|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-229 |
1.23e-101 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 297.75 E-value: 1.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGmLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYLS 86
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 167 QGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:COG1131 160 SGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-229 |
9.90e-80 |
|
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: 242.46 E-value: 9.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMlAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYL 85
Cdd:COG4555 1 MIEVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 166 TQGLDPESVAEFLSLITSLRDTEHmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-217 |
8.83e-77 |
|
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: 232.29 E-value: 8.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMlAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYLS 86
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYtarflglsakerrerilgalqrmrlenrkndkvhtfSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03230 80 EEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 359351306 167 QGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:cd03230 124 SGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-317 |
2.03e-75 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 233.08 E-value: 2.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRtpLEVKRRVGYL 85
Cdd:COG4152 1 MLELKGLTKRFG-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLD--PEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 166 TQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQqfGGRQIIELRVDSEK 245
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ--FGRNTLRLEADGDA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 246 NLAETFAGISEVTKVlpagRQTWNLECMEDvrpAVANAVFKEGIGLISI---EMQMHSLYDIykasFKEVADETA 317
Cdd:COG4152 234 GWLRALPGVTVVEED----GDGAELKLEDG---ADAQELLRALLARGPVrefEEVRPSLNEI----FIEVVGEKA 297
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-221 |
3.27e-69 |
|
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: 214.39 E-value: 3.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGmLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRtPLEVKRRVGYLS 86
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLsakeRRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEhMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-221 |
5.07e-69 |
|
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: 213.98 E-value: 5.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMlAVDDISLTLNKGeIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYLS 86
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 167 QGLDPESVAEFLSLITSLrdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03264 159 AGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-226 |
1.43e-68 |
|
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: 213.00 E-value: 1.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 9 ISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYLSDT 88
Cdd:cd03265 3 VENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 VGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQG 168
Cdd:cd03265 82 LSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 169 LDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-305 |
2.11e-68 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 215.33 E-value: 2.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 14 KQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYLSDTVGFYD 93
Cdd:TIGR01188 1 KVYGD-FKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 94 TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPES 173
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 174 VAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ------QFGGRQIIELRVDSEK-- 245
Cdd:TIGR01188 160 RRAIWDYIRALKE-EGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRlgkdtlESRPRDIQSLKVEVSMli 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 246 -NLAETFAGISEVTkvLPAGRQTWNLECMEDVRPAVANAVFKEGIGLISIEMQMHSLYDIY 305
Cdd:TIGR01188 239 aELGETGLGLLAVT--VDSDRIKILVPDGDETVPEIVEAAIRNGIRIRSISTERPSLDDVF 297
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-226 |
3.66e-63 |
|
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: 199.27 E-value: 3.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGM-LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYL 85
Cdd:cd03263 1 LQIRNLTKTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 --SDTvgFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:cd03263 81 pqFDA--LFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-221 |
2.14e-62 |
|
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: 197.20 E-value: 2.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYG---KGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVG 83
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDTEHmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-226 |
3.19e-59 |
|
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: 189.47 E-value: 3.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL-EVKRRVGYL 85
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 ---------SDTVgfydtmtaYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:COG1122 81 fqnpddqlfAPTV--------EEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-216 |
4.28e-59 |
|
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: 188.64 E-value: 4.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRTplEVKRRVGYLS 86
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-KPLDI--AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 359351306 167 QGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGK 216
Cdd:cd03269 157 SGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-217 |
1.37e-54 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 177.59 E-value: 1.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMlAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLevkRRVGYLS 86
Cdd:TIGR03740 1 LETKNLSKRFGKQT-AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDL---HKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLSakerRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 359351306 167 QGLDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFP-EQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-216 |
4.60e-54 |
|
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: 175.73 E-value: 4.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 8 SISHLRKQYGKGM-LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL-EVKRRVGYL 85
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 sdtvgFYD------TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEI 159
Cdd:cd03225 81 -----FQNpddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 160 AILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGK 216
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-253 |
1.61e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 175.28 E-value: 1.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplRTPLEVKR 80
Cdd:COG1121 1 MMMMPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 RVGYLSDTVGFYDT--MTAYE----NLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLV 154
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 155 KNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGkLLKNGTVAElseqqfggr 234
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEE--------- 224
|
250
....*....|....*....
