKL 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
478-688 |
5.27e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 146.86 E-value: 5.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRkkNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARkm 557
Cdd:COG4133 3 LEAENLSCRRG--ERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIiqEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHfmDEADILADRKAVISQ 688
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAaHLARGGAVLLTTH--QPLELAAARVLDLGD 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
475-691 |
1.05e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 143.65 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 475 KEAIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA 554
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 ---RKMIGICPQSdmnF---DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:COG1136 82 rlrRRHIGFVFQF---FnllPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADIlADRKAVISQGML 691
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
477-689 |
1.52e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.38 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemfeARK 556
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 637 LLDEPTAGMDPCSRHIVWN-LLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG1116 161 LMDEPFGALDALTRERLQDeLLRLWQETGKTVlFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
479-689 |
2.92e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.99 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 479 RISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMI 558
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-LEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 559 GICPQsdmnfdvltveenlsilasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29170396 639 DEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTViIVTHDPELAELAADRVIVLKDG 156
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
478-788 |
4.56e-37 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 151.70 E-value: 4.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVseIDEMFEARKM 557
Cdd:TIGR01257 1938 LRLNELTKVY--SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 638 LDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSSIFLKSKWGIGYRLSMYI-- 714
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNtIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIks 2173
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 715 ---DRYCATESLSSLVRQHIPAAALLQQNDQQIVYSLPFKDMDKfsgLFSALDIHSN-LGVISYGVSMTTLEDVFLKL 788
Cdd:TIGR01257 2174 pkdDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLAR---IFQLLISHKDsLLIEEYSVTQTTLDQVFVNF 2248
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
478-689 |
1.03e-36 |
|
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: 138.40 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKneTVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:cd03261 1 IELRGLTKSFGGR--TV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEvqKVLLDLDMQAIKDNQAKK---LSGGQKRKLSLGIAVLGN 632
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIRE--IVLEKLEAVGLRGAEDLYpaeLSGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 633 PKILLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFS-THFMDEADILADRKAVISQG 689
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLiRSLKKELGLTSIMvTHDLDTAFAIADRIAVLYDG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
497-643 |
1.28e-36 |
|
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: 135.08 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEaRKMIGICPQSDMNFDVLTVEEN 576
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 577 LSILASVKGIPANNIIQEVQKVLLDLDMQAIKD----NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-689 |
2.82e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 140.35 E-value: 2.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeiDEMFEARK 556
Cdd:PRK13536 41 AIDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDmNFDV-LTVEENLSILASVKGIPANNIiQEVQKVLLDL-DMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK13536 115 RIGVVPQFD-NLDLeFTVRENLLVFGRYFGMSTREI-EAVIPSLLEFaRLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 635 ILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTIlLTTHFMEEAERLCDRLCVLEAG 248
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
497-691 |
4.95e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.63 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDeMFEARKMIGICPQ-SDMNFDvlTV 573
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG--EIYldGKPLSAMP-PPEWRRQVAYVPQePALWGG--TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EENLSILASVKGIPANniIQEVQKVL--LDLDmQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:COG4619 91 RDNLPFPFQLRERKFD--RERALELLerLGLP-PDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29170396 652 IVWNLLK-YRKANRVTVFS-THFMDEADILADRKAVISQGML 691
Cdd:COG4619 168 RVEELLReYLAEEGRAVLWvSHDPEQIERVADRVLTLEAGRL 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-689 |
9.84e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.47 E-value: 9.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARK 556
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQ-----SDMnfdvlTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:COG4152 72 RIGYLPEerglyPKM-----KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 632 NPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTViFSSHQMELVEELCDRIVIINKG 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
478-689 |
1.18e-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: 131.49 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfEARKM 557
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP---PERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29170396 638 LDEPTAGMDPCSR-HIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03259 154 LDEPLSALDAKLReELREELKELQRELGITtIYVTHDQEEALALADRIAVMNEG 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-689 |
1.22e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 134.55 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKneTVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARK 556
Cdd:PRK13537 7 PIDFRNVEKRYGDK--LV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDmNFDV-LTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13537 81 RVGVVPQFD-NLDPdFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQG 689
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILlTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
478-689 |
1.52e-34 |
|
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: 131.25 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRkkneTVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARKM 557
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-----IAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29170396 638 LDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDvIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
475-691 |
4.04e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 130.92 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 475 KEAIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFea 554
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIGIC--PQSDMNFDvLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03267 93 LRRIGVVfgQKTQLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 633 PKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKeYNRERGTTVlLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
478-689 |
6.62e-34 |
|
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: 127.88 E-value: 6.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03228 1 IEFKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD-LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDvLTVEENLsilasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03228 78 IAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
478-689 |
1.01e-33 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 129.59 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFE-ARK 556
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-LPMHKrARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29170396 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQG 689
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEG 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
478-696 |
2.14e-33 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 128.96 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKV--LLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELlaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 636 LLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
477-696 |
1.23e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.80 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARK 556
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQS-DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 636 LLLDEPTAGMDPCSRH-IVWNLLKYRKANRVTVFS-THFMDEAdILADRKAVISQGMLKCVGS 696
Cdd:PRK13632 164 IIFDESTSMLDPKGKReIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
477-689 |
1.28e-32 |
|
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: 126.63 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEA 554
Cdd:COG1127 5 MIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIGICPQSDMNFDVLTVEENLSI-LASVKGIPANNIIqevQKVLLDLDMQAIKDNQAKK---LSGGQKRKLSLGIAVL 630
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFpLREHTDLSEAEIR---ELVLEKLELVGLPGAADKMpseLSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 631 GNPKILLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFS-THFMDEADILADRKAVISQG 689
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELiRELRDELGLTSVVvTHDLDSAFAIADRVAVLADG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
478-689 |
2.34e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 125.24 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS-----EIdemf 552
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpphER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 553 eARKMIGICPQSDMNFDVLTVEENLsILASVKGIPANN--IIQEVqkvlLDL--DMQAIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:cd03224 73 -ARAGIGYVPEGRRIFPELTVEENL-LLGAYARRRAKRkaRLERV----YELfpRLKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQG 689
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILlVEQNARFALEIADRAYVLERG 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
478-689 |
4.99e-32 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 124.54 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE--MFEAR 555
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQSDMN-FD-VLTVE----ENLSILASVKGIPANNIIQEVQKVLLDLDmQAIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:cd03257 82 KEIQMVFQDPMSsLNpRMTIGeqiaEPLRIHGKLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 630 LGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKkLQEELGLTLlFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
478-689 |
5.30e-32 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 124.62 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQsdmNFDVL---TVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 633 PKILLLDEPTAGMDPCSRHIVWNLLkyRKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALL--RDINRelgLTiVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
478-691 |
9.49e-32 |
|
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: 123.83 E-value: 9.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP-----PSDGFASIYGHRVSEIDEMF 552
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 553 EA-RKMIGICPQSDMNFDvLTVEENLSILASVKGIPANNIIQE-VQKVLLDLDM-QAIKDNQ-AKKLSGGQKRKLSLGIA 628
Cdd:cd03260 77 LElRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
475-699 |
4.69e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 475 KEAIRISGIQkaYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEA 554
Cdd:PRK13635 3 EEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE-ETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIGICPQS-DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GIAVLgN 632
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIaGVLAL-Q 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKAN-RVTVFS-THFMDEAdILADRKAVISQGMLKCVG--SSIF 699
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGtpEEIF 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-691 |
8.62e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.73 E-value: 8.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemfeARK 556
Cdd:COG1121 6 AIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQ-SDMNFDV-LTVEE----NLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:COG1121 76 RIGYVPQrAEVDWDFpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 631 GNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTIlVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
477-689 |
1.00e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 127.71 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGHRVSEIDEmFE 553
Cdd:COG1123 4 LLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE-AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 554 ARKMIGICPQSDMN-FDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:COG1123 81 RGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTtvLLITHDLGVVAEIADRVVVMDDG 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
474-689 |
2.48e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.56 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 474 GKEAIRISGIQKAYR-KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEID- 549
Cdd:COG1123 257 AEPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSG--SILfdGKDLTKLSr 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 550 -EMFEARKMIGICPQ--SDMNFDVLTVEENLS-ILASVKGIPANNIIQEVQKVL----LDLDMqaikdnqAKK----LSG 617
Cdd:COG1123 335 rSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAePLRLHGLLSRAERRERVAELLervgLPPDL-------ADRypheLSG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29170396 618 GQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdLQRELGLTyLFISHDLAVVRYIADRVAVMYDG 481
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
477-696 |
3.17e-30 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 120.15 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR-ELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQS-DMNFDvLTVEE--------NLSILASvkgiPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGI 627
Cdd:COG1120 76 RIAYVPQEpPAPFG-LTVRElvalgrypHLGLFGR----PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
479-671 |
1.18e-29 |
|
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: 116.97 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 479 RISGIQKAYRKKNETveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemFEARKMI 558
Cdd:cd03226 1 RIENISFSYKKGTEI---LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 559 GICPQ-SDMNFDVLTVEENLSIlaSVKGIPANNiiQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLL--GLKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190
....*....|....*....|....*....|....*
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STH 671
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIvITH 184
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
477-696 |
1.55e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.95 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDEmfeA 554
Cdd:COG3839 3 SLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG--EILigGRDVTDLPP---K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 635 ILLLDEPTAGMDPCSRhivWNL---LKY--RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG3839 154 VFLLDEPLSNLDAKLR---VEMraeIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
477-691 |
1.83e-29 |
|
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: 117.98 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARK 556
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 --MIGICPQSDMNfDVLTVEENLSILASVKGIPanNIIQEVQKVLLDLDM-QAIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:COG1124 81 vqMVFQDPYASLH-PRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 634 KILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQGML 691
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKdLREERGLTyLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
478-691 |
2.43e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.69 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:COG2884 2 IRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQsdmNF---DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:COG2884 79 RRIGVVFQ---DFrllPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHfmdEADILADRKA---VISQGML 691
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLiATH---DLELVDRMPKrvlELEDGRL 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
496-676 |
3.36e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 125.62 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemFEARKMIGICPQSdmnFDV---LT 572
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD--IATRRRVGYMSQA---FSLygeLT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 573 VEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180
....*....|....*....|....*.
gi 29170396 653 VWNLL-KYRKANRVTVF-STHFMDEA 676
Cdd:NF033858 436 FWRLLiELSREDGVTIFiSTHFMNEA 461
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
478-656 |
3.88e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.67 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKneTVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFE-ARK 556
Cdd:COG1137 4 LEAENLVKSYGKR--TV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP-MHKrARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180
....*....|....*....|....
gi 29170396 637 LLDEPTAGMDPCS----RHIVWNL 656
Cdd:COG1137 159 LLDEPFAGVDPIAvadiQKIIRHL 182
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
477-710 |
1.01e-28 |
|
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: 122.18 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG4987 333 SLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED-DLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDMNFDVlTVEENLSIlasvkgipANN------IIQEVQKVLLD---------LDMQAikDNQAKKLSGGQKR 621
Cdd:COG4987 410 RIAVVPQRPHLFDT-TLRENLRL--------ARPdatdeeLWAALERVGLGdwlaalpdgLDTWL--GEGGRRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGMLKCVGSSIFLK 701
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELL 557
|
....*....
gi 29170396 702 SKWGIGYRL 710
Cdd:COG4987 558 AQNGRYRQL 566
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
477-710 |
1.02e-28 |
|
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: 123.41 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDeMFEA 554
Cdd:COG2274 473 DIELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG--RILidGIDLRQID-PASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIGICPQSDMNFDVlTVEENLSIlaSVKGIPANNIIQEVQKVLLD---------LDMQaIKDNqAKKLSGGQKRKLSL 625
Cdd:COG2274 548 RRQIGVVLQDVFLFSG-TIRENITL--GDPDATDEEIIEAARLAGLHdfiealpmgYDTV-VGEG-GSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHfmDEADI-LADRKAVISQGMLKCVGSSIFLKSKW 704
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH--RLSTIrLADRIIVLDKGRIVEDGTHEELLARK 700
|
....*.
gi 29170396 705 GIGYRL 710
Cdd:COG2274 701 GLYAEL 706
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
496-704 |
1.34e-28 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 116.01 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMFEARKMIGIC---PQSDMnFDv 570
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItaKKKKKLKDLRKKVGLVfqfPEHQL-FE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 571 LTVEE-------NLsilasvkGIPANNIIQEVQKVL--LDLDmQAIKDNQAKKLSGGQKRKLSlgIA-VLG-NPKILLLD 639
Cdd:TIGR04521 98 ETVYKdiafgpkNL-------GLSEEEAEERVKEALelVGLD-EEYLERSPFELSGGQMRRVA--IAgVLAmEPEVLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 640 EPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSS--IFLKSKW 704
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKrlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPreVFSDVDE 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
477-689 |
2.04e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 114.77 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKnetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEA 554
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIGICPQsdmNFDV---LTVEEN--------LSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKL 623
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 624 slGIA--VLGNPKILLLDEPTAGMDPCSRHIVWNLLkyRKANR---VTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG3638 156 --AIAraLVQEPKLILADEPVASLDPKTARQVMDLL--RRIARedgITVvVNLHQVDLARRYADRIIGLRDG 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
478-695 |
2.48e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.50 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM 557
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
495-689 |
2.75e-28 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 113.77 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTVE 574
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLSILASVKGIPANNIIQEVqkvlLDLdMQAIKDNQAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPcsrH 651
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIPDEI----YEL-FPVLKEMLGRRggdLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP---S 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29170396 652 IVWN----LLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:TIGR03410 166 IIKDigrvIRRLRAEGGMAIlLVEQYLDFARELADRYYVMERG 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
478-689 |
3.13e-28 |
|
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: 111.90 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV-SEIDEMFEARK 556
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDMNFDVLTVEENLSILasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 637 LLDEPTAGMDPCSRHIVWNLLKYRKANR-VTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLgITVvLVTHDLDEAARLADRVVVLRDG 177
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
477-689 |
3.20e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.12 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfEARK 556
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL----PPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 -MIGICPQSDMNFDVLTVEEN----LsilaSVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLG--IAV 629
Cdd:COG3842 77 rNVGMVFQDYALFPHLTVAENvafgL----RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAraLAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 630 lgNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG3842 153 --EPRVLLLDEPLSALDAKLREEMREELRrLQRELGITfIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
497-671 |
4.99e-28 |
|
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: 111.87 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCG-LCPPSD-GFASIYGHRVSeideMFEARKMIGICPQSDMNFDVLTVE 574
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRPLD----KRSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLSILASVKGIpanniiqevqkvlldldmqaikdnqakklSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVW 654
Cdd:cd03213 101 ETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170
....*....|....*...