gi 359351306 235 qiielrVDSEKNLAETFAG 253
Cdd:COG1121 225 ------VLTPENLSRAYGG 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-231 |
4.15e-52 |
|
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: 171.32 E-value: 4.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTP----LEV 78
Cdd:COG1127 2 SEPMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYLsdtvgF-----YDTMTAYENLDYTAR-FLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEV 152
Cdd:COG1127 81 RRRIGML-----FqggalFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 153 LVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE---- 228
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAsddp 235
|
....*
gi 359351306 229 --QQF 231
Cdd:COG1127 236 wvRQF 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-205 |
7.55e-52 |
|
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: 169.58 E-value: 7.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYL 85
Cdd:COG4133 2 MLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTMTAYENLDYTARFLGLSAkeRRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 359351306 166 TQGLDPESVAEFLSLITSLRDTEHMtILLSSHQLEEVQSV 205
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELAAA 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
2.89e-51 |
|
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: 176.63 E-value: 2.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRKQYGKGML-AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPT---SGSVDILGFDPLRTPLEVK 79
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 80 -RRVGYLsdtvgFYDTMTA------YENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEV 152
Cdd:COG1123 82 gRRIGMV-----FQDPMTQlnpvtvGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 153 LVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-226 |
8.13e-51 |
|
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: 175.48 E-value: 8.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYG----KGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD----PLR 73
Cdd:COG1123 256 AAEPLLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 74 TPLEVKRRVGYLsdtvgFYD-------TMTAYENLDYTARFLG-LSAKERRERILGALQRMRLENRKNDK-VHTFSHGMK 144
Cdd:COG1123 336 SLRELRRRVQMV-----FQDpysslnpRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLADRyPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 145 QRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVA 224
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
..
gi 359351306 225 EL 226
Cdd:COG1123 491 EV 492
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-226 |
7.89e-49 |
|
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: 163.06 E-value: 7.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDplRTPL------EVKR 80
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGED--ISGLseaelyRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 RVGYLSDTVGFYDTMTAYENLDYTAR-FLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEI 159
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 160 AILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-221 |
2.28e-48 |
|
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: 161.15 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKRRVGYLS 86
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-225 |
3.15e-48 |
|
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: 161.45 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV-----DILGFDPLRTpleVKRR 81
Cdd:cd03219 1 LEVRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeDITGLPPHEI---ARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSDTVGFYDTMTAYENL--------DYTARFLGLSAKER--RERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAE 151
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVmvaaqartGSGLLLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 152 VLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-217 |
5.15e-48 |
|
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: 160.35 E-value: 5.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGML---AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRtpLEVKRRVG 83
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISK--LSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGF----Y---DTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:cd03255 79 FRRRHIGFvfqsFnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQlEEVQSVCDRVGLFYRGKL 217
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-260 |
1.13e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 162.28 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLeVKRR 81
Cdd:PRK13537 4 SVAPIDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvPSRARH-ARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 162 LDEPTQGLDPES---VAEFL-SLITSLRdtehmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQFGGrQII 237
Cdd:PRK13537 162 LDEPTTGLDPQArhlMWERLrSLLARGK-----TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGC-DVI 235
|
250 260
....*....|....*....|...
gi 359351306 238 ELRVDSEKNLAETFAGISEVTKV 260
Cdd:PRK13537 236 EIYGPDPVALRDELAPLAERTEI 258
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-226 |
2.09e-45 |
|
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: 153.89 E-value: 2.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYG---KGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTP----LEV 78
Cdd:cd03258 1 MIELKNVSKVFGdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCE 158
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 159 IAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-223 |
3.64e-45 |
|
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: 152.69 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPlevkRRVGYLSDTVGFyDT---MTAY 98
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVPQRRSI-DRdfpISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 99 E----NLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESV 174
Cdd:cd03235 89 DvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 359351306 175 AEFLSLITSLRDTEhMTILLSSHQLEEVQSVCDRVglfyrgkLLKNGTV 223
Cdd:cd03235 169 EDIYELLRELRREG-MTILVVTHDLGLVLEYFDRV-------LLLNRTV 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-225 |
8.92e-45 |
|
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: 152.89 E-value: 8.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV-----DILGFDP------ 71
Cdd:COG0411 1 SDPLLEVRGLTKRFG-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrDITGLPPhriarl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 72 --LRTplevkrrvgylsdtvgF-----YDTMTAYENL-------------DYTARFLGLSAKER--RERILGALQRMRLE 129
Cdd:COG0411 80 giART----------------FqnprlFPELTVLENVlvaaharlgrgllAALLRLPRARREEReaRERAEELLERVGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 130 NRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRV 209
Cdd:COG0411 144 DRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRI 223
|
250
....*....|....*.