gi 29170396 655 NLLK-YRKANRVTVFSTH 671
Cdd:cd03213 152 SLLRrLADTGRTIICSIH 169
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
478-689 |
5.48e-28 |
|
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: 113.30 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---F--ASIYGHRVSEIdemf 552
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlFdgEDITGLPPHEI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 553 eARKmiGIC-----PQSdmnFDVLTVEENLSI-------LASVKGIPANNIIQEVQKV--LLD-LDMQAIKDNQAKKLSG 617
Cdd:cd03219 73 -ARL--GIGrtfqiPRL---FPELTVLENVMVaaqartgSGLLLARARREEREARERAeeLLErVGLADLADRPAGELSY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 618 GQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVlLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
477-696 |
8.94e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 112.82 E-value: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfeaRK 556
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDMNFDVLTVEENLSILASVKGI----PANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 633 PKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRrlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
495-691 |
9.95e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.86 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfeaRKMIGICPQS-DMNFDV-LT 572
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVPQRrSIDRDFpIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 573 VEENLSiLASVKGIPANNII-----QEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:cd03235 87 VRDVVL-MGLYGHKGLFRRLskadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29170396 648 CSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03235 166 KTQEDIYELLReLRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
490-701 |
2.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.97 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFAS---IYGHRVSEiDEMFEARKMIGICPQS-D 565
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTA-KTVWDIREKVGIVFQNpD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 566 MNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GIAVLGnPKILLLDEPTAG 644
Cdd:PRK13640 95 NQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIaGILAVE-PKIIILDESTSM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 645 MDPCSRHIVWNLL-KYRKANRVTVFS-THFMDEADiLADRKAVISQGMLKCVGS--SIFLK 701
Cdd:PRK13640 174 LDPAGKEQILKLIrKLKKKNNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSpvEIFSK 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
478-689 |
2.18e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.40 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEID--EMFE 553
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSG--SVLvdGVDLTALSerELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 554 ARKMIGICPQsdmNFDVL---TVEEN----LSILasvkGIPANNIIQEVQKvLLDL-DMQAIKDNQAKKLSGGQKRKlsL 625
Cdd:COG1135 80 ARRKIGMIFQ---HFNLLssrTVAENvalpLEIA----GVPKAEIRKRVAE-LLELvGLSDKADAYPSQLSGGQKQR--V 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 626 GIA-VL-GNPKILLLDEPTAGMDPCSRHIVWNLLKyrKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1135 150 GIArALaNNPKVLLCDEATSALDPETTRSILDLLK--DINRelgLTiVLITHEMDVVRRICDRVAVLENG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
494-647 |
9.05e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 109.69 E-value: 9.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FA--SIYGHRVSEIdemfeARKMIGICPQSDMNF 568
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirFDgeDITGLPPHRI-----ARLGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVLTVEENLsILASVKGIPANNIIQEVQKVLlDL--DMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG0410 91 PSLTVEENL-LLGAYARRDRAEVRADLERVY-ELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
.
gi 29170396 647 P 647
Cdd:COG0410 169 P 169
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
477-696 |
1.24e-26 |
|
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: 115.63 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG4988 336 SIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA-SWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDMNFDvLTVEENLSILASvkGIPANNIIQEVQKVLLD---------LDMQaIKDNqAKKLSGGQKRKLSLGI 627
Cdd:COG4988 412 QIAWVPQNPYLFA-GTIRENLRLGRP--DASDEELEAALEAAGLDefvaalpdgLDTP-LGEG-GRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHfmDEADI-LADRKAVISQGMLKCVGS 696
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
499-691 |
2.28e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 107.77 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 499 NLSFDIyEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRVseideMFEARKMIGICP---------QSDMNFD 569
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTV-----LFDSRKKINLPPqqrkiglvfQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 570 VLTVEENlsILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:cd03297 89 HLNVREN--LAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29170396 650 RHIVWNLLKYRKA--NRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
479-695 |
2.40e-26 |
|
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: 106.75 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 479 RISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMI 558
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK-ELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 559 GICPQsdmnfdvltveenlsilasvkgipanniiqevqkVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd03214 76 AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 639 DEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
478-689 |
2.56e-26 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 108.42 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS--EIDEMFEAR 555
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQSDMNFDVLTVEEN-----LSILASVKGIPANNIIQEVQKVLLDLDMQAIKD---NQAKKLSGGQKRKLSLGI 627
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDkayQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29170396 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
478-694 |
2.57e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKN--ETVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIYGHRVSEIDE---MF 552
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEKK-ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSG--KIIIDGVDITDKkvkLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 553 EARKMIGIC---PQSDMnFDVlTVEENLSILASVKGIPANNIIQEVQKV--LLDLDMQAIKDNQAKKLSGGQKRKLSLGI 627
Cdd:PRK13637 80 DIRKKVGLVfqyPEYQL-FEE-TIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGmlKCV 694
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVAKLADRIIVMNKG--KCE 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
489-689 |
2.61e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.44 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQS-DMN 567
Cdd:PRK13650 15 KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE-ENVWDIRHKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 568 FDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13650 94 FVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29170396 648 CSR-HIVWNLLKYRKANRVTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13650 174 EGRlELIKTIKGIRDDYQMTVISiTHDLDEV-ALSDRVLVMKNG 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
478-676 |
2.86e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKK--NETVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEAR 555
Cdd:COG1101 2 LELKNLSKTFNPGtvNEKR-ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 K--------MIGICPQsdmnfdvLTVEENLSiLASVKG-----IPANNI--IQEVQKVL--LDLDMQAIKDNQAKKLSGG 618
Cdd:COG1101 81 YigrvfqdpMMGTAPS-------MTIEENLA-LAYRRGkrrglRRGLTKkrRELFRELLatLGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 619 QKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYR-KANRVTVFS-THFMDEA 676
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMvTHNMEQA 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
478-696 |
4.92e-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: 107.32 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM 557
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP---HKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 638 LDEPTAGMDpcsrhivwnlLKYRKANRVT------------VFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03300 154 LDEPLGALD----------LKLRKDMQLElkrlqkelgitfVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
488-671 |
5.47e-26 |
|
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: 106.97 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLcppSDGFASIYGH-----RVSEIDEMfeaRKMIGICP 562
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGTTSGQilfngQPRKPDQF---QKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 563 QSDMNFDVLTVEENLSILASVKG--IPANNIIQEV--QKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190
....*....|....*....|....*....|....
gi 29170396 639 DEPTAGMDPCSRH-IVWNLLKYRKANRVTVFSTH 671
Cdd:cd03234 168 DEPTSGLDSFTALnLVSTLSQLARRNRIVILTIH 201
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
478-689 |
5.77e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 110.24 E-value: 5.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRkkneTVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRVSEIDEMFEARKm 557
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL-NGRDLFTNLPPRERR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKvLLDL-DMQAIKD---NQakkLSGGQKRKLSLGIAVLGNP 633
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEE-LLELvQLEGLADrypSQ---LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 634 KILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRrlHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
474-696 |
6.00e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 474 GKEAIRISGIQKAYRKKNETVE--ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEM 551
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 552 FEARKMIGICPQSDMNFDVLT-VEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 631 GNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEAdILADRKAVISQGMLKCVGS 696
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
488-695 |
6.10e-26 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 108.11 E-value: 6.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR-KMIGICPQS 564
Cdd:cd03294 31 LKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkELRELRrKKISMVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 565 DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:cd03294 111 FALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29170396 645 MDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03294 191 LDPLIRREMQDELLrlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
478-696 |
6.67e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 104.82 E-value: 6.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeIDEMFEARKM 557
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-FASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 -IGICPQsdmnfdvltveenlsilasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03216 76 gIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGmlKCVGS 696
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAViFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
478-689 |
1.14e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.12 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQsdmNFDVL---TVEENLSILASVKGIPANNIIQEVQKvLLDL-DMQAIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:PRK11153 82 RQIGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKARVTE-LLELvGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 632 NPKILLLDEPTAGMDPCSRHIVWNLLKyrKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLK--DINRelgLTiVLITHEMDVVKRICDRVAVIDAG 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
488-728 |
1.36e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 108.64 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeaRKMIGIcpqsdmn 567
Cdd:COG4586 29 RREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEF--ARRIGV------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 568 fdV----------LTVEENLSILASVKGIPaNNIIQEVQKVLLD-LDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:COG4586 100 --VfgqrsqlwwdLPAIDSFRLLKAIYRIP-DAEYKKRLDELVElLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 637 LLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVF-STHFMDeaDI--LADRKAVISQGMLKCVGSSIFLKSKWGIGYRLSM 712
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKeYNRERGTTILlTSHDMD--DIeaLCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVL 254
|
250
....*....|....*.
gi 29170396 713 YIDRYCATESLSSLVR 728
Cdd:COG4586 255 ELAEPVPPLELPRGGE 270
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
484-691 |
1.46e-25 |
|
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: 105.57 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 484 QKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--RKMIGIC 561
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 562 PQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29170396 642 TAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKkINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
494-647 |
1.87e-25 |
|
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: 106.28 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FA--SIYGHRVSEIdemfeARKmiGIC-----PQ 563
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGrilFDgrDITGLPPHRI-----ARL--GIArtfqnPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 564 SdmnFDVLTVEENL----------SILASVKGIPAN-----NIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:COG0411 90 L---FPELTVLENVlvaaharlgrGLLAALLRLPRArreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170
....*....|....*....
gi 29170396 629 VLGNPKILLLDEPTAGMDP 647
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNP 185
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
494-676 |
2.76e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 104.04 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEID----EMFEARKMIGICPQS-DMNF 568
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG---EPLDysrkGLLERRQRVGLVFQDpDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*....
gi 29170396 649 SRHIVWNLL-KYRKANRVTVFSTHFMDEA 676
Cdd:TIGR01166 162 GREQMLAILrRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
497-703 |
4.64e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 104.73 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKMIGICPQSDMNFDVLTVEEN 576
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDITNLPPEKRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 LSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNL 656
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29170396 657 LK-YRKANRVTVFS-THFMDEADILADRKAVISQGMLKCVGS--SIFLKSK 703
Cdd:cd03299 172 LKkIRKEFGVTVLHvTHDFEEAWALADKVAIMLNGKLIQVGKpeEVFKKPK 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
487-689 |
5.98e-25 |
|
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: 103.82 E-value: 5.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 487 YRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDM 566
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 567 NFDVlTVEENLS----------ILASVKGIPANNIiqeVQKVLLDLDMQaIKDnQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03245 89 LFYG-TLRDNITlgapladderILRAAELAGVTDF---VNKHPNGLDLQ-IGE-RGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29170396 637 LLDEPTAGMDPCS-RHIVWNLLKYRkANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03245 163 LLDEPTSAMDMNSeERLKERLRQLL-GDKTLIIITHRPSLLD-LVDRIIVMDSG 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
496-689 |
6.67e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.22 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQSDMN-------- 567
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DNFEKLRKHIGIVFQNPDNqfvgsivk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 568 FDVLTVEENLSIlasvkgiPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMD 646
Cdd:PRK13648 103 YDVAFGLENHAV-------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIaGVLAL-NPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29170396 647 PCSRHIVWNLLKYRKANR-VTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHnITIISiTHDLSEA-MEADHVIVMNKG 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
477-696 |
1.39e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.32 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfEAR- 555
Cdd:PRK10851 2 SIEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL----HARd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQSDMNFDVLTVEEN----LSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 632 NPKILLLDEPTAGMDPCSRHIV--W-----NLLKYrkanrVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELrrWlrqlhEELKF-----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
478-689 |
2.43e-24 |
|
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: 100.75 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIqkAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN-ELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDvltveenlsilasvkGIPANNIiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03246 78 VGYLPQDDELFS---------------GSIAENI-----------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMdEADILADRKAVISQG 689
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATrIVIAHRP-ETLASADRILVLEDG 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
497-675 |
8.30e-24 |
|
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: 101.31 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF-ASIYGHRVSEIDeMFEARKMIGIC-PQSDMNFDV-LTV 573
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED-VWELRKRIGLVsPALQLRFPRdETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EEN-LSILASVKGIPAN---NIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:COG1119 98 LDVvLSGFFDSIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGA 177
|
170 180
....*....|....*....|....*...
gi 29170396 650 RHIVWNLLKY--RKANRVTVFSTHFMDE 675
Cdd:COG1119 178 RELLLALLDKlaAEGAPTLVLVTHHVEE 205
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
478-689 |
1.08e-23 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 100.84 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQSDMNFDVLTVEENLSI--LASVKGIPAnnII-----QEVQKVLLDLDMQAIKD---NQAKKLSGGQKRKLSL 625
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVLHgrLGYKPTWRS--LLgrfseEDKERALSALERVGLADkayQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
460-689 |
1.61e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 106.87 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 460 SLNEIVE-----PVSSEFIGKE----AIRISGIQKAYrkKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGL 530
Cdd:TIGR03375 437 SLDELMQlpverPEGTRFLHRPrlqgEIEFRNVSFAY--PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGL 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 531 CPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMNFDVlTVEENL----------SILASVKGIPANNIIQEVQKvll 600
Cdd:TIGR03375 515 YQPTEGSVLLDGVDIRQID-PADLRRNIGYVPQDPRLFYG-TLRDNIalgapyaddeEILRAAELAGVTEFVRRHPD--- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 601 DLDMQAIKDNQAkkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLA 680
Cdd:TIGR03375 590 GLDMQIGERGRS--LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLD-LV 666
|
....*....
gi 29170396 681 DRKAVISQG 689
Cdd:TIGR03375 667 DRIIVMDNG 675
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
495-689 |
2.64e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS-EIDEMFEARKMIGICPQ-SDMNFDVLT 572
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQnPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 573 VEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 29170396 653 VWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13639 176 IMKLLYDLNKEGITiIISTHDVDLVPVYADKVYVMSDG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
459-682 |
3.04e-23 |
|
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: 104.68 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 459 ISLNEIVEPVSSEFIGKEA--IRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG 536
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAAPAssLEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 537 FASIYGHRVSEIDEMFeARKMIGICPQSDMNFDVlTVEENlsILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKK-- 614
Cdd:TIGR02857 378 SIAVNGVPLADADADS-WRDQIAWVPQHPFLFAG-TIAEN--IRLARPDASDAEIREALERAGLDEFVAALPQGLDTPig 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 615 -----LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR-HIVWNLLKYRKaNRVTVFSTHfmDEADI-LADR 682
Cdd:TIGR02857 454 eggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEaEVLEALRALAQ-GRTVLLVTH--RLALAaLADR 525
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
497-704 |
4.77e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDEMFEARKMIGICPQsdmnFDVLTV 573
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpeTGNKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EENlSILASVKGIPAN----------NIIQEVQKVLLDLDMQaikDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNfgfsedeakeKALKWLKKVGLSEDLI---SKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29170396 644 GMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS--SIFLKSKW 704
Cdd:PRK13641 175 GLDPEGRKEMMQLFKdYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASpkEIFSDKEW 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
496-696 |
5.10e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfeaRKMIGICPQSDMNFDVLTVEE 575
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINMMFQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR----H 651
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdrmqL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29170396 652 IVWNLLKYRKANRVTVfsTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK11607 191 EVVDILERVGVTCVMV--THDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
487-689 |
8.37e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.42 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 487 YRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmFEARKMIGICPQ--S 564
Cdd:PRK13647 12 FRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE-KWVRSKVGLVFQdpD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 565 DMNFDVlTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:PRK13647 90 DQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29170396 645 MDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13647 169 LDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
489-689 |
8.47e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.40 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQS-DMN 567
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 568 FDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13642 94 FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29170396 648 CSRHIVWNLL-KYRKANRVTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13642 174 TGRQEIMRVIhEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
478-689 |
8.86e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.07 E-value: 8.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03254 3 IEFENVNFSYDEKKPV---LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK-SLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVlTVEENLS----------ILASVKGIPANNIIQEVQKvllDLDMQAikDNQAKKLSGGQKRKLSLGI 627
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRlgrpnatdeeVIEAAKEAGAHDFIMKLPN---GYDTVL--GENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMD---EAD--ILADRKAVISQG 689
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNADkiLVLDDGKIIEEG 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
497-658 |
1.32e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 103.59 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGHRVsEIDEMfeaRKMIGICPQSDMNFDVLTV 573
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEM---RAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EENLSILASVK---GIPANNIIQEVQKVLLDLDMQAIKD------NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:TIGR00955 117 REHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170
....*....|....