gi 359351306 210 GLFYRGKLLKNGTVAE 225
Cdd:COG0411 224 VVLDFGRVIAEGTPAE 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-217 |
1.70e-44 |
|
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: 151.50 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGML---AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVK--- 79
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 80 -RRVGYLsdtvgFYD-------TMTAYENLDYTARFLGLSAKERRERILGALQRMRL---ENRKNDKVHTFSHGMKQRLG 148
Cdd:cd03257 81 rKEIQMV-----FQDpmsslnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 149 LAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-230 |
3.40e-44 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 161.06 E-value: 3.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG--FDPlrTPLEVKRRVGYLSDTVGFYDTMTAYE 99
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDA--GDIATRRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 100 NLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPesVA--EF 177
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP--VArdMF 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 359351306 178 LSLITSLRDTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:NF033858 437 WRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAAR 488
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-231 |
5.94e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 147.90 E-value: 5.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPL----RTPLEVKRR 81
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrgRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSDTVGFYDTMTAYEN-----LDYT---ARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVL 153
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrLGRTstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 154 VKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDR-VGLfYRGKLLKNGTVAELSEQQF 231
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRiIGL-RDGRVVFDGPPAELTDAVL 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-209 |
7.51e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.11 E-value: 7.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSeqVLSISHLRKQYGKGML---AVDDISLTLNKGEIFGLLGPNGSGKTTtILMLLGLLE-PTSGSVDILGFDPLRtpL 76
Cdd:COG1136 1 MSP--LLELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKST-LLNILGGLDrPTSGEVLIDGQDISS--L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 EVKRRVGYLSDTVGF----Y---DTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGL 149
Cdd:COG1136 76 SERELARLRRRHIGFvfqfFnllPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQlEEVQSVCDRV 209
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRV 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-216 |
9.45e-43 |
|
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: 144.69 E-value: 9.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 8 SISHLRKQYGKGmLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL-EVKRRVGYls 86
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 dtvgfydtmtayenldytarflglsakerrerilgalqrmrlenrkndkVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd00267 78 -------------------------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 359351306 167 QGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGK 216
Cdd:cd00267 109 SGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-226 |
1.46e-42 |
|
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: 149.05 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQY--GKGML-AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEP---TSGSV-----DILGFDP--- 71
Cdd:COG0444 1 LLEVRNLKVYFptRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEIlfdgeDLLKLSEkel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 72 --LRtplevKRRVGYLsdtvgFYDTMTAyenLD--YT---------ARFLGLSAKERRERILGALQRMRL---ENRKNDK 135
Cdd:COG0444 81 rkIR-----GREIQMI-----FQDPMTS---LNpvMTvgdqiaeplRIHGGLSKAEARERAIELLERVGLpdpERRLDRY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 136 VHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRG 215
Cdd:COG0444 148 PHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAG 227
|
250
....*....|.
gi 359351306 216 KLLKNGTVAEL 226
Cdd:COG0444 228 RIVEEGPVEEL 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-166 |
1.58e-42 |
|
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: 143.94 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLE-VKRRVGYLSDTVGFYDTMTAYENL 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 102 DYTARFLGLSAKERRERILGALQRMRLENRKNDKV----HTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-226 |
3.67e-42 |
|
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: 145.38 E-value: 3.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPlrTPLEVKRR----V 82
Cdd:cd03218 1 LRAENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI--TKLPMHKRarlgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 83 GYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAIL 162
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 163 DEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-226 |
8.47e-42 |
|
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: 145.19 E-value: 8.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRT--PLEVKRRVG 83
Cdd:COG1120 1 MLEAENLSVGYGGRPV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLASlsRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYE-----NLDYTARFLGLSAKErRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCE 158
Cdd:COG1120 79 YVPQEPPAPFGLTVRElvalgRYPHLGLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 159 IAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-239 |
1.36e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 147.28 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLeVKRR 81
Cdd:PRK13536 38 STVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvPARARL-ARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 162 LDEPTQGLDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQFGGrQIIEL 239
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGC-QVIEI 271
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-226 |
1.76e-41 |
|
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: 145.29 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDP-------LRtplEVKRRVGYL--------- 85
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkkkkLK---DLRKKVGLVfqfpehqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVgfydtmtaYENLDYTARFLGLSAKERRERILGALQRMRLEnRKNDKVHTF--SHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:TIGR04521 97 EETV--------YKDIAFGPKNLGLSEEEAEERVKEALELVGLD-EEYLERSPFelSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-229 |
3.21e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.40 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKRRVGYLs 86
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-KRNVGMV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 dtvgFYD-----TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:COG3842 83 ----FQDyalfpHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 162 LDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-249 |
3.87e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 145.62 E-value: 3.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPlrtpleVKRRVGYLSD-TVGF-------YD 93
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP------FKRRKEFARRiGVVFgqrsqlwWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 94 tMTAYENLDYTARFLGLSAKERRERiLGAL-QRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPE 172
Cdd:COG4586 111 -LPAIDSFRLLKAIYRIPDAEYKKR-LDELvELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 173 SVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEqQFGGRQIIELRVDSEKNLAE 249
Cdd:COG4586 189 SKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE-RFGPYKTIVLELAEPVPPLE 264
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-226 |
2.30e-40 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 141.26 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRR--VG 83
Cdd:TIGR04406 1 TLVAENLIKSYKK-RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYTARFLG-LSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAIL 162
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 163 DEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-216 |
2.89e-40 |
|
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: 138.86 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD---PLRTPLEVKRRVG 83
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYtarflGLSAkerrerilgalqrmrlenrkndkvhtfshGMKQRLGLAEVLVKNCEIAILD 163
Cdd:cd03229 80 MVFQDFALFPHLTVLENIAL-----GLSG-----------------------------GQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGK 216
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-226 |
3.02e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 141.80 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPL--RTPLEVKRRVG 83
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YL-------------SDTVGFydtmtAYENLdytarflGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLA 150
Cdd:TIGR04520 81 MVfqnpdnqfvgatvEDDVAF-----GLENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 151 EVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAEL 226
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-226 |
6.15e-40 |
|
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: 139.62 E-value: 6.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMlAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLE-----PTSGSVDILG---FDPLRTPLEV 78
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdiYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYLsdtvgFYDT----MTAYENLDYTARFLG-LSAKERRERILGALQRMRLENRKNDKVH--TFSHGMKQRLGLAE 151
Cdd:cd03260 80 RRRVGMV-----FQKPnpfpGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 152 VLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTehMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-228 |
3.52e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 137.85 E-value: 3.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPlrTPLEVKRR---- 81
Cdd:COG1137 3 TLEAENLVKSYGK-RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI--THLPMHKRarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 162 LDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKE-RGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-226 |
8.78e-39 |
|
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: 137.05 E-value: 8.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRT-PLEVKRRVGYL 85
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLE--NRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-226 |
9.26e-39 |
|
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: 137.14 E-value: 9.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSG-SVDILGFDPLRTPL-EVKRR 81
Cdd:COG1119 1 DPLLELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVwELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLS--------------DTV--GFYDTMTAYENLDytarflglsaKERRERILGALQRMRLENRKNDKVHTFSHGMKQ 145
Cdd:COG1119 80 IGLVSpalqlrfprdetvlDVVlsGFFDSIGLYREPT----------DEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 146 RLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229
|
.
gi 359351306 226 L 226
Cdd:COG1119 230 V 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-229 |
2.17e-38 |
|
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: 135.83 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKRRVGYLS 86
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-226 |
4.67e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.98 E-value: 4.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPL----RTPLEVKRR 81
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIkydkKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYL---SDTVGFYDTMTayENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCE 158
Cdd:PRK13639 80 VGIVfqnPDDQLFAPTVE--EDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 159 IAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-217 |
6.44e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.02 E-value: 6.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD----------PLRtp 75
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlkrreipYLR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 76 levkRRVGY-------LSDtvgfydtMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLG 148
Cdd:COG2884 79 ----RRIGVvfqdfrlLPD-------RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 149 LAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEhMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-231 |
7.20e-38 |
|
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: 134.62 E-value: 7.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-------PLRTpleVK 79
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkALRQ---LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 80 RRVGYLSDTVGFYDTMTAYEN-----LDYTARF---LGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAE 151
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENvlsgrLGRRSTWrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 152 VLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDR-VGLfYRGKLLKNGTVAELSEQQ 230
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRiVGL-KDGRIVFDGPPAELTDEV 236
|
.
gi 359351306 231 F 231
Cdd:cd03256 237 L 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-221 |
1.16e-37 |
|
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: 134.00 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 8 SISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYL-- 85
Cdd:cd03267 22 SLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDtMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:cd03267 102 QKTQLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 166 TQGLD---PESVAEFLSLITSLRDTehmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03267 181 TIGLDvvaQENIRNFLKEYNRERGT---TVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-226 |
2.38e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.98 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY---GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV-----DILGFDP--LRtpl 76
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVlvdgvDLTALSEreLR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 EVKRRVGY-------LSdtvgfydTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGL 149
Cdd:COG1135 79 AARRKIGMifqhfnlLS-------SRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-212 |
2.94e-37 |
|
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: 132.21 E-value: 2.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGM---LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRTPlevKRRVG 83
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-LVDGEPVTGP---GPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLF 212
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-209 |
5.24e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.48 E-value: 5.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRT--PLEVKRRVGY 84
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-YLDGKPLSAmpPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSDTVGFYDtMTAYENLDYTARFLGLSAKerRERILGALQRMRLENRKNDK-VHTFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:COG4619 79 VPQEPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRV 209
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRV 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-221 |
6.37e-37 |
|
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: 130.25 E-value: 6.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 8 SISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLR-TPLEVKRRVGYLS 86
Cdd:cd03214 1 EVENLSVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DtvgfydtmtayenldytarflglsakerrerilgALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-230 |
1.01e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.47 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTtiLM--LLGLLEPTSGSVDILGFD-PLRTPLEV 78
Cdd:COG3845 1 MMPPALELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKST--LMkiLYGLYQPDSGEILIDGKPvRIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 kRRVGylsdtVG-----F--YDTMTAYENL---DYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLG 148
Cdd:COG3845 78 -IALG-----IGmvhqhFmlVPNLTVAENIvlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 149 LAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSE 230
|
..