gi 29170396 645 MDPCSRHIVWNLLK 658
Cdd:TIGR00955 197 LDSFMAYSVVQVLK 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
478-695 |
1.41e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.56 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKM 557
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSI----LASVKGIPA---NNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 631 GNPKILLLDEPTAGM-DPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK09700 162 LDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
478-689 |
2.65e-22 |
|
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: 96.06 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS----EIDEMfe 553
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 554 aRKMIGICPQSDMNFDVLTVEENLSI-LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03262 75 -RQKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTmVVVTHEMGFAREVADRVIFMDDG 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
476-689 |
2.95e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 476 EAIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfeAR 555
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KmiGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:COG4525 78 R--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 636 LLLDEPTAGMDPCSR-HIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQG 689
Cdd:COG4525 156 LLMDEPFGALDALTReQMQELLLDVWQRTGKGVFlITHSVEEALFLATRLVVMSPG 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
512-697 |
4.11e-22 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 98.33 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 512 LLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQSDMNFDVLTVEENLSILASVKGIPANNI 591
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP---HLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 592 IQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFS 669
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITFVFV 157
|
170 180
....*....|....*....|....*...
gi 29170396 670 THFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
496-696 |
5.95e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.95 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTVEE 575
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRKFQKPTVFEELTVFE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NL--------SILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:COG4674 105 NLelalkgdrGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29170396 648 CSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4674 185 AETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
499-689 |
6.96e-22 |
|
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: 94.87 E-value: 6.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 499 NLSFD--IYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQSDMNFDVLTVEEN 576
Cdd:cd03298 14 PMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 LSiLASVKGIPANNIIQE-VQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN 655
Cdd:cd03298 91 VG-LGLSPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 29170396 656 L-LKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03298 170 LvLDLHAETKMTVlMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
483-696 |
9.11e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.35 E-value: 9.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 483 IQKAYrKKNETVEalrNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICP 562
Cdd:PRK10895 9 LAKAY-KGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 563 QSDMNFDVLTVEENL-SILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PRK10895 85 QEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 642 TAGMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
487-710 |
1.11e-21 |
|
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: 94.86 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 487 YRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQSDM 566
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW-LRRQVGVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 567 NFDvLTVEENLS----------ILASVKGIPANNIIQEvqkvlLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03252 87 LFN-RSIRDNIAladpgmsmerVIEAAKLAGAHDFISE-----LPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29170396 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMdEADILADRKAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
478-647 |
1.22e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 94.68 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS----EIDEMfe 553
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 554 aRKMIGICPQSdMN-FDVLTVEENLsILA--SVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQK------RKLS 624
Cdd:COG1126 76 -RRKVGMVFQQ-FNlFPHLTVLENV-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQqrvaiaRALA 152
|
170 180
....*....|....*....|...
gi 29170396 625 LgiavlgNPKILLLDEPTAGMDP 647
Cdd:COG1126 153 M------EPKVMLFDEPTSALDP 169
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
477-696 |
1.44e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.33 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVsEIDEMFEA 554
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG--EILidGKPV-RIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKM-IGICPQSDMNFDVLTVEENLsILASVKG----IPANNIIQEVQKVL----LDLDMQA-IKDnqakkLSGGQKRKLS 624
Cdd:COG3845 78 IALgIGMVHQHFMLVPNLTVAENI-VLGLEPTkggrLDRKAARARIRELSerygLDVDPDAkVED-----LSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 625 lgI--AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGmlKCVGS 696
Cdd:COG3845 152 --IlkALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIiFITHKLREVMAIADRVTVLRRG--KVVGT 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
497-689 |
1.56e-21 |
|
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: 94.45 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE--IDEMfearkmigICPQSDMNFDVLTVE 574
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLSIlaSVKGIPANNIIQEVQKVLLD-LDMQAIKDNQAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR 650
Cdd:TIGR01184 73 ENIAL--AVDRVLPDLSKSERRAIVEEhIALVGLTEAADKRpgqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29170396 651 -HIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR01184 151 gNLQEELMQIWEEHRVTvLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
479-671 |
2.01e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 479 RISGIQKAYRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRvSEIDEMFEARKMI 558
Cdd:PRK13539 2 MLEGEDLACVRGGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 559 GicPQSDMNfDVLTVEENLSILASVKGIPANNIIQevqkVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PRK13539 79 G--HRNAMK-PALTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 29170396 639 DEPTAGMDPCSRHIVWNLLKYR-KANRVTVFSTH 671
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHlAQGGIVIAATH 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
474-696 |
3.26e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.69 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 474 GKEAIRISGIQKAY-RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASI------------ 540
Cdd:PRK13631 18 DDIILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 541 ---YGHRVSEIDEMFEARKMIGIC---PQSDMNFDvlTVEENLSILASVKGIPANNIIQEVQKVL--LDLDMQAIkDNQA 612
Cdd:PRK13631 98 eliTNPYSKKIKNFKELRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLnkMGLDDSYL-ERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 613 KKLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFS-THFMDEADILADRKAVISQGM 690
Cdd:PRK13631 175 FGLSGGQKRRVAIaGILAI-QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFViTHTMEHVLEVADEVIVMDKGK 253
|
....*.
gi 29170396 691 LKCVGS 696
Cdd:PRK13631 254 ILKTGT 259
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
497-680 |
4.41e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.54 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHRVSEIDEmfEARKmIGICPQSDMNFDVLTV 573
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRR-IGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EENLSiLASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR--- 650
Cdd:COG4136 94 GENLA-FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRaqf 172
|
170 180 190
....*....|....*....|....*....|.
gi 29170396 651 -HIVWNLLkyRKANRVTVFSTHfmDEADILA 680
Cdd:COG4136 173 rEFVFEQI--RQRGIPALLVTH--DEEDAPA 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
480-658 |
4.60e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 480 ISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA---RK 556
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlrRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180
....*....|....*....|..
gi 29170396 637 LLDEPTAGMDPCSRHIVWNLLK 658
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILH 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
477-682 |
4.85e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRkkneTVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVsEIDEMFEARK 556
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 M-IGICPQsDMN-FDVLTVEENLSI--LASVKG-IPANNIIQEVQKVL----LDLDMQAIkdnqAKKLSGGQKRKLSLGI 627
Cdd:COG1129 79 AgIAIIHQ-ELNlVPNLSVAENIFLgrEPRRGGlIDWRAMRRRARELLarlgLDIDPDTP----VGDLSVAQQQLVEIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADR 682
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAiIYISHRLDEVFEIADR 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
477-647 |
7.58e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 7.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS---EIDE--M 551
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 552 FEARKMIGICPQSDMNFDVLTVEENLsILASVK--GIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170
....*....|....*...
gi 29170396 630 LGNPKILLLDEPTAGMDP 647
Cdd:COG4161 157 MMEPQVLLFDEPTAALDP 174
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
487-710 |
1.10e-20 |
|
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: 91.91 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 487 YRKKNEtvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQSDM 566
Cdd:cd03251 10 YPGDGP--PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 567 NFDVlTVEENLS----------ILASVKGIPANNIIQEvqkvlLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03251 87 LFND-TVAENIAygrpgatreeVEEAARAANAHEFIME-----LPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH----FMDeadilADRKAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHrlstIEN-----ADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
475-703 |
1.19e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 475 KEAIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCP--PSDGFASIYGHRV-SEI 548
Cdd:PRK14239 3 EPILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPevTITGSIVYNGHNIySPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 549 DEMFEARKMIGICPQSDMNFDvLTVEENLSILASVKGIPANNIIQE-VQKVLLDLDM-QAIKD---NQAKKLSGGQKRKL 623
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEaVEKSLKGASIwDEVKDrlhDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 624 SLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS--SIFLK 701
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDtkQMFMN 237
|
..
gi 29170396 702 SK 703
Cdd:PRK14239 238 PK 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
478-696 |
1.20e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.01 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKm 557
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA--ENRH- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKAlqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
478-689 |
1.24e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.66 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:PRK15439 12 LCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 -IGICPQSDMNFDVLTVEENlsILAsvkGIPAN--------NIIQEVQkVLLDLDMQA----IKDNQAKKLSGGQKRkls 624
Cdd:PRK15439 87 gIYLVPQEPLLFPNLSVKEN--ILF---GLPKRqasmqkmkQLLAALG-CQLDLDSSAgsleVADRQIVEILRGLMR--- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 625 lgiavlgNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRV-TVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK15439 158 -------DSRILILDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADRISVMRDG 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
496-712 |
4.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.62 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRV--SEIDE--MFEARKMIGIC---PQSDMnF 568
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNkkLKPLRKKVGIVfqfPEHQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVlTVEENLSILASVKGIPANNIIQEVQKV--LLDLDmQAIKDNQAKKLSGGQKRKLSlgIA-VLG-NPKILLLDEPTAG 644
Cdd:PRK13634 100 EE-TVEKDICFGPMNFGVSEEDAKQKAREMieLVGLP-EELLARSPFELSGGQMRRVA--IAgVLAmEPEVLVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 645 MDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS--SIFLKSKWGIGYRLSM 712
Cdd:PRK13634 176 LDPKGRKEMMEMFYklHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPDELEAIGLDL 247
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
495-691 |
4.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG---HRVSEIDEMFEARKMIGIC---PQSDMNF 568
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIRPVRKRIGMVfqfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DvlTVEENLSILASVKGIPANNIIQEVQKVLLDLDM-QAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13646 101 D--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29170396 648 CSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13646 179 QSKRQVMRLLKslQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
478-696 |
5.02e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKM 557
Cdd:PRK13644 2 IRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQS-DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 637 LLDEPTAGMDPCS-RHIVWNLLKYRKANRVTVFSTHFMDEADIlADRKAVISQGMLKCVGS 696
Cdd:PRK13644 159 IFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
494-689 |
5.06e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTV 573
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EENLSIlasvKGIPAN--NIIQEVQKVL-LDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR 650
Cdd:PRK11614 98 EENLAM----GGFFAErdQFQERIKWVYeLFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29170396 651 HIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQG 689
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENG 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
478-689 |
5.46e-20 |
|
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: 89.48 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG-LHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVlTVEENL------------SILASVKgipannIIQEVQKVLLDLDMQaIKDNQaKKLSGGQKRKLSL 625
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLdpfgeysdeelwQALERVG------LKEFVESLPGGLDTV-VEEGG-ENLSVGQRQLLCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH----FMDeadilADRKAVISQG 689
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKG 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
487-689 |
5.93e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 487 YRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE-MFEARKMIGICPQS- 564
Cdd:PRK13636 13 YNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKgLMKLRESVGMVFQDp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 565 DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:PRK13636 92 DNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29170396 645 MDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13636 172 LDPMGVSEIMKLLVemQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
495-710 |
6.46e-20 |
|
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: 89.98 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSdmnfdvlTVE 574
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRAIGVVPQD-------TVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLSILASVK-GIP-ANN--IIQEVQKVLLDLDMQAIKDNQAK-------KLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:cd03253 87 FNDTIGYNIRyGRPdATDeeVIEAAKAAQIHDKIMRFPDGYDTivgerglKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 644 GMD-PCSRHIVWNLLKYRKaNRVTVFSTHFMDEAdILADRKAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:cd03253 167 ALDtHTEREIQAALRDVSK-GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
478-710 |
8.35e-20 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 89.52 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNEtVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVlTVEENLSIlasvkGipANNIIQEvqkvlldLDMQAIKD-------------------NQAKKLSGG 618
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRY-----G--KPDATDE-------EVEEAAKKanihdfimslpdgydtlvgERGSQLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 619 QKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMdeADIL-ADRKAVISQGMLKCVGSS 697
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL--STIRnADLIAVLQNGQVVEQGTH 221
|
250
....*....|...
gi 29170396 698 IFLKSKWGIGYRL 710
Cdd:cd03249 222 DELMAQKGVYAKL 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
478-691 |
8.73e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.16 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrEVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 636 LLLDEPTAGMDPCSRHIVWNLlkYRKANRVTV---FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRL--FEEFNRVGVtvlMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
495-671 |
1.42e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.69 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMNFDvLTVE 574
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT-LESLRRQIGVVPQDTFLFS-GTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLSIlasvkGIP-ANNiiQEVqkvlldldMQAIKDNQAK-------------------KLSGGQKRKLSLGIAVLGNPK 634
Cdd:COG1132 432 ENIRY-----GRPdATD--EEV--------EEAAKAAQAHefiealpdgydtvvgergvNLSGGQRQRIAIARALLKDPP 496
|
170 180 190
....*....|....*....|....*....|....*...
gi 29170396 635 ILLLDEPTAGMDPCS-RHIVWNLLKYRKaNRVTVFSTH 671
Cdd:COG1132 497 ILILDEATSALDTETeALIQEALERLMK-GRTTIVIAH 533
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
484-689 |
1.42e-19 |
|
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: 88.36 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 484 QKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhRVSEIDEMfearkMIGICPQ 563
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGL-----GGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 564 sdmnfdvLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:cd03220 99 -------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29170396 644 GMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTViLVSHDPSSIKRLCDRALVLEKG 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
495-671 |
1.48e-19 |
|
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: 93.19 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQSDMNFDVlTVE 574
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD-EVRRRVSVCAQDAHLFDT-TVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLSILAsvKGIPANNIIQEVQKVLLDLDMQAIKDN-------QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:TIGR02868 427 ENLRLAR--PDATDEELWAALERVGLADWLRALPDGldtvlgeGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....
gi 29170396 648 CSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITH 528
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
478-685 |
1.54e-19 |
|
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: 90.50 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHRVSEID--EMF 552
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 553 EAR-KMIGICPQSDMN-FD-VLTVEENLS-ILASVKGIPANNIIQEVQKVL----LDLDMQAIKD--NQakkLSGGQKRK 622
Cdd:COG0444 82 KIRgREIQMIFQDPMTsLNpVMTVGDQIAePLRIHGGLSKAEARERAIELLervgLPDPERRLDRypHE---LSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 623 LSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHfmdeaDI-----LADRKAV 685
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLaiLFITH-----DLgvvaeIADRVAV 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
478-689 |
1.66e-19 |
|
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: 86.98 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVltveenlsilasvkgipanniiqevqkvlldldmqAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03247 77 ISVLNQRPYLFDT-----------------------------------TLRNNLGRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH------FMDEAdILADRKAVISQG 689
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHhltgieHMDKI-LFLENGKIIMQG 178
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
496-691 |
1.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDEMFEARKMIGIC---PQSDMnfd 569
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIKQIRKKVGLVfqfPESQL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 570 vltVEEnlSILASVKGIPANNIIQEVQKVLL---DLDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK13649 99 ---FEE--TVLKDVAFGPQNFGVSQEEAEALareKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29170396 643 AGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTiVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
473-695 |
2.16e-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: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 473 IGKEAIRISGIQKAYRKKNE-TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyghRVSE---- 547
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYISVDRgVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDewvd 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 548 -----IDEMFEARKMIGICPQSDMNFDVLTVEENLSILASVKgIPANniiQEVQKVLLDLDMQAIKDNQAK--------K 614
Cdd:TIGR03269 352 mtkpgPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLE-LPDE---LARMKAVITLKMVGFDEEKAEeildkypdE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 615 LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKA-NRVTVFSTHFMDEADILADRKAVISQGMLK 692
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
...