gi 359351306 229 QQ 230
Cdd:COG3845 231 EE 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-228 |
7.92e-36 |
|
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: 128.71 E-value: 7.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLE--VKRRVGY 84
Cdd:cd03224 1 LEVENLNAGYGK-SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSDTVGFYDTMTAYENLDYTARFLGLSA-KERRERILGALQrmRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKrKARLERVYELFP--RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDTEhMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-209 |
1.01e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.44 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQ-VLSISHLRKQY---GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplRTPL 76
Cdd:COG1116 1 MSAAApALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 EVKRRVGYL--SDTVgfYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLV 154
Cdd:COG1116 77 GPGPDRGVVfqEPAL--LPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 155 KNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRV 209
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRV 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-226 |
1.22e-35 |
|
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: 129.69 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 21 LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTP----LEVKR-RVGYLSDTVGFYDTM 95
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelRELRRkKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 96 TAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVA 175
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 359351306 176 EFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-225 |
1.52e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.78 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLrkqYGKGM----LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL-- 76
Cdd:PRK13637 2 SIKIENLTHI---YMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 -EVKRRVGYL---SDTVGFYDTMtaYENLDYTARFLGLSAKERRERILGALQRMRL--ENRKNDKVHTFSHGMKQRLGLA 150
Cdd:PRK13637 79 sDIRKKVGLVfqyPEYQLFEETI--EKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 151 EVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-226 |
1.67e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.58 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPL----RTPLEVKRR 81
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIdysrKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLsdtvgFYD------TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVK 155
Cdd:PRK13636 84 VGMV-----FQDpdnqlfSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 156 NCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-217 |
7.49e-35 |
|
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: 125.72 E-value: 7.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG---FDPLRTPLEVKRRVG 83
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlklTDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYTAR-FLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAIL 162
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 163 DEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-217 |
1.71e-34 |
|
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: 125.34 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtplevkrRVGYLSD-TVGFYDTMTAYEN 100
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGlGGGFNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 101 LDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSL 180
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 359351306 181 ITSLRDTEhMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:cd03220 185 LRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-226 |
3.76e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.50 E-value: 3.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV-----DILGFDPlrtpleVKRR 81
Cdd:COG3839 4 LELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrDVTDLPP------KDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLsdtvgF-----YDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:COG3839 77 IAMV-----FqsyalYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-242 |
3.95e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFdPL--RTPLEV 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-VLseETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYL-------------SDTVGFydtmtAYENLdytarflGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQ 145
Cdd:PRK13635 80 RRQVGMVfqnpdnqfvgatvQDDVAF-----GLENI-------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 146 RLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAE 225
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEGTPEE 226
|
250
....*....|....*..
gi 359351306 226 LSEQqfgGRQIIELRVD 242
Cdd:PRK13635 227 IFKS---GHMLQEIGLD 240
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-209 |
4.09e-34 |
|
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: 123.91 E-value: 4.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 8 SISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDplRTPLEVKRRVGYLSD 87
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP--IKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGFYDTM-TAYENLDYTARFLGlsakERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03226 79 DVDYQLFTdSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHmTILLSSHQLEEVQSVCDRV 209
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRV 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-230 |
9.78e-34 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 123.85 E-value: 9.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYgKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRR--VG 83
Cdd:PRK10895 3 TLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYTARFL-GLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAIL 162
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 163 DEPTQGLDPESVAEFLSLITSLRDTeHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE-LSEQQ 230
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEiLQDEH 229
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-200 |
1.10e-33 |
|
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: 122.15 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 16 YGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPL----RTPLEVKRRVGYL---SDT 88
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAV-LIDGEPLdysrKGLLERRQRVGLVfqdPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 VGFYDTMtaYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQG 168
Cdd:TIGR01166 80 QLFAADV--DQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180 190
....*....|....*....|....*....|..
gi 359351306 169 LDPESVAEFLSLITSLRDtEHMTILLSSHQLE 200
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRA-EGMTVVISTHDVD 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-225 |
4.78e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 122.11 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 8 SISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdPLRTPLEVkrrvgylsd 87
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--RVSALLEL--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGFYDTMTAYENLDYTARFLGLSAKERRERI--------LGALQRMrlenrkndKVHTFSHGMKQRLGLAEVLVKNCEI 159
Cdd:COG1134 96 GAGFHPELTGRENIYLNGRLLGLSRKEIDEKFdeivefaeLGDFIDQ--------PVKTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 160 AILDEptqGLdpeSV--AEF----LSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:COG1134 168 LLVDE---VL---AVgdAAFqkkcLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-226 |
7.65e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 121.25 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGF---DPLRTPLEVKRRV 82
Cdd:COG1126 1 MIEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdltDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 83 GYLsdtvgF-----YDTMTAYENLDYTARF-LGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:COG1126 80 GMV-----FqqfnlFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-225 |
2.26e-32 |
|
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: 120.13 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLavDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKRRVGYLS 86
Cdd:cd03299 1 LKVENLSKDWKEFKL--KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-239 |
6.81e-32 |
|
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: 124.49 E-value: 6.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRTPLE--VKRRVG 83
Cdd:COG4987 334 LELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG-VDLRDLDEddLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTmTAYENLdytaRFLGLSAKErrERILGALQRMRLE---NRKNDKVHT--------FSHGMKQRLGLAEV 152
Cdd:COG4987 413 VVPQRPHLFDT-TLRENL----RLARPDATD--EELWAALERVGLGdwlAALPDGLDTwlgeggrrLSGGERRRLALARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 153 LVKNCEIAILDEPTQGLDPESVAEFLSLItsLRDTEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSEQQFG 232
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNGR 562
|
....*..
gi 359351306 233 GRQIIEL 239
Cdd:COG4987 563 YRQLYQR 569
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-226 |
8.92e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.41 E-value: 8.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMlAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRTPLEV-KRRVGYL 85
Cdd:COG1118 3 IEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLNGRDLFTNLPPrERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 sdtvgF--YD---TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIA 160
Cdd:COG1118 81 -----FqhYAlfpHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 161 ILDEPTQGLDpESVAEFL-SLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG1118 156 LLDEPFGALD-AKVRKELrRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-217 |
1.00e-31 |
|
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: 117.89 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 14 KQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPlevKRRVGYLSDTVG--F 91
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLR---GRAIPYLRRKIGvvF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 92 YD-----TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03292 85 QDfrllpDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 359351306 167 QGLDPESVAEFLSLITSLRDTeHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-231 |
1.10e-31 |
|
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: 118.55 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-------PLRtplEV 78
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklrgkKLR---KL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYLSDTVGFYDTMTAYENLdYTARF---------LGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGL 149
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENV-LHGRLgykptwrslLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
..
gi 359351306 230 QF 231
Cdd:TIGR02315 237 VL 238
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-228 |
2.37e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 117.39 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV-----DILGfdpLRTPLEVKR 80
Cdd:COG0410 3 MLEVENLHAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrfdgeDITG---LPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 RVGYLSDTVGFYDTMTAYENLDytarfLGLSAKERRERILGALQRM-----RLENRKNDKVHTFSHGMKQRLGLAEVLVK 155
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLL-----LGAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 156 NCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
20-226 |
4.65e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.39 E-value: 4.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 20 MLAVDDI-----------SLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKRRVGYLsdt 88
Cdd:COG3840 1 MLRLDDLtyrygdfplrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERPVSML--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 vgFYDT-----MTAYENLDytarfLGLSAK-----ERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCE 158
Cdd:COG3840 77 --FQENnlfphLTVAQNIG-----LGLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 159 IAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-246 |
5.01e-31 |
|
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: 123.20 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKR 80
Cdd:TIGR01257 1933 NKTDILRLNELTKVYsGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 RVGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIA 160
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 161 ILDEPTQGLDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELsEQQFGGRQIIELR 240
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL-KSKFGDGYIVTMK 2170
|
....*.
gi 359351306 241 VDSEKN 246
Cdd:TIGR01257 2171 IKSPKD 2176
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-226 |
5.04e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.01 E-value: 5.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRR 81
Cdd:PRK11300 1 MSQPLLSVSGLMMRFG-GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLS--DTVGFYDTMTAYENLDY-------TARFLGL--------SAKERRERILGALQRMRLENRKNDKVHTFSHGMK 144
Cdd:PRK11300 80 MGVVRtfQHVRLFREMTVIENLLVaqhqqlkTGLFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 145 QRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVA 224
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
..