gi 29170396 693 CVG 695
Cdd:TIGR03269 508 KIG 510
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
477-647 |
2.44e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDE--M 551
Cdd:PRK11124 2 SIQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 552 FEARKMIGICPQSDMNFDVLTVEENLsILASVK--GIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNL-IEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170
....*....|....*...
gi 29170396 630 LGNPKILLLDEPTAGMDP 647
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDP 174
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
496-696 |
3.48e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FASIYGHRVSEIDEMFEARKMIGIC---PQSDMnfd 569
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtVGDIVVSSTSKQKEIKPVRKKVGVVfqfPESQL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 570 vltVEEnlSILASVKGIPANNII--QEVQKVLLD-LDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK13643 98 ---FEE--TVLKDVAFGPQNFGIpkEKAEKIAAEkLEMVGLADEFWEKspfeLSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 643 AGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13643 173 AGLDPKARIEMMQLFEsIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
500-696 |
5.96e-19 |
|
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: 89.40 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE----IDEMFEARKmIGICPQSDMNFDVLTVEE 575
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRR-IGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NLSILASVKGIPANNIIQEvqKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD-PCSRHIVW 654
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFE--RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29170396 655 NLLKYRKANRV-TVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:TIGR02142 173 YLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
501-696 |
8.64e-19 |
|
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: 89.00 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGH----RVSEIDEMFEARKmIGICPQSDMNFDVLTVEEN 576
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRR-IGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 LsiLASVKGIPANNiiqevQKVLLD-----LDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:COG4148 98 L--LYGRKRAPRAE-----RRISFDevvelLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29170396 652 ivwNLLKY-----RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4148 171 ---EILPYlerlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
474-642 |
1.11e-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: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 474 GKEAIRISGIQKAYRKKneTVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSI-YGHRVSeidemf 552
Cdd:COG0488 312 GKKVLELEGLSKSYGDK--TL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG--TVkLGETVK------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 553 earkmIGICPQSDMNFDvltveENLSILASVKGIPANNIIQEVQKVLLDL----DMQaikDNQAKKLSGGQKRKLSLGIA 628
Cdd:COG0488 380 -----IGYFDQHQEELD-----PDKTVLDELRDGAPGGTEQEVRGYLGRFlfsgDDA---FKPVGVLSGGEKARLALAKL 446
|
170
....*....|....
gi 29170396 629 VLGNPKILLLDEPT 642
Cdd:COG0488 447 LLSPPNVLLLDEPT 460
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-691 |
1.49e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.24 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF----------ASIYGHRVS 546
Cdd:COG1117 11 KIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeilldgEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 547 EIdemfEARKMIGicpqsdMNFDV-----LTVEENLSILASVKGIPANNIIQE-VQKVLLdldmQA-----IKDN---QA 612
Cdd:COG1117 87 VV----ELRRRVG------MVFQKpnpfpKSIYDNVAYGLRLHGIKSKSELDEiVEESLR----KAalwdeVKDRlkkSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 613 KKLSGGQKRKLSL--GIAVlgNPKILLLDEPTAGMDPCSRHIVWNL---LKyrkaNRVT-VFSTHFMDEADILADRKAVI 686
Cdd:COG1117 153 LGLSGGQQQRLCIarALAV--EPEVLLMDEPTSALDPISTAKIEELileLK----KDYTiVIVTHNMQQAARVSDYTAFF 226
|
....*
gi 29170396 687 SQGML 691
Cdd:COG1117 227 YLGEL 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
478-695 |
1.88e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.16 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM 557
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 638 LDEPTAGMDPCSR---HIVWNLLkYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK11000 157 LDEPLSNLDAALRvqmRIEISRL-HKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
496-696 |
1.92e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR-KMIGICPQSDMNFDVLT 572
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 573 VEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29170396 653 VWN-LLKYR-KANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10070 203 MQDeLVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
496-689 |
5.31e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 82.87 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMFEA--------RKMIGICPQsd 565
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAgiayvpedRKREGLVLD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 566 mnfdvLTVEENLSILASvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03215 93 -----LSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29170396 646 DPCSRHIVWNLL-KYRKANR-VTVFSTHfMDEADILADRKAVISQG 689
Cdd:cd03215 136 DVGAKAEIYRLIrELADAGKaVLLISSE-LDELLGLCDRILVMYEG 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
486-691 |
6.07e-18 |
|
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: 83.67 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 486 AYRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmIGICPQSD 565
Cdd:cd03248 20 AYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 566 MNFdVLTVEENLS----------ILASVKGIPANNIIQEVQKvlldlDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:cd03248 98 VLF-ARSLQDNIAyglqscsfecVKEAAQKAHAHSFISELAS-----GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGML 691
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
507-646 |
6.96e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 6.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 507 GQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEAR-----KMIGICPQSDMNFDVLTVEENLSILA 581
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE--EARaklraKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 582 SVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK10584 114 LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
476-696 |
8.19e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 8.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 476 EAIRISGIQKAYR------------------KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF 537
Cdd:COG1134 3 SMIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 538 ASIYGhRVSEIDEMfearkMIGICPQsdmnfdvLTVEENLSILASVKGIPAnniiQEVQKVlldldMQAIK--------- 608
Cdd:COG1134 83 VEVNG-RVSALLEL-----GAGFHPE-------LTGRENIYLNGRLLGLSR----KEIDEK-----FDEIVefaelgdfi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 609 DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-----CSRHIvwnlLKYRKANRVTVFSTHFMDEADILADRK 683
Cdd:COG1134 141 DQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkkCLARI----RELRESGRTVIFVSHSMGAVRRLCDRA 216
|
250
....*....|...
gi 29170396 684 AVISQGMLKCVGS 696
Cdd:COG1134 217 IWLEKGRLVMDGD 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
477-682 |
1.03e-17 |
|
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: 83.25 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEAR- 555
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE--DARa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 ----KMIGICPQSDMNFDVLTVEENlsilasvkgipanniiqevqkVLLDLDMQAIKDNQA------------------- 612
Cdd:COG4181 86 rlraRHVGFVFQSFQLLPTLTALEN---------------------VMLPLELAGRRDARArarallervglghrldhyp 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 613 KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLL-KYRKANRVT-VFSTHfmDEAdiLADR 682
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTlVLVTH--DPA--LAAR 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
477-677 |
2.03e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.49 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidEMFEARK 556
Cdd:NF033858 1 VARLEGVSHRYGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGG------DMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQ-SDM------N-FDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:NF033858 71 RRAVCPRiAYMpqglgkNlYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29170396 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANR----VTVfSTHFMDEAD 677
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmsVLV-ATAYMEEAE 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
476-696 |
2.30e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.90 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 476 EAIRISGIqkAYRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMfe 553
Cdd:PRK13548 1 AMLEARNL--SVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 554 ARkMIGICPQ-SDMNFDvLTVEE----NLSILASVKGiPANNIIQEvqkVLLDLDMQAIKDNQAKKLSGGQKRKLSLgiA 628
Cdd:PRK13548 75 AR-RRAVLPQhSSLSFP-FTVEEvvamGRAPHGLSRA-EDDALVAA---ALAQVDLAHLAGRDYPQLSGGEQQRVQL--A 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 629 -VL-------GNPKILLLDEPTAGMDPCSRHIVWNLLKYR-KANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13548 147 rVLaqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVlHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
493-701 |
2.55e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 493 TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQ-SDMNFDVL 571
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKFVGLVFQnPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 572 TVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:PRK13652 95 TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 652 ivwNLLKYRKANRVT-----VFSTHFMDEADILADRKAVISQGMLKCVGS--SIFLK 701
Cdd:PRK13652 175 ---ELIDFLNDLPETygmtvIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQ 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-697 |
3.48e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.27 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC-----PPSDGFASIYGHRVSEIDeMFEARKMIgicpqsDMNF 568
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMD-VIELRRRV------QMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQ------------AKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK14247 89 QIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQlwdevkdrldapAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
497-695 |
5.43e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 85.48 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID-EMFEarKMIGICPQSDMNFDVlTVEE 575
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDrETFG--KHIGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NLS----ILASVKGIPANNIIQeVQKVLLDLDM---QAIKDNQAKkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:TIGR01842 411 NIArfgeNADPEKIIEAAKLAG-VHELILRLPDgydTVIGPGGAT-LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29170396 649 SRHIVWNLLKYRKANRVTV-FSTHfMDEADILADRKAVISQGMLKCVG 695
Cdd:TIGR01842 489 GEQALANAIKALKARGITVvVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
495-647 |
5.64e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.10 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQSDMNfDVLTVE 574
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLK-PELSAL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 575 ENLSILASVKGIPANNIIQEVQKVLLDldmqAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:TIGR01189 92 ENLHFWAAIHGGAQRTIEDALAAVGLT----GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
496-684 |
8.15e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.37 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCPP--SDGFASIYGHRV--SEIDEMfEARKMIGICPQSDMNF 568
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLyaPDVDPV-EVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVlTVEENLSILASVKGIPANniIQEV------QKVLLDLDMQAIKDNqAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGD--MDELverslrQAALWDEVKDKLKQS-GLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29170396 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKA 684
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
496-682 |
1.53e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV-------SEIDEMFearkmigicPqsdmnf 568
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqrSEVPDSL---------P------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 dvLTVEENLSI----LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:NF040873 72 --LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 29170396 645 MDPCSRHIVWNLLKYRKANRVTVF-STHFMDEAdILADR 682
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVvVTHDLELV-RRADP 187
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-703 |
2.00e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 474 GKEAIRISGIQKAYRKKNETVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP------PSDGFASIYGHRVSE 547
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 548 IDEMfEARKMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEV-----QKVLLDLDMQAIKDNQAKKLSGGQKRK 622
Cdd:PRK14246 83 IDAI-KLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIveeclRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 623 LSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSS--IFL 700
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSneIFT 241
|
...
gi 29170396 701 KSK 703
Cdd:PRK14246 242 SPK 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
483-646 |
2.22e-16 |
|
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: 78.46 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 483 IQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLcppSDGFASIYGHrVS----EIDEMFE-ARKM 557
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGD-IHyngiPYKEFAEkYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQSDMNFDVLTVEENLSILASVKGipaNNIIqevqkvlldldmqaikdnqaKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG---NEFV--------------------RGISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 29170396 638 LDEPTAGMD 646
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
501-695 |
2.47e-16 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 78.75 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQSDMNFDVLTVEENLSiL 580
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP---YQRPVSMLFQENNLFAHLTVRQNIG-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 581 ASVKGIPANNIIQE-VQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY 659
Cdd:TIGR01277 94 GLHPGLKLNAEQQEkVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 29170396 660 --RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:TIGR01277 174 lcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
214-416 |
2.53e-16 |
|
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: 81.28 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 214 DTFPRGVILIYLVIAFSPFGYFLAIHIVAEKEKRLKEFLKIMGLHDTAFWLSWVLLYTSLIFLMSLLMAVIATASSlFPQ 293
Cdd:pfam12698 157 SGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIG-IPF 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 294 SSSIVIFLLFFLYGLSSVFFALMLTPLFKKSKHVGVVEFFVTVVFGFVGLLIVLVESFPRSLVWLFSPLCQCAFLIGIAQ 373
Cdd:pfam12698 236 GNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29170396 374 VMhledfnegalfssLTEGPYPLIITLTMLALDSVFYALLAVY 416
Cdd:pfam12698 316 LI-------------YGDSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
494-691 |
2.87e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 83.23 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQSDMNFDVlTV 573
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY-TLASLRRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EENLSIlasvkGIPANNIIQEVQKVLLDLDMQAIKDN-----------QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:TIGR02203 423 ANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29170396 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGML 691
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
478-696 |
4.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.67 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNE-TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfASIYGH-----RVSEIDEM 551
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG-QTIVGDyaipaNLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 552 FEARKMIGIC---PQSDMNFDvlTVEENLSILASVKGIPANNIIQEVQKVLldlDMQAIKDNQAKK----LSGGQKRKLS 624
Cdd:PRK13645 86 KRLRKEIGLVfqfPEYQLFQE--TIEKDIAFGPVNLGENKQEAYKKVPELL---KLVQLPEDYVKRspfeLSGGQKRRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 625 LGIAVLGNPKILLLDEPTAGMDPCSRHIVWNL---LKYRKANRVtVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRI-IMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
485-692 |
5.90e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 485 KAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEAR---KMIGIC 561
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 562 PQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29170396 642 TAGMDPCSRHIVWNLLKYRKANRVTVF--STHFMDEADILaDRKAVISQGMLK 692
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
487-689 |
6.01e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 487 YRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE-MFEARKMIGICPQ-- 563
Cdd:PRK13638 9 FRYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgLLALRQQVATVFQdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 564 ------SDMNFDVLTVEENLsilasvkGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:PRK13638 87 eqqifyTDIDSDIAFSLRNL-------GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLK--YRKANRVtVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRriVAQGNHV-IISSHDIDLIYEISDAVYVLRQG 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
461-689 |
6.66e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.79 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 461 LNEIVE-PVSSEFIGKE-------AIRISGIQKAYrkKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP 532
Cdd:PRK11160 314 INEITEqKPEVTFPTTStaaadqvSLTLNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 533 PSDGFASIYGHRVSEIDEMfEARKMIGICPQSdmnFDVL--TVEENLSILASvkgiPANN--IIQEVQKVLLDLDMQAIK 608
Cdd:PRK11160 392 PQQGEILLNGQPIADYSEA-ALRQAISVVSQR---VHLFsaTLRDNLLLAAP----NASDeaLIEVLQQVGLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 609 DNQA------KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-CSRHIVWNLLKYRKaNRVTVFSTH---FMDEAD- 677
Cdd:PRK11160 464 GLNAwlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAeTERQILELLAEHAQ-NKTVLMITHrltGLEQFDr 542
|
250
....*....|...
gi 29170396 678 -ILADRKAVISQG 689
Cdd:PRK11160 543 iCVMDNGQIIEQG 555
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
490-658 |
7.08e-16 |
|
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: 76.90 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcppsdgfASIYGHRVSEI-------DEMFeaRKMIGICP 562
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--------RKTAGVITGEIlingrplDKNF--QRSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 563 QSDMNFDVLTVEENLSILASVKGipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:cd03232 86 QQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170
....*....|....*.
gi 29170396 643 AGMDPCSRHIVWNLLK 658
Cdd:cd03232 137 SGLDSQAAYNIVRFLK 152
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
475-671 |
7.66e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 475 KEAIRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfea 554
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIGICPQS---DMNFDVLtVEEnlSILASVKG------IPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL 625
Cdd:PRK15056 77 KNLVAYVPQSeevDWSFPVL-VED--VVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29170396 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTH 671
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLReLRDEGKTMLVSTH 200
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
458-710 |
1.46e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 81.32 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 458 NISLNEiVEPVSSEFIGK----EAIRISG---IQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGL 530
Cdd:TIGR01193 445 NNRLNE-VYLVDSEFINKkkrtELNNLNGdivINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 531 CPPSDGFASIYGHRVSEIDEMfEARKMIGICPQSDMNFDVlTVEENLsILASVKGIPANNIIQEVQKVLLDLDMQAIK-- 608
Cdd:TIGR01193 524 FQARSGEILLNGFSLKDIDRH-TLRQFINYLPQEPYIFSG-SILENL-LLGAKENVSQDEIWAACEIAEIKDDIENMPlg 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 609 -----DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH-IVWNLLKYRkaNRVTVFSTHFMDEADiLADR 682
Cdd:TIGR01193 601 yqtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKkIVNNLLNLQ--DKTIIFVAHRLSVAK-QSDK 677
|
250 260
....*....|....*....|....*...
gi 29170396 683 KAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:TIGR01193 678 IIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
496-689 |
1.48e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfeARKmiGICPQSDMNFDVLTVEE 575
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AER--GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN 655
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 29170396 656 LL--KYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11248 170 LLlkLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
478-696 |
1.57e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNetveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeideMFEARKM 557
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS----MLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 ---IGICPQsdmnfdVLTVEENLSI--LASVKGIPANNII--------QEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLS 624
Cdd:PRK11231 75 arrLALLPQ------HHLTPEGITVreLVAYGRSPWLSLWgrlsaednARVNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 625 LGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVlHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
479-689 |
1.65e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 479 RISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG--HRVSEIDEMFEARk 556
Cdd:PRK11288 6 SFDGIGKTF----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAALAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 mIGICPQSDMNFDVLTVEENLSI--LASVKG-IPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:PRK11288 81 -VAIIYQELHLVPEMTVAENLYLgqLPHKGGiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 634 KILLLDEPTAGMDpcSRHIVwNLLK----YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11288 160 RVIAFDEPTSSLS--AREIE-QLFRvireLRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
495-695 |
2.00e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCPPS--DGFASIYGHRVSEID-EMFEARKMIGICPQSDMNF 568
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArvEGEVRLFGRNIYSPDvDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVLTVEENLSILASVKGI--PANNIIQEVQKVLLDLDM-QAIKD---NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDrlnDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29170396 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
476-682 |
4.46e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 75.55 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 476 EAIRISGIQKAYRKKNE---TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSI-YGHRVSEID-- 549
Cdd:COG4778 3 TLLEVENLSKTFTLHLQggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG--SIlVRHDGGWVDla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 550 -----EMFEARK-MIGICPQsdmnFdvLTVeenlsilasVKGIPANNIiqeVQKVLLDLDM-QAIKDNQAKKL------- 615
Cdd:COG4778 81 qasprEILALRRrTIGYVSQ----F--LRV---------IPRVSALDV---VAEPLLERGVdREEARARARELlarlnlp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 616 -----------SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSThFMDEA--DILADR 682
Cdd:COG4778 143 erlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADR 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
500-689 |
5.33e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 75.18 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 500 LSFD--IYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKMIGICPQSDMNFDVLTVEENL 577
Cdd:COG3840 16 LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG---QDLTALPPAERPVSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 578 SIlasvkGI-PANNI----IQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:COG3840 93 GL-----GLrPGLKLtaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 29170396 653 VWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:COG3840 168 MLDLVDelCRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
500-646 |
6.15e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.45 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQSDMNfDVLTVEENLSI 579
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIK-TTLSVLENLRF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 580 LAsvkgipANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03231 97 WH------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
477-696 |
7.18e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.19 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKnetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARK 556
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQsdmNFDV---LTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:PRK11650 77 DIAMVFQ---NYALyphMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 634 KILLLDEPTAGMDPcsrhivwnllKYRKANRV------------TVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK11650 154 AVFLFDEPLSNLDA----------KLRVQMRLeiqrlhrrlkttSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
477-689 |
7.28e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIyghRVSEID------- 549
Cdd:PRK11264 3 AIEVKNLVKKF--HGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAG--TI---RVGDITidtarsl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 550 -----EMFEARKMIGICPQSDMNFDVLTVEENlsILAS---VKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKR 621
Cdd:PRK11264 74 sqqkgLIRQLRQHVGFVFQNFNLFPHRTVLEN--IIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 622 KLSLGIAVLGNPKILLLDEPTAGMDPcsrHIVWNLLKYRKA----NRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
489-677 |
1.29e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 73.66 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQSD--M 566
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQEPwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 567 NfdvLTVEENlsILAsvkGIPANNiiQEVQKVL----LDLDMQAIKD-----------NqakkLSGGQKRKLSLGIAVLG 631
Cdd:cd03250 79 N---GTIREN--ILF---GKPFDE--ERYEKVIkacaLEPDLEILPDgdlteigekgiN----LSGGQKQRISLARAVYS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29170396 632 NPKILLLDEPTAGMDP-CSRHIVWN-LLKYRKANRVTVFSTH---FMDEAD 677
Cdd:cd03250 145 DADIYLLDDPLSAVDAhVGRHIFENcILGLLLNNKTRILVTHqlqLLPHAD 195
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
499-646 |
1.67e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.91 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeiDEMFEARKmIGICPQSDMNFDVLTVEENLS 578
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRD-ICMVFQSYALFPHMSLGENVG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 579 ILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK11432 101 YGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
478-691 |
2.48e-14 |
|
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: 74.07 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYR-----KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--E 550
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 551 MFEARKMIGICPQSDMNfdvlTVEENLSILASVkGIPANNII-----QEVQKVLLDLDMQAIKDNQAKK----LSGGQKR 621
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSPS----AVNPRMTVRQII-GEPLRHLTsldesEQKARIAELLDMVGLRSEDADKlprqLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHFMDEADILADRKAVISQGML 691
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
498-643 |
2.81e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 498 RNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQSDMNfDVLTVEENL 577
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQPGIK-TELTALENL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 578 SILASVKGIPANNIIQEV-QKVLLdldmQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP-TA 643
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEAlAQVGL----AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPfTA 159
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
480-642 |
3.23e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 480 ISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghRVSeidemFEARKMIG 559
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVS-----IPKGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 560 ICPQSDMNFDVLTVEENlsILASVKGIPAnnIIQEVQKVL-----LDLDMQAIKDNQAK--------------------- 613
Cdd:COG0488 65 YLPQEPPLDDDLTVLDT--VLDGDAELRA--LEAELEELEaklaePDEDLERLAELQEEfealggweaearaeeilsglg 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29170396 614 -----------KLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG0488 141 fpeedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
489-697 |
3.37e-14 |
|
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: 76.38 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGL--CPPSDGfASIY------------------------G 542
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSG-RIIYhvalcekcgyverpskvgepcpvcG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 543 HRVSEIDEMF---------EARKMIGICPQSDMN-FDVLTVEENlsILASVK--GIPANNIIQEVQKVLLDLDMQAIKDN 610
Cdd:TIGR03269 87 GTLEPEEVDFwnlsdklrrRIRKRIAIMLQRTFAlYGDDTVLDN--VLEALEeiGYEGKEAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 611 QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVT-VFSTHFMDEADILADRKAVISQ 688
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISmVLTSHWPEVIEDLSDKAIWLEN 244
|
....*....
gi 29170396 689 GMLKCVGSS 697
Cdd:TIGR03269 245 GEIKEEGTP 253
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
474-705 |
3.43e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.16 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 474 GKEAIRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTG--KSTLMNILCGlcpPSDG-----FASIYGHRVS 546
Cdd:NF000106 10 ARNAVEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGrrpwrF*TWCANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 547 eidemfeARKMIGIC-PQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL 625
Cdd:NF000106 83 -------LRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGMLKCVGSSIFLKSKW 704
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVlLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKV 235
|
.
gi 29170396 705 G 705
Cdd:NF000106 236 G 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
478-697 |
4.30e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC---PPSDGFASIYGHRVSE----IDE 550
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 551 MFEARKMIGICPQSDMNFDVLTVEENLsILASVKGIP---------ANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKR 621
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
489-689 |
5.54e-14 |
|
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: 75.63 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGH----RVSEIDEMfeARKMIGICPQS 564
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSgsplKASNIRDT--ERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 565 DMNFDVLTVEENLSI---LASVKGIPANN-IIQEVQKVLLDLDMQAIKDNQA-KKLSGGQKRKLSLGIAVLGNPKILLLD 639
Cdd:TIGR02633 87 LTLVPELSVAENIFLgneITLPGGRMAYNaMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29170396 640 EPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVKAVCDTICVIRDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
473-689 |
7.93e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 473 IGKEAIRISGIQKAyrkknetveALRN-LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeIDEM 551
Cdd:PRK11288 253 LGEVRLRLDGLKGP---------GLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 552 FEA-RKMIGICPQsDMNFD----VLTVEENLSILASVKGIPANNII---QEVQKVLLDLDMQAIK----DNQAKKLSGG- 618
Cdd:PRK11288 323 RDAiRAGIMLCPE-DRKAEgiipVHSVADNINISARRHHLRAGCLInnrWEAENADRFIRSLNIKtpsrEQLIMNLSGGn 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 619 -QK----RKLSLGIavlgnpKILLLDEPTAGMDPCSRHIVWNLLkYRKANR---VTVFSTHFMdEADILADRKAVISQG 689
Cdd:PRK11288 402 qQKailgRWLSEDM------KVILLDEPTRGIDVGAKHEIYNVI-YELAAQgvaVLFVSSDLP-EVLGVADRIVVMREG 472
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
490-658 |
8.03e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.92 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHrvsEIDEMFEARkmIGICPQSDM 566
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGR---PLDSSFQRS--IGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 567 NFDVLTVEENLSILASVKgIPANNIIQE----VQKVLLDLDMQAIKDN----QAKKLSGGQKRKLSLGIAVLGNPKILL- 637
Cdd:TIGR00956 847 HLPTSTVRESLRFSAYLR-QPKSVSKSEkmeyVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180
....*....|....*....|.
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLK 658
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMR 946
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-684 |
9.12e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF----------ASIYGHRVS 546
Cdd:PRK14258 7 AIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrvegrveffnQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 547 eIDEMFEARKMIGICPqsdmNFDVLTVEENLSILASVKGI-PANNIIQEVQKVLLDLDM-QAIKDN---QAKKLSGGQKR 621
Cdd:PRK14258 83 -LNRLRRQVSMVHPKP----NLFPMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLwDEIKHKihkSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYR--KANRVTVFSTHFMDEADILADRKA 684
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
478-676 |
1.35e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETV-EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG-----FASIYGHRVSEIDEM 551
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 552 F------------------EARKMIGICPQ-SDMNFDVLTVEENLSILASVKGIPANNIIQEVQKV--LLDLDMQAIKDN 610
Cdd:PRK13651 83 VleklviqktrfkkikkikEIRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYieLVGLDESYLQRS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 611 QAKkLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEA 676
Cdd:PRK13651 163 PFE-LSGGQKRRVALaGILAM-EPDFLVFDEPTAGLDPQGVKEILEIFdNLNKQGKTIILVTHDLDNV 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-691 |
2.58e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 509 ITALLGHSGTGKSTLMNILCGLCPPSDGF-----ASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTVEENLSILASV 583
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 584 KGIPANNIIQEVQKVLLDLDM-QAIKDNQAK---KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKy 659
Cdd:PRK14271 129 KLVPRKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR- 207
|
170 180 190
....*....|....*....|....*....|...
gi 29170396 660 RKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK14271 208 SLADRLTViIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
489-689 |
2.77e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.42 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIY---------GHRVSEidemfeaRKMIG 559
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfegeelqasNIRDTE-------RAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 560 ICPQSDMNFDVLTVEENLsILAS--VKG--IPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13549 86 IIHQELALVKELSVLENI-FLGNeiTPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIAcIYISHKLNEVKAISDTICVIRDG 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
480-689 |
3.05e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 480 ISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE----MF-EA 554
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdtrlMFqDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RkmigICPQSdmnfdvlTVEENLSIlaSVKGIPANNIIQEVQKVLLDldmqaikdNQAKK----LSGGQKRKLSLGIAVL 630
Cdd:PRK11247 91 R----LLPWK-------KVIDNVGL--GLKGQWRDAALQALAAVGLA--------DRANEwpaaLSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 631 GNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIEslWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
497-695 |
3.13e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 73.24 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQsdmnfDV-L---T 572
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE-ELGRHIGYLPQ-----DVeLfdgT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 573 VEENLSILASVkgiPANNIIQEVQKV-----LLDL----DMQaIKDNQAKkLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:COG4618 422 IAENIARFGDA---DPEKVVAAAKLAgvhemILRLpdgyDTR-IGEGGAR-LSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 644 GMDPCSRHIVWNLLKYRKANRVTVF-STHfmdEADIL--ADRKAVISQGMLKCVG 695
Cdd:COG4618 497 NLDDEGEAALAAAIRALKARGATVVvITH---RPSLLaaVDKLLVLRDGRVQAFG 548
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
499-689 |
3.97e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.56 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEARKMIGICPQSDMNFDVLTVEEN 576
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 LSI-LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN 655
Cdd:PRK11831 105 VAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29170396 656 LL-KYRKANRVT-VFSTH-------FMDEADILADRKaVISQG 689
Cdd:PRK11831 185 LIsELNSALGVTcVVVSHdvpevlsIADHAYIVADKK-IVAHG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
460-671 |
5.70e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 460 SLNEIV--EP-VSSEFIGKEAIRISGIQ-KAYRKKNET---VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP 532
Cdd:PTZ00265 357 SLYEIInrKPlVENNDDGKKLKDIKKIQfKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 533 PSDGFASIY-GHRVSEIDEMFeARKMIGICPQSDMNF---------------------------DVLTVEENLSILASVK 584
Cdd:PTZ00265 437 PTEGDIIINdSHNLKDINLKW-WRSKIGVVSQDPLLFsnsiknnikyslyslkdlealsnyyneDGNDSQENKNKRNSCR 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 585 GIPA---NNIIQEV------------------------QKVLLDLDMQAIKD-------NQAKKLSGGQKRKLSLGIAVL 630
Cdd:PTZ00265 516 AKCAgdlNDMSNTTdsneliemrknyqtikdsevvdvsKKVLIHDFVSALPDkyetlvgSNASKLSGGQKQRISIARAII 595
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 29170396 631 GNPKILLLDEPTAGMDPCSRHIVWNLLKYRKA--NRVTVFSTH 671
Cdd:PTZ00265 596 RNPKILILDEATSSLDNKSEYLVQKTINNLKGneNRITIIIAH 638
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
497-646 |
6.35e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEmfEARKMIGICPQSdMNFDV---LTV 573
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKR--NGKLRIGYVPQK-LYLDTtlpLTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 574 EENLSILASVKG---IPANNIIQEVQkvLLDLDMQaikdnqakKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK09544 87 NRFLRLRPGTKKediLPALKRVQAGH--LIDAPMQ--------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
497-675 |
8.31e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID-EMFeaRKMIGICPQSDMNFDVlTVEE 575
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIY--RQQVSYCAQTPTLFGD-TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NLSILASVKgipanNIIQEVQKVLLDLDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:PRK10247 100 NLIFPWQIR-----NQQPDPAIFLDDLERFALPDTILTKniaeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|....*.