gi 359351306 225 EL 226
Cdd:PRK11300 240 EI 241
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-230 |
5.60e-31 |
|
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: 122.17 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLR--TPLEVKRRVGY 84
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING-VDLSdlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LS-DTVGFYDTMtaYENLdytaRFLGLSAKErrERILGALQRMRLE---NRKNDKVHT--------FSHGMKQRLGLAEV 152
Cdd:COG4988 416 VPqNPYLFAGTI--RENL----RLGRPDASD--EELEAALEAAGLDefvAALPDGLDTplgeggrgLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 153 LVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-229 |
5.72e-31 |
|
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: 116.28 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 9 ISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKRRVGYLSDT 88
Cdd:cd03296 5 VRNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 VGFYDTMTAYEN----LDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDE 164
Cdd:cd03296 83 YALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 165 PTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-226 |
2.91e-30 |
|
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: 119.79 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLR---KQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEP----TSGSVDILGFDPLR 73
Cdd:COG4172 1 MMSMPLLSVEDLSvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 74 TPLEVKRRV-GylsDTVG--FYDTMTA-----------YENLdytARFLGLSAKERRERILGALQRMRL---ENRKNDKV 136
Cdd:COG4172 81 LSERELRRIrG---NRIAmiFQEPMTSlnplhtigkqiAEVL---RLHRGLSGAAARARALELLERVGIpdpERRLDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 137 HTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGK 216
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250
....*....|
gi 359351306 217 LLKNGTVAEL 226
Cdd:COG4172 235 IVEQGPTAEL 244
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-216 |
3.68e-30 |
|
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: 112.09 E-value: 3.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLR--TPLEVKRRVG 83
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRdlDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDtMTAYENLdytarflglsakerrerilgalqrmrlenrkndkvhtFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:cd03228 80 YVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDteHMTILLSSHQLEEVQSvCDRVGLFYRGK 216
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-229 |
3.90e-30 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 120.23 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTtilmLLGLL----EPTSGSVDILGFD----PLRTplE 77
Cdd:NF033858 1 VARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarKIQQGRVEVLGGDmadaRHRR--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 78 VKRRVGYLSDTVG--FYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLE---NRKNDKVhtfSHGMKQRLGLAEV 152
Cdd:NF033858 74 VCPRIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLApfaDRPAGKL---SGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 153 LVKNCEIAILDEPTQGLDPESVAEFLSLITSLR-DTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRaERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLAR 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-217 |
4.27e-30 |
|
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: 111.75 E-value: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtplevkRRVGYLS 86
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------KEVSFAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTvgfydtmtayenldyTARFLGLSAkerrerilgalqrmrlenrkndkVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03216 69 PR---------------DARRAGIAM-----------------------VYQLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 359351306 167 QGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-229 |
1.25e-29 |
|
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: 117.98 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRKQY---GKGML-AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPL-----RT 74
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWvdmtkPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 75 PLE---VKRRVGYLSDTVGFYDTMTAYENLDyTARFLGLSAKERRERILGALQRMRLENRKNDKV-----HTFSHGMKQR 146
Cdd:TIGR03269 357 PDGrgrAKRYIGILHQEYDLYPHRTVLDNLT-EAIGLELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 147 LGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
...
gi 359351306 227 SEQ 229
Cdd:TIGR03269 516 VEE 518
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-230 |
2.60e-29 |
|
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: 118.01 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLRT--PLEVKRRVG 83
Cdd:COG2274 474 IELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID-LRQidPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 Y-LSDTVGFYDTMtaYENLDYTARFLGLsakerrERILGALQR-------MRLENRKNDKV----HTFSHGMKQRLGLAE 151
Cdd:COG2274 553 VvLQDVFLFSGTI--RENITLGDPDATD------EEIIEAARLaglhdfiEALPMGYDTVVgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 152 VLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-278 |
3.41e-29 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 117.81 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 19 GMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLRTPLEVKRR-VGYLSDTVGFYDTMTA 97
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD-IETNLDAVRQsLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 98 YENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEF 177
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 178 LSLITSLRDTEhmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELsEQQFGGRQIIELrVDSEKNLAETFAGISEV 257
Cdd:TIGR01257 1101 WDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL-KNCFGTGFYLTL-VRKMKNIQSQRGGCEGT 1176
|
250 260
....*....|....*....|.
gi 359351306 258 TKVLPAGRQTWNLECMEDVRP 278
Cdd:TIGR01257 1177 CSCTSKGFSTRCPARVDEITP 1197
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-226 |
3.65e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.13 E-value: 3.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 21 LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTP----LEVKRR-VGYLSDTVGFYDTM 95
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKkIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 96 TAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVA 175
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 359351306 176 EFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-229 |
8.25e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.72 E-value: 8.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 17 GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTP--LEVKRRVGY--------LS 86
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlWDIRNKAGMvfqnpdnqIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLdytarflGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:PRK13633 100 ATIVEEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-239 |
1.37e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 114.73 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLEVKRRvGy 84
Cdd:COG1129 4 LLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvRFRSPRDAQAA-G- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 lsdtVGF-------YDTMTAYENLdytarFLG--------LSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGL 149
Cdd:COG1129 81 ----IAIihqelnlVPNLSVAENI-----FLGreprrgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTED 230
|
250
....*....|
gi 359351306 230 qfggrQIIEL 239
Cdd:COG1129 231 -----ELVRL 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-217 |
1.88e-28 |
|
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: 108.29 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRkqyGKGmlAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLE-VKRR 81
Cdd:cd03215 2 EPVLEVRGLS---VKG--AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvTRRSPRDaIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSD---TVGFYDTMTAYENLdytarflglsakerrerILGALqrmrlenrkndkvhtFSHGMKQRLGLAEVLVKNCE 158
Cdd:cd03215 77 IAYVPEdrkREGLVLDLSVAENI-----------------ALSSL---------------LSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 159 IAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-230 |
2.68e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 109.33 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMlAVDDISLTLNKGEIFGLLGPNGSGKtTTILMLLGLLE-PTSGSVDILG--FDPLRTP-----LEV 78
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGK-SSLLRVLNLLEmPRSGTLNIAGnhFDFSKTPsdkaiREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYLSDTVGFYDTMTAYENL-DYTARFLGLSAKERRERILGALQRMRLEnrknDKVHTF----SHGMKQRLGLAEVL 153
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLK----PYADRFplhlSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 154 VKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTeHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQ 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-198 |
5.18e-28 |
|
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: 107.44 E-value: 5.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYLSDTVGFYDTMTAYENLDYTA 105
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 106 RFLGlsaKERRErILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLItslr 185
Cdd:TIGR01189 99 AIHG---GAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL---- 170
|
170
....*....|....*..