gi 29170396 652 IVWNLL-KYRKANRVTV-FSTHFMDE 675
Cdd:PRK10247 175 NVNEIIhRYVREQNIAVlWVTHDKDE 200
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
509-705 |
8.94e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 509 ITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMF----EARKmIGICPQSDMNFDVLTVEENLSIlasvk 584
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppEKRR-IGYVFQDARLFPHYKVRGNLRY----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 585 GIPANNIIQEVQKVLLdLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD-PCSRHivwnLLKY--RK 661
Cdd:PRK11144 100 GMAKSMVAQFDKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE----LLPYleRL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29170396 662 ANRVT---VFSTHFMDEADILADRKAVISQGMLKCVGSsifLKSKWG 705
Cdd:PRK11144 175 AREINipiLYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
490-657 |
9.10e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.43 E-value: 9.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARK--MIGICPQSDMN 567
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRirMIFQDPSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 568 --------FDV-LTVEENLSILASVKgipanNIIQEVQKVLLDLDMQAIKDNQakkLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PRK15112 102 prqrisqiLDFpLRLNTDLEPEQREK-----QIIETLRQVGLLPDHASYYPHM---LAPGQKQRLGLARALILRPKVIIA 173
|
170
....*....|....*....
gi 29170396 639 DEPTAGMDPCSRHIVWNLL 657
Cdd:PRK15112 174 DEALASLDMSMRSQLINLM 192
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
496-690 |
1.40e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.86 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTVEE 575
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NL----------SILASVKGIPA-----NNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDE 640
Cdd:PRK11300 100 NLlvaqhqqlktGLFSGLLKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29170396 641 PTAGMDPCSRHIVWNLL-KYRKANRVTVFST-HFMDEADILADRKAVISQGM 690
Cdd:PRK11300 180 PAAGLNPKETKELDELIaELRNEHNVTVLLIeHDMKLVMGISDRIYVVNQGT 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
494-691 |
1.82e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE--IDEMFEA--------RKMIGICPq 563
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsPRERRRLgvayipedRLGRGLVP- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 564 sDMnfdvlTVEENLsILASVKGIP-ANNIIqevqkvlldLDMQAIKDN-----------------QAKKLSGGQKRKLSL 625
Cdd:COG3845 350 -DM-----SVAENL-ILGRYRRPPfSRGGF---------LDRKAIRAFaeelieefdvrtpgpdtPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANR-VTVFSTHfMDEADILADRKAVISQGML 691
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDAGAaVLLISED-LDEILALSDRIAVMYEGRI 480
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
458-695 |
2.71e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.92 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 458 NISLNeiVEPVSSEF----IGKEAIRISGIQKayrKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP 533
Cdd:PRK13546 2 NVSVN--IKNVTKEYriyrTNKERMKDALIPK---HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 534 SDGFASIYGH-RVSEIDEMFEARkmigicpqsdmnfdvLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQA 612
Cdd:PRK13546 77 TVGKVDRNGEvSVIAISAGLSGQ---------------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 613 KKLSGGQKRKLSLGIAVLGNPKILLLDEP-TAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13546 142 KKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
....
gi 29170396 692 KCVG 695
Cdd:PRK13546 222 KDYG 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
467-689 |
2.96e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 467 PVSSEFIGKEAIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG---- 542
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 543 ---HRVSEIDEMFEAR---------KMIGICPQSDMNfDVLTVEENlsILASVK---GIPANNIIQEVQKvLLDL----D 603
Cdd:PRK10261 82 rrsRQVIELSEQSAAQmrhvrgadmAMIFQEPMTSLN-PVFTVGEQ--IAESIRlhqGASREEAMVEAKR-MLDQvripE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 604 MQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILAD 681
Cdd:PRK10261 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVlqKEMSMGVIFITHDMGVVAEIAD 237
|
....*...
gi 29170396 682 RKAVISQG 689
Cdd:PRK10261 238 RVLVMYQG 245
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
478-689 |
3.25e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.78 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNetveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFaSIYGHRVSeidemfearkm 557
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTVK----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 IGICPQsdmnfdvltveenlsilasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03221 65 IGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVfsTH---FMDEadiLADRKAVISQG 689
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPGTVILV--SHdryFLDQ---VATKIIELEDG 143
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-671 |
3.42e-12 |
|
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: 70.71 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpSDGFASIYGHRVSEIdEMFEARKMIGICPQSDMNFDVlTVEEN 576
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSV-TLQTWRKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 LSILASVKGipanniiQEVQKVLLDLDMQAIKDNQAKKL-----------SGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:TIGR01271 1312 LDPYEQWSD-------EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180
....*....|....*....|....*.
gi 29170396 646 DPCSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
501-689 |
3.55e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG--HRVSEIdemfeARKMIGICPQSDMNFDVLTVEENLS 578
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdHTTTPP-----SRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 579 IlasvkGIPANNIIQEVQKVLLdldmQAIKDNQA---------KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:PRK10771 94 L-----GLNPGLKLNAAQREKL----HAIARQMGiedllarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29170396 650 RHIVWNLLKYRKANR-VTVFS-THFMDEADILADRKAVISQG 689
Cdd:PRK10771 165 RQEMLTLVSQVCQERqLTLLMvSHSLEDAARIAPRSLVVADG 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
473-692 |
3.58e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 473 IGKEAIRISGIQkAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS-DGFASIYGHRV------ 545
Cdd:TIGR02633 253 IGDVILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdirnpa 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 546 ----SEIDEMFEARKMIGICPQsdmnfdvLTVEEN--LSILASVKGIPANNIIQEVQKVLLDLDMQAIK----DNQAKKL 615
Cdd:TIGR02633 332 qairAGIAMVPEDRKRHGIVPI-------LGVGKNitLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtaspFLPIGRL 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 616 SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHfMDEADILADRKAVISQGMLK 692
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
493-691 |
5.23e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 493 TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICP----QSDMNF 568
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrqSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVltveenlSILASVKGIPANNI---IQEVQ-KVLLDLDMQAI------KDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PRK15439 355 DA-------PLAWNVCALTHNRRgfwIKPAReNAVLERYRRALnikfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29170396 639 DEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
503-685 |
5.98e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.66 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 503 DIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemfeaRKMIGICPQSDMnfdvlTVEENLSILAS 582
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPQYIKADYEG-----TVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 583 VKGIPA---NNIIQEVQkvlldldMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK- 658
Cdd:cd03237 88 DFYTHPyfkTEIAKPLQ-------IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRr 160
|
170 180
....*....|....*....|....*...
gi 29170396 659 YRKANRVTVFST-HFMDEADILADRKAV 685
Cdd:cd03237 161 FAENNEKTAFVVeHDIIMIDYLADRLIV 188
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
497-692 |
6.90e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.19 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCpPSDGFASIYGHRVSEIdEMFEARKMIGICPQSDMNFDVlTVEEN 576
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSV-PLQKWRKAFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 LSILASVKGipanniiQEVQKVLLDLDMQAIKDNQAKK-----------LSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03289 97 LDPYGKWSD-------EEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29170396 646 DPCSRHIVWNLLKYRKANRVTVFSTHFMdEADILADRKAVISQGMLK 692
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
499-675 |
9.22e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpSDGFASIYGHRVSEIDEMfEARKMIGICPQSDMNFDVlTVEENLS 578
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPE-SWRKHLSWVGQNPQLPHG-TLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 579 iLASVKgipANNiiQEVQKVLLD------LDMQA------IKDnQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK11174 445 -LGNPD---ASD--EQLQQALENawvsefLPLLPqgldtpIGD-QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180
....*....|....*....|....*....
gi 29170396 647 PCSRHIVWNLLKYRKANRVTVFSTHFMDE 675
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
494-710 |
9.73e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmIGICPQSDMNFDVlTV 573
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EENLS----------ILASVKGIPANNIIQEVQKvlldlDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:TIGR00958 572 RENIAygltdtpdeeIMAAAKAANAHDFIMEFPN-----GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 644 GMDPCSRHIVWNLLKyrKANRVTVFSTHFMDEADiLADRKAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:TIGR00958 647 ALDAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
477-646 |
2.55e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKNETveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARK 556
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLV---LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV-LRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGICPQ-----SDMNFDVLTVEENLSilasvkgipANNIIQEVQKVLLDLDMQAIKD-------NQAKKLSGGQKRKLS 624
Cdd:PRK10790 416 GVAMVQQdpvvlADTFLANVTLGRDIS---------EEQVWQALETVQLAELARSLPDglytplgEQGNNLSVGQKQLLA 486
|
170 180
....*....|....*....|..
gi 29170396 625 LGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID 508
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
473-646 |
2.69e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 473 IGKEAIRISGIQKAyrkknetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS--EIDE 550
Cdd:COG1129 252 PGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 551 MFEA--------RKMIGICPQsdmnfdvLTVEENLSiLASVKGIPANNII------QEVQKVLLDLDmqaIK----DNQA 612
Cdd:COG1129 324 AIRAgiayvpedRKGEGLVLD-------LSIRENIT-LASLDRLSRGGLLdrrrerALAEEYIKRLR---IKtpspEQPV 392
|
170 180 190
....*....|....*....|....*....|....
gi 29170396 613 KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
496-646 |
2.77e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.29 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMNFDvLTVEE 575
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQDAGLFN-RSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NLSI----------LASVKGIPANNIIqevQKVLLDLDMQAikDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:PRK13657 428 NIRVgrpdatdeemRAAAERAQAHDFI---ERKPDGYDTVV--GERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
.
gi 29170396 646 D 646
Cdd:PRK13657 503 D 503
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
488-692 |
4.84e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE------MFEARKMIGIC 561
Cdd:PRK10619 12 HKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkVADKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 562 PQSDMNFDVLTVEENLSILASVKGIPANNI----IQEVQKVLLDLDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNP 633
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKypvhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 634 KILLLDEPTAGMDPcsrHIVWNLL----KYRKANRVTVFSTHFMDEADILADRKAVISQGMLK 692
Cdd:PRK10619 172 EVLLFDEPTSALDP---ELVGEVLrimqQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
490-646 |
7.67e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE----------IDEMFEARKMIG 559
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangIVYISEDRKRDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 560 IcpqsdmnfdVL--TVEENLSILA----SVKGIPANNIiQEVQKVLLDLDMQAIK----DNQAKKLSGGQKRKLSLGIAV 629
Cdd:PRK10762 341 L---------VLgmSVKENMSLTAlryfSRAGGSLKHA-DEQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGL 410
|
170
....*....|....*..
gi 29170396 630 LGNPKILLLDEPTAGMD 646
Cdd:PRK10762 411 MTRPKVLILDEPTRGVD 427
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
492-646 |
1.09e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 492 ETVEALRNLSFDIY-------------EGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmI 558
Cdd:PRK10575 9 DTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 559 GICPQSDMNFDVLTVEEnlsiLASVKGIPANNII--------QEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK10575 88 AYLPQQLPAAEGMTVRE----LVAIGRYPWHGALgrfgaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170
....*....|....*.
gi 29170396 631 GNPKILLLDEPTAGMD 646
Cdd:PRK10575 164 QDSRCLLLDEPTSALD 179
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
495-646 |
1.15e-10 |
|
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: 62.04 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMNFDVlTVE 574
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-LEDLRSSLTIIPQDPTLFSG-TIR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 575 ENLSILasvkgipanNIIQEVQkVLLDLDMQAIKDNqakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03369 100 SNLDPF---------DEYSDEE-IYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
498-691 |
1.15e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 498 RNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMN---FDVLTVE 574
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDngfFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLSILASVK--------GIPANNI---IQEVQKVLLDLDMQAIKDNqAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:PRK09700 360 QNMAISRSLKdggykgamGLFHEVDeqrTAENQRELLALKCHSVNQN-ITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29170396 644 GMDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK09700 439 GIDVGAKAEIYKVMrQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
497-653 |
1.29e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 65.64 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcPPSDGFasIYGH-RVSEIDEMFEARKMI-GICPQSDMNFDVLTVE 574
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGY--IEGDiRISGFPKKQETFARIsGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLsILASVKGIPANNIIQE----VQKVLLDLDMQAIKDN-----QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:PLN03140 972 ESL-IYSAFLRLPKEVSKEEkmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
....*...
gi 29170396 646 DPCSRHIV 653
Cdd:PLN03140 1051 DARAAAIV 1058
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
507-671 |
2.60e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 507 GQITALLGHSGTGKSTLMNILCGLCPPSD--GFASIYGHRVSEidemfEARKMIGICPQSDMNFDVLTVEENL------- 577
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTVRETLvfcsllr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 578 ---SILASVKGIPANNIIQEVQkvLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH-IV 653
Cdd:PLN03211 169 lpkSLTKQEKILVAESVISELG--LTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYrLV 246
|
170
....*....|....*...
gi 29170396 654 WNLLKYRKANRVTVFSTH 671
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMH 264
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
488-640 |
2.67e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.14 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvseidemfeARKMIGIcpQSDMN 567
Cdd:PRK13545 31 SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAI--SSGLN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29170396 568 fDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDE 640
Cdd:PRK13545 98 -GQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
495-696 |
3.94e-10 |
|
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: 60.23 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlCP---PSDGfaSIY--GHRVSEIdEMFE-ARKMIGICPQSDMNF 568
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEG--EILfkGEDITDL-PPEErARLGIFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVLTVEEnlsilasvkgipanniiqevqkVLLDLDMqaikdnqakKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:cd03217 90 PGVKNAD----------------------FLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29170396 649 SRHIVWNLL-KYRKANRVTVFSTHFMDEAD-ILADRKAVISQGMLKCVGS 696
Cdd:cd03217 139 ALRLVAEVInKLREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
493-689 |
4.46e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.88 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 493 TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMfEARKMIGICPQSDMNFDV 570
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDER-LIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 571 LTVEENLSI-LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:PRK09493 92 LTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29170396 650 RHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK09493 172 RHEVLKVMQDLAEEGMTmVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
455-712 |
4.56e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 455 INGNISLNEIVEP-VSSEFI---------GKEAIRISGIQKAYRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLM 524
Cdd:PLN03232 582 VNANVSLQRIEELlLSEERIlaqnpplqpGAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLI 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 525 NILCGLCPPSDgfasiyghrvseiDEMFEARKMIGICPQSDMNFDVlTVEENLSILASVKGIPANNIIqEVQKVLLDLDM 604
Cdd:PLN03232 661 SAMLGELSHAE-------------TSSVVIRGSVAYVPQVSWIFNA-TVRENILFGSDFESERYWRAI-DVTALQHDLDL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 605 QAIKD-----NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFST---HFMDe 675
Cdd:PLN03232 726 LPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTnqlHFLP- 804
|
250 260 270
....*....|....*....|....*....|....*..
gi 29170396 676 adiLADRKAVISQGMLKCVGSSIFLkSKWGIGYRLSM 712
Cdd:PLN03232 805 ---LMDRIILVSEGMIKEEGTFAEL-SKSGSLFKKLM 837
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
500-647 |
5.88e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM--IGICPQSDMNFDVLtveENL 577
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMayLGHLPGLKADLSTL---ENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 578 SILASVKGIPANniiQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13543 104 HFLCGLHGRRAK---QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
497-646 |
5.88e-10 |
|
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: 62.92 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEA-RKMIGICPQsdmnfDvlTVEE 575
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ--ASlRAAIGIVPQ-----D--TVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NLSIlasvkgipANNII--------QEVQKVLldlDMQAIKDNQAK--------------KLSGGQKRKLslGIA--VLG 631
Cdd:COG5265 445 NDTI--------AYNIAygrpdaseEEVEAAA---RAAQIHDFIESlpdgydtrvgerglKLSGGEKQRV--AIArtLLK 511
|
170
....*....|....*
gi 29170396 632 NPKILLLDEPTAGMD 646
Cdd:COG5265 512 NPPILIFDEATSALD 526
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
496-689 |
8.33e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASiYGHR---VSEIDEMFEA-RKMI-----GICPQSDM 566
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-YRMRdgqLRDLYALSEAeRRRLlrtewGFVHQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 567 NFDVLTVEENLSILASVKGIPAN---NIIQE----VQKVLLDLDMQaikDNQAKKLSGGQKRKLSLGIAVLGNPKILLLD 639
Cdd:PRK11701 100 DGLRMQVSAGGNIGERLMAVGARhygDIRATagdwLERVEIDAARI---DDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29170396 640 EPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRglVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
478-683 |
1.04e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.47 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYR-----KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmf 552
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 553 EARKmigicpqsDMNFDVLTV-EENLSILASVKGIPAnnIIQEVQKVLLDLDMQA-----------------IKDNQAKK 614
Cdd:PRK10419 82 AQRK--------AFRRDIQMVfQDSISAVNPRKTVRE--IIREPLRHLLSLDKAErlarasemlravdlddsVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 615 LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTH-------------FMDEADIL 679
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHdlrlverfcqrvmVMDNGQIV 231
|
....
gi 29170396 680 ADRK 683
Cdd:PRK10419 232 ETQP 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
467-653 |
1.08e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.56 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 467 PVSSEFIGKEAIRISGIQKAYRKKnetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGH 543
Cdd:PLN03140 154 PNAARNIAESALGMLGINLAKKTK---LTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGY 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 544 RVSEidemFEARKMIGICPQSDMNFDVLTVEENLSILASVKGIPA----------------------------------- 588
Cdd:PLN03140 231 RLNE----FVPRKTSAYISQNDVHVGVMTVKETLDFSARCQGVGTrydllselarrekdagifpeaevdlfmkatamegv 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 589 -NNIIQEVQKVLLDLDM---QAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP--------CSRHIV 653
Cdd:PLN03140 307 kSSLITDYTLKILGLDIckdTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSsttyqivkCLQQIV 383
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
467-691 |
1.58e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.53 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 467 PVSSEFIGKEAIRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS 546
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAYQDNGF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 547 EiDEMFEARKMIgicpqSDMNFDVLTVEEnlsiLASVKGIPANNiiQEVQKVLLDLDMQ---AIKDNQAK--KLSGGQKR 621
Cdd:PRK10522 389 A-EQPEDYRKLF-----SAVFTDFHLFDQ----LLGPEGKPANP--ALVEKWLERLKMAhklELEDGRISnlKLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
489-657 |
1.61e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--RKMIGIC---PQ 563
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllRQKIQIVfqnPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 564 SDMN-----FDVLtvEENLSILASVkgipanNIIQEVQKVLLDLDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK11308 103 GSLNprkkvGQIL--EEPLLINTSL------SAAERREKALAMMAKVGLRPEHYDRyphmFSGGQRQRIAIARALMLDPD 174
|
170 180
....*....|....*....|...
gi 29170396 635 ILLLDEPTAGMDPCSRHIVWNLL 657
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQVLNLM 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
497-646 |
1.91e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC---------------------PPSDGFASIYGHrVSE-IDEMFEA 554
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqdPPRNVEGTVYDF-VAEgIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKMIgicpqSDMNFDVLT--VEENLSILASVKGIPAN-------NIIQEVQKvLLDLDmqaiKDNQAKKLSGGQKRKLSL 625
Cdd:PRK11147 98 LKRY-----HDISHLVETdpSEKNLNELAKLQEQLDHhnlwqleNRINEVLA-QLGLD----PDAALSSLSGGWLRKAAL 167
|
170 180
....*....|....*....|.
gi 29170396 626 GIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
479-646 |
2.41e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 479 RISGIQKAYRKKNETVEalRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmI 558
Cdd:PRK10253 7 RLRGEQLTLGYGKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 559 GICPQSDMNFDVLTVEEnlsiLASVKGIPANNII--------QEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK10253 84 GLLAQNATTPGDITVQE----LVARGRYPHQPLFtrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170
....*....|....*.
gi 29170396 631 GNPKILLLDEPTAGMD 646
Cdd:PRK10253 160 QETAIMLLDEPTTWLD 175
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
478-642 |
4.66e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 60.08 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKS-TLMNILcGLCPPSDGFASiyghrvSEIdeMFEARK 556
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAAHPS------GSI--LFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 MIGiCPQSDMN----------FD--------VLTVEENLS-ILASVKGIPAnniiQEVQKVLLD-LDMQAIKDNQAK--- 613
Cdd:COG4172 78 LLG-LSERELRrirgnriamiFQepmtslnpLHTIGKQIAeVLRLHRGLSG----AAARARALElLERVGIPDPERRlda 152
|
170 180 190
....*....|....*....|....*....|..
gi 29170396 614 ---KLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
486-671 |
8.43e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.26 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 486 AYRKKNETveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQSD 565
Cdd:PRK11176 350 TYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY-TLASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 566 MNFDVlTVEENL-----------SILASVKGIPANNIIQEVQKVlLDldmQAIKDNQAkKLSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK11176 427 HLFND-TIANNIayarteqysreQIEEAARMAYAMDFINKMDNG-LD---TVIGENGV-LLSGGQRQRIAIARALLRDSP 500
|
170 180 190
....*....|....*....|....*....|....*..
gi 29170396 635 ILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
479-671 |
1.53e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 479 RISGIQKAYRKKNETVE--ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCG--LCPPSDGFASIyghrvseidemfea 554
Cdd:COG2401 26 RVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV-------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 rkmigicpqsdmnfDVLTVEENLSILASvkgIPANNIIQEVQKVlldLDMQAIKDNQA-----KKLSGGQKRKLSLGIAV 629
Cdd:COG2401 92 --------------PDNQFGREASLIDA---IGRKGDFKDAVEL---LNAVGLSDAVLwlrrfKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29170396 630 LGNPKILLLDEPTAGMDP-CSRHIVWNLLKY-RKANRVTVFSTH 671
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRqTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
480-646 |
1.64e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.41 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 480 ISGIQKAYRKKNETveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvseidemfEARKMIG 559
Cdd:TIGR03719 7 MNRVSKVVPPKKEI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------------EARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 560 IC-------PQSDMNFDVL-TVEENLS----ILASVKGIPAN-------------------NIIQEVQkvLLDLD----- 603
Cdd:TIGR03719 68 IKvgylpqePQLDPTKTVReNVEEGVAeikdALDRFNEISAKyaepdadfdklaaeqaelqEIIDAAD--AWDLDsqlei 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29170396 604 -MQAIK----DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR03719 146 aMDALRcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
476-647 |
1.80e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 56.35 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 476 EAIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvsEIDEMFEAR 555
Cdd:COG4598 7 PALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG----EEIRLKPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 556 KmiGICPQSDM---------------NFDV---LTVEENLsILA--SVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKL 615
Cdd:COG4598 79 D--GELVPADRrqlqrirtrlgmvfqSFNLwshMTVLENV-IEApvHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190
....*....|....*....|....*....|..
gi 29170396 616 SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
486-694 |
2.54e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 486 AYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKS-TLMNILCGL-CPP---SDGFASIYGHRVSEIDEMfEARK---- 556
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLLHASEQ-TLRGvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 ---MIGICPQSDMNfDVLTVEENLS-ILASVKGI---PANNiiqevqKVLLDLDMQAIKdnQAKK--------LSGGQKR 621
Cdd:PRK15134 93 kiaMIFQEPMVSLN-PLHTLEKQLYeVLSLHRGMrreAARG------EILNCLDRVGIR--QAAKrltdyphqLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGmlKCV 694
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLADRVAVMQNG--RCV 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
473-692 |
2.79e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 473 IGKEAIRISGIQkAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP-PSDGFASIYGHRVS----- 546
Cdd:PRK13549 255 IGEVILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnpq 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 547 -----EIDEMFEARKMIGICPqsdmnfdVLTVEENLSiLASVKGIPANNIIQEVQKvlLDLDMQAIKDNQAK-------- 613
Cdd:PRK13549 334 qaiaqGIAMVPEDRKRDGIVP-------VMGVGKNIT-LAALDRFTGGSRIDDAAE--LKTILESIQRLKVKtaspelai 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 614 -KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLkYRKANR---VTVFSTHfMDEADILADRKAVISQG 689
Cdd:PRK13549 404 aRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI-NQLVQQgvaIIVISSE-LPEVLGLSDRVLVMHEG 481
|
...
gi 29170396 690 MLK 692
Cdd:PRK13549 482 KLK 484
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
494-695 |
4.91e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.39 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQS---DMNFDV 570
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVASVPQDtslSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 571 LTVEE-----NLSILASVKgiPANNiiQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:PRK09536 95 RQVVEmgrtpHRSRFDTWT--ETDR--AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29170396 646 DpcSRHIVWNLLKYRK---ANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK09536 171 D--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
488-646 |
5.77e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcpPSDGFA-------SIYGHRVSEIDEMFeaRKMIGI 560
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHigvegviTYDGITPEEIKKHY--RGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 561 CPQSDMNFDVLTVEENLSILASVKGiPANNII----QEVQKVLLDLDMQA----------IKDNQAKKLSGGQKRKLSLG 626
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARCKT-PQNRPDgvsrEEYAKHIADVYMATyglshtrntkVGNDFVRGVSGGERKRVSIA 221
|
170 180
....*....|....*....|
gi 29170396 627 IAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLD 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
478-642 |
6.45e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARKM 557
Cdd:PRK10762 5 LQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-----FNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 558 -----IGICPQsDMNF-DVLTVEENL----SILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGI 627
Cdd:PRK10762 76 sqeagIGIIHQ-ELNLiPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170
....*....|....*
gi 29170396 628 AVLGNPKILLLDEPT 642
Cdd:PRK10762 155 VLSFESKVIIMDEPT 169
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
490-658 |
7.33e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE--MFEARK---MIGICPQS 564
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSdiqMIFQDPLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 565 DMNfDVLTVEEnlsilasvkgipannIIQEVQKVLL-DLDMQAIKD---NQAKKL--------------SGGQKRKLSLG 626
Cdd:PRK15079 110 SLN-PRMTIGE---------------IIAEPLRTYHpKLSRQEVKDrvkAMMLKVgllpnlinryphefSGGQCQRIGIA 173
|
170 180 190
....*....|....*....|....*....|..
gi 29170396 627 IAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK 658
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQ 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-646 |
1.00e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.85 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCpPSDGFASIYGHRVSEID--EMFEARKMIGIC---P 562
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrrALRPLRRRMQVVfqdP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 563 QSDMN--FDVL-TVEENLSILAsvKGIPANNIIQEVQKVL----LDLDMQaikDNQAKKLSGGQKRKLSlgIA---VLgN 632
Cdd:COG4172 372 FGSLSprMTVGqIIAEGLRVHG--PGLSAAERRARVAEALeevgLDPAAR---HRYPHEFSGGQRQRIA--IAralIL-E 443
|
170
....*....|....
gi 29170396 633 PKILLLDEPTAGMD 646
Cdd:COG4172 444 PKLLVLDEPTSALD 457
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
497-697 |
2.29e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghRVSeidemfeARKMIGICPQSD--MN------- 567
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG-------RVW-------AERSIAYVPQQAwiMNatvrgni 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 568 --FDvltvEENLSILASVkgipanniiqeVQKVLLDLDMQAIKD-------NQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PTZ00243 742 lfFD----EEDAARLADA-----------VRVSQLEADLAQLGGgleteigEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29170396 639 DEPTAGMDP-CSRHIVWNLLKYRKANRVTVFSTHfmdEADIL--ADRKAVISQGMLKCVGSS 697
Cdd:PTZ00243 807 DDPLSALDAhVGERVVEECFLGALAGKTRVLATH---QVHVVprADYVVALGDGRVEFSGSS 865
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
488-646 |
3.48e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMN 567
Cdd:PLN03232 1243 RYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRRVLSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 568 FDVlTVEENLSILAS------VKGIPANNIIQEVQKVLLDLDMQAIKDNQakKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PLN03232 1322 FSG-TVRFNIDPFSEhndadlWEALERAHIKDVIDRNPFGLDAEVSEGGE--NFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
....*
gi 29170396 642 TAGMD 646
Cdd:PLN03232 1399 TASVD 1403
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
497-667 |
3.89e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 51.00 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFasiyghrvseidemfearkmIGICPQSDMNFdvltveen 576
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR--------------------IGMPEGEDLLF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 lsilasvkgIPanniiqevQKVLLDLD--MQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVW 654
Cdd:cd03223 69 ---------LP--------QRPYLPLGtlREQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|...
gi 29170396 655 NLLKYRKANRVTV 667
Cdd:cd03223 132 QLLKELGITVISV 144
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
455-696 |
3.95e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 455 INGNISLNEIVEPVSSEF----------IGKEAIRISGIQKAYRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLM 524
Cdd:PLN03130 582 VNANVSLKRLEELLLAEErvllpnpplePGLPAISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 525 NILCGLCPP-SDGFASIYGH--RVSEIDEMFEArkmigicpqsdmnfdvlTVEENLSILASVKGIPANNIIqEVQKVLLD 601
Cdd:PLN03130 661 SAMLGELPPrSDASVVIRGTvaYVPQVSWIFNA-----------------TVRDNILFGSPFDPERYERAI-DVTALQHD 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 602 LDMQAIKD-----NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-CSRHIVWNLLK--YRKANRVTVFST-HF 672
Cdd:PLN03130 723 LDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKdeLRGKTRVLVTNQlHF 802
|
250 260
....*....|....*....|....
gi 29170396 673 MDEadilADRKAVISQGMLKCVGS 696
Cdd:PLN03130 803 LSQ----VDRIILVHEGMIKEEGT 822
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-671 |
6.39e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.10 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQSDMNfDVLTVEEN 576
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGIN-PYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 lsilaSVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS-RHIVWN 655
Cdd:PRK13540 95 -----CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSlLTIITK 169
|
170
....*....|....*.
gi 29170396 656 LLKYRKANRVTVFSTH 671
Cdd:PRK13540 170 IQEHRAKGGAVLLTSH 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
497-696 |
8.03e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQSDMnFDVLTVEEN 576
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAW-IQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 LsILASVKGIPANNIIQEVQKVLLDLDMQAIKDN-----QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-CSR 650
Cdd:TIGR00957 719 I-LFGKALNEKYYQQVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29170396 651 HIVWNLL--KYRKANRVTVFSTH---FMDEADILadrkAVISQGMLKCVGS 696
Cdd:TIGR00957 798 HIFEHVIgpEGVLKNKTRILVTHgisYLPQVDVI----IVMSGGKISEMGS 844
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
497-677 |
8.28e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.79 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIYGHRVSEIDEMFEA-----RKMIGICPQSDMNFDVl 571
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 572 TVEENLSIlasvkGIPANN----IIQEVQKVLLDLDMQAIKDN-----QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:cd03290 94 TVEENITF-----GSPFNKqrykAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29170396 643 AGMD-PCSRHIVW-NLLKY-RKANRVTVFSTH---FMDEAD 677
Cdd:cd03290 169 SALDiHLSDHLMQeGILKFlQDDKRTLVLVTHklqYLPHAD 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
499-642 |
8.56e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 499 NLSFdiYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvseidemfEARKM----IGICPQS---DMNFDVL 571
Cdd:PRK11819 27 SLSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----------------EARPApgikVGYLPQEpqlDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 572 -TVEENLS----ILASVKGIPAN-------------------NIIQevQKVLLDLD------MQAIK----DNQAKKLSG 617
Cdd:PRK11819 89 eNVEEGVAevkaALDRFNEIYAAyaepdadfdalaaeqgelqEIID--AADAWDLDsqleiaMDALRcppwDAKVTKLSG 166
|
170 180
....*....|....*....|....*
gi 29170396 618 GQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
491-647 |
1.29e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.44 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 491 NETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS-----DGFasiyghRVSEIDEM----FEARKMIG-- 559
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtaDRF------RWNGIDLLklspRERRKIIGre 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 560 IC-----PQSDMNfDVLTVEENLsilasVKGIPANN---------------IIQEVQKVlldldmqAIKDNQA------K 613
Cdd:COG4170 91 IAmifqePSSCLD-PSAKIGDQL-----IEAIPSWTfkgkwwqrfkwrkkrAIELLHRV-------GIKDHKDimnsypH 157
|
170 180 190
....*....|....*....|....*....|....
gi 29170396 614 KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMES 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
441-646 |
1.38e-06 |
|
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: 51.86 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 441 SKNK---RNYKELSEGNINGNISLNEIVEPVSsEFIGKEAIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSG 517
Cdd:TIGR03719 284 AKSKarlARYEELLSQEFQKRNETAEIYIPPG-PRLGDKVIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 518 TGKSTLMNILCGLCPPSDGFASIyGHRVSeidemfearkmIGICPQSDMNFDvltveenlsilasvkgiPANNIIQEVQK 597
Cdd:TIGR03719 359 AGKSTLFRMITGQEQPDSGTIEI-GETVK-----------LAYVDQSRDALD-----------------PNKTVWEEISG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29170396 598 VLLDLDMQAIKDN--------------QAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR03719 410 GLDIIKLGKREIPsrayvgrfnfkgsdQQKKvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
501-689 |
1.70e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG-----FASIygHRVSeidemFEA-RKMIGICPQsDMNFDVLTVE 574
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqFSHI--TRLS-----FEQlQKLVSDEWQ-RNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 575 ENLSilasvkGIPANNIIQE-------VQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK10938 95 EDDT------GRTTAEIIQDevkdparCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29170396 648 CSRHIVWNLLKYRKANRVTV------FST--HFMDEADILADRkAVISQG 689
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLvlvlnrFDEipDFVQFAGVLADC-TLAETG 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
506-646 |
2.46e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.06 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 506 EGQITALLGHSGTGKSTLMNILCG-----LC----PPS-DGFASIYghRVSEIDEMFEARKmigicpqsDMNFDVLTVEE 575
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpnLGkfddPPDwDEILDEF--RGSELQNYFTKLL--------EGDVKVIVKPQ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 576 NLSIL-ASVKGIPANNIIQEVQKVLLD-----LDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03236 95 YVDLIpKAVKGKVGELLKKKDERGKLDelvdqLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
497-658 |
2.59e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.35 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIygHRVSEIDEMFEARK--MIG------IC-PQSDMN 567
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG--RI--ARPAGARVLFLPQRpyLPLgtlreaLLyPATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 568 FDVLTVEEnlsILASVkGIPAnniiqevqkvLLD-LDMQAikdNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG4178 455 FSDAELRE---ALEAV-GLGH----------LAErLDEEA---DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170
....*....|..
gi 29170396 647 PCSRHIVWNLLK 658
Cdd:COG4178 518 EENEAALYQLLR 529
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-646 |
2.62e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQSDMNFDVlTVEEN 576
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 577 LSILASVKGIPANNIIQEVQkVLLDLDMQAIKDNQ-----AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQ-LEEDIALFPEKDKTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
497-646 |
2.63e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQSDMNFDVlTVEEN 576
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM-DLRKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 577 LSIL--------------ASVKGIPANNIIQevqkvlLDLDMQAIKDNqakkLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PLN03130 1333 LDPFnehndadlweslerAHLKDVIRRNSLG------LDAEVSEAGEN----FSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
....
gi 29170396 643 AGMD 646
Cdd:PLN03130 1403 AAVD 1406
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
496-691 |
3.17e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE------IDEMF----EARKMIGICPQSD 565
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneaINHGFalvtEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 566 MNFDVLTveENLSILASVKGIPANNIIQEvqkvlldlDMQAIKDNQAKK----------LSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK10982 343 IGFNSLI--SNIRNYKNKVGLLDNSRMKS--------DTQWVIDSMRVKtpghrtqigsLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 636 LLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLiAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
494-695 |
3.29e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEARKMI---------GICP 562
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgKLQALRRDIqfifqdpyaSLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 563 QSDMNFDVLtveENLSILASVKGIPANniiqevQKVLLDLDMQAIKDNQA----KKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PRK10261 417 RQTVGDSIM---EPLRVHGLLPGKAAA------ARVAWLLERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29170396 639 DEPTAGMDPCSRHIVWNLL--KYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLldLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
497-651 |
3.44e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCG-LCPPSD-------GFASIYGHRVSEIDEMFEARkMIGICPQSDMNF 568
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLAR-LRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 569 DVLTVEENLSI----LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAV---------LGNPKI 635
Cdd:PRK13547 96 FAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170
....*....|....*.
gi 29170396 636 LLLDEPTAGMDPCSRH 651
Cdd:PRK13547 176 LLLDEPTAALDLAHQH 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
497-653 |
4.28e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpsDGFAS---IYGHRVSEIDEMFEARKMIG-ICPQSDMNFDVLT 572
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGYSNdltLFGRRRGSGETIWDIKKHIGyVSSSLHLDYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 573 VEENLSILASVKGIpanNIIQEV---QKVLLD--LDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:PRK10938 354 SVRNVILSGFFDSI---GIYQAVsdrQQKLAQqwLDILGIDKRTADApfhsLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
|
170
....*....|
gi 29170396 644 GMDPCSRHIV 653
Cdd:PRK10938 431 GLDPLNRQLV 440
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
503-646 |
6.88e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.78 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 503 DIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEmfEARkmIGICPQ---SDMNfdvLTVEENLSi 579
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------EVDE--DLK--ISYKPQyisPDYD---GTVEEFLR- 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 580 LASVKGIPANNIIQEVQKvllDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG1245 424 SANTDDFGSSYYKTEIIK---PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
496-689 |
8.05e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQSDMNFDVlTVEE 575
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL-QLDSWRSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 576 NLSI---LASVKGIPANNIIQEVQKVLLDLDmQAIKDNQAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:PRK10789 408 NIALgrpDATQQEIEHVARLASVHDDILRLP-QGYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29170396 650 RH-IVWNLLKYRKaNRVTVFSTHFMdEADILADRKAVISQG 689
Cdd:PRK10789 487 EHqILHNLRQWGE-GRTVIISAHRL-SALTEASEILVMQHG 525
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
494-532 |
8.64e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 8.64e-06
10 20 30
....*....|....*....|....*....|....*....
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP 532
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP 52
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
494-646 |
9.58e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGHRV-----SEIDEM-FEARKMIGICPQS 564
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELNKLrAEQISMIFQDPMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 565 DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLldldmQAIKDNQAKK--------LSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRML-----DAVKMPEARKrmkmypheFSGGMRQRVMIAMALLCRPKLL 183
|
170
....*....|
gi 29170396 637 LLDEPTAGMD 646
Cdd:PRK09473 184 IADEPTTALD 193
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
497-646 |
9.67e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.31 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQSDMNFDVlTVEEN 576
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29170396 577 LSILASVKGIPANNIIQEVQkvlLDLDMQAI--KDNQ-----AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQ---LEEDITKFpeKDNTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
494-653 |
1.15e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIY-----GHRVSEIDEMFEARKMIG--------- 559
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFknehtNDMTNEQDYQGDEEQNVGmknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 560 -------------------------ICpqsDMN-------FDVLTVEE---NLSILASVKGIPANNIIQEVQKV----LL 600
Cdd:PTZ00265 1261 tkeggsgedstvfknsgkilldgvdIC---DYNlkdlrnlFSIVSQEPmlfNMSIYENIKFGKEDATREDVKRAckfaAI 1337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 601 DLDMQAIKDNQ-------AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIV 653
Cdd:PTZ00265 1338 DEFIESLPNKYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
489-529 |
1.43e-05 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 47.80 E-value: 1.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 29170396 489 KKNETVEALRnlsfDIYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:COG1162 152 KTGEGLDELR----ELLKGKTSVLVGQSGVGKSTLINALLP 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
504-646 |
1.54e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 504 IYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASiyghrvSEIDemfearkmIGICPQ-----SDMnfdvlTVEENLS 578
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELK--------ISYKPQyikpdYDG-----TVEDLLR 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29170396 579 ilaSVKGIPANNIIQEvqKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK13409 423 ---SITDDLGSSYYKS--EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
489-529 |
1.56e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 47.01 E-value: 1.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 29170396 489 KKNETVEALRNLsfdiYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:cd01854 71 KTGEGLDELREL----LKGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
477-646 |
8.27e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEMFEARk 556
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSENAN- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 557 mIGICPQ-SDMNFDV-LTVEENLSILASVKGIpanniIQEVQKVLLDLDMQA--IKdNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:PRK15064 384 -IGYYAQdHAYDFENdLTLFDWMSQWRQEGDD-----EQAVRGTLGRLLFSQddIK-KSVKVLSGGEKGRMLFGKLMMQK 456
|
170
....*....|....
gi 29170396 633 PKILLLDEPTAGMD 646
Cdd:PRK15064 457 PNVLVMDEPTNHMD 470
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
487-646 |
1.99e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.32 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 487 YRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSD- 565
Cdd:TIGR00957 1294 YREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG-LHDLRFKITIIPQDPv 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 566 -------MNFDVLTVEENLSI-----LASVKGIpanniiqeVQKVLLDLDMQAIKDNQakKLSGGQKRKLSLGIAVLGNP 633
Cdd:TIGR00957 1371 lfsgslrMNLDPFSQYSDEEVwwaleLAHLKTF--------VSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKT 1440
|
170
....*....|...
gi 29170396 634 KILLLDEPTAGMD 646
Cdd:TIGR00957 1441 KILVLDEATAAVD 1453
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
489-529 |
2.59e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 42.53 E-value: 2.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 29170396 489 KKNETVEALRNLsfdiYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:pfam03193 92 KTGEGIEALKEL----LKGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
501-642 |
2.83e-04 |
|
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: 44.78 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 501 SFDIY------EGQITALLGHSGTGKSTLMNILCGLCPPSDGfasIYGH-----------RVSEIDEMFE---------A 554
Cdd:COG1245 87 GFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYDEepswdevlkrfRGTELQDYFKklangeikvA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 555 RKmigicPQS-DMNFDVL--TVEEnlsILASV--KGIpANNIIQEvqkvlldLDMQAIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:COG1245 164 HK-----PQYvDLIPKVFkgTVRE---LLEKVdeRGK-LDELAEK-------LGLENILDRDISELSGGELQRVAIAAAL 227
|
170
....*....|...
gi 29170396 630 LGNPKILLLDEPT 642
Cdd:COG1245 228 LRDADFYFFDEPS 240
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
473-527 |
2.88e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 44.04 E-value: 2.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 29170396 473 IGKEAIRISGiqkayrKKNETVEALRNLsfdiYEGQITALLGHSGTGKSTLMNIL 527
Cdd:PRK00098 140 IGYDVLELSA------KEGEGLDELKPL----LAGKVTVLAGQSGVGKSTLLNAL 184
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
497-671 |
3.96e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFearkmigiCPQSDMNFDV---LTV 573
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--------CTYIGHNLGLkleMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 574 EENLSILASVKgipanNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIV 653
Cdd:PRK13541 88 FENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|
gi 29170396 654 WNLLKYrKANR--VTVFSTH 671
Cdd:PRK13541 163 NNLIVM-KANSggIVLLSSH 181
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
498-665 |
5.83e-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: 42.21 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 498 RNLSFDIYEGqITALLGHSGTGKSTLMNILcglcppsdgFASIYGHRVSEIDEMFEARKMIGICP---QSDMNFDV---- 570
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTTIIEAL---------KYALTGELPPNSKGGAHDPKLIREGEvraQVKLAFENangk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 571 -LTVEENLSILASVKGIPanniiQEVQKVLLdLDMqaikdnqAKKLSGGQKRKLSLGI------AVLGNPKILLLDEPTA 643
Cdd:cd03240 84 kYTITRSLAILENVIFCH-----QGESNWPL-LDM-------RGRCSGGEKVLASLIIrlalaeTFGSNCGILALDEPTT 150
|
170 180
....*....|....*....|...
gi 29170396 644 GMDPCSRHIVW-NLLKYRKANRV 665
Cdd:cd03240 151 NLDEENIEESLaEIIEERKSQKN 173
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
572-646 |
1.43e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 572 TVEENLSiLASVKGIPANNIIQEVQKVLLDLDMQA---IK----DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:NF040905 356 DIKRNIT-LANLGKVSRRGVIDENEEIKVAEEYRKkmnIKtpsvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRG 434
|
..
gi 29170396 645 MD 646
Cdd:NF040905 435 ID 436
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
613-689 |
1.48e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 613 KKLSGGQKRKLS----LGIAVLGNPKILLLDEPTAGMDPCSRH-IVWNLLKYRKANRVTVFSTH---FMDEADILADRKA 684
Cdd:cd03227 76 LQLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQaLAEAILEHLVKGAQVIVITHlpeLAELADKLIHIKK 155
|
....*
gi 29170396 685 VISQG 689
Cdd:cd03227 156 VITGV 160
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
507-647 |
1.91e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.66 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 507 GQITALLGHSGTGKSTLMNILCGLCPPSdgfasiyGHRVSEIDemfearkmigicpqsdmnfdvltveenlsilasvkgi 586
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPP-------GGGVIYID------------------------------------- 37
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29170396 587 panniIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:smart00382 38 -----GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDA 93
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
491-646 |
5.16e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 491 NETvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcPPS----DGFASIYGHRVSEIDEmfEARKMIGI------ 560
Cdd:CHL00131 18 NEN-EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEP--EERAHLGIflafqy 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 561 ---CPQSDmNFDVLTVEEN----LSILASVKGIPANNIIQEVQKvLLDLDMQAIKDNQAKKLSGGQKRKLS-LGIAVLgN 632
Cdd:CHL00131 93 pieIPGVS-NADFLRLAYNskrkFQGLPELDPLEFLEIINEKLK-LVGMDPSFLSRNVNEGFSGGEKKRNEiLQMALL-D 169
|
170
....*....|....
gi 29170396 633 PKILLLDEPTAGMD 646
Cdd:CHL00131 170 SELAILDETDSGLD 183
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
441-536 |
5.44e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29170396 441 SKNK---RNYKELSEGNINGNISLNEIVEPVSsEFIGKEAIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSG 517
Cdd:PRK11819 286 AKSKarlARYEELLSEEYQKRNETNEIFIPPG-PRLGDKVIEAENLSKSFGDR----LLIDDLSFSLPPGGIVGIIGPNG 360
|
90
....*....|....*....
gi 29170396 518 TGKSTLMNILCGLCPPSDG 536
Cdd:PRK11819 361 AGKSTLFKMITGQEQPDSG 379
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
506-529 |
7.70e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 7.70e-03
10 20
....*....|....*....|....
gi 29170396 506 EGQITALLGHSGTGKSTLMNILCG 529
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLG 217
|
|
| |