gi 359351306 186 dTEHM----TILLSSHQ 198
Cdd:TIGR01189 171 -RAHLarggIVLLTTHQ 186
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-228 |
5.39e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.47 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYgKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPlEVKRRVGYL 85
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 166 TQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-228 |
9.30e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.81 E-value: 9.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKRRVGYL 85
Cdd:PRK09452 14 LVELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 166 TQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-221 |
1.78e-27 |
|
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: 106.57 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKRRVGYLS 86
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-258 |
1.92e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.80 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG--FDPLRTPLEVK 79
Cdd:PRK09700 1 MATPYISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 80 RRVGYLSDTVGFYDTMTAYENLDY----TARFLGLSA---KERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEV 152
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 153 LVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQqfg 232
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND--- 235
|
250 260
....*....|....*....|....*.
gi 359351306 233 grQIIELRVDSEknLAETFAGISEVT 258
Cdd:PRK09700 236 --DIVRLMVGRE--LQNRFNAMKENV 257
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-221 |
2.33e-27 |
|
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: 106.04 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDplRTPLEVKRR-VGYLSDTVGFYDTMTAYENLDy 103
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD--VTAAPPADRpVSMLFQENNLFAHLTVEQNVG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 104 tarfLGLSAK-----ERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFL 178
Cdd:cd03298 93 ----LGLSPGlkltaEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 359351306 179 SLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-227 |
4.13e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkgmlaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLE-VKRRVG 83
Cdd:COG1129 256 VLEVEGLSVGGV-----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvRIRSPRDaIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSD---TVGFYDTMTAYEN-----LDYTARFLGLSAKERRERILGALQRMRLE-NRKNDKVHTFSHGMKQRLGLAEVLV 154
Cdd:COG1129 331 YVPEdrkGEGLVLDLSIRENitlasLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 155 KNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLlkngtVAELS 227
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRILVMREGRI-----VGELD 477
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-225 |
4.34e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.35 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 9 ISHLRKQY---GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV-----DILGFDP--LRtplEV 78
Cdd:PRK11153 4 LKNISKVFpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqDLTALSEkeLR---KA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGY-------LSdtvgfydTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAE 151
Cdd:PRK11153 81 RRQIGMifqhfnlLS-------SRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 152 VLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-258 |
5.35e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.74 E-value: 5.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLEVKRRV 82
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 83 GYLsdtvgFYD------TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:PRK13647 82 GLV-----FQDpddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLrDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQFGGRQI 236
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAG 235
|
250 260
....*....|....*....|..
gi 359351306 237 IELRVdseknLAETFAGISEVT 258
Cdd:PRK13647 236 LRLPL-----VAQIFEDLPELG 252
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-221 |
6.27e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 105.07 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNkGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG---FD---PLRTPLEvKRRVGYLSDTVGFYDTMTAY 98
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDsrkKINLPPQ-QRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 99 ENLDYTARFLglSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFL 178
Cdd:cd03297 94 ENLAFGLKRK--RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 359351306 179 SLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-243 |
3.74e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 104.30 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGKG-MLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtpLEVKR 80
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG-------ITISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 R-VGYLSDTVGFydtmtAYENLDytARFLGLSA---------------KERRERILGALQRMRLENRKNDKVHTFSHGMK 144
Cdd:PRK13632 76 EnLKEIRKKIGI-----IFQNPD--NQFIGATVeddiafglenkkvppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 145 QRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVqSVCDRVGLFYRGKLLKNGTVA 224
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
250 260
....*....|....*....|
gi 359351306 225 ELseqqFGGRQIIEL-RVDS 243
Cdd:PRK13632 228 EI----LNNKEILEKaKIDS 243
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-229 |
3.95e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 12 LRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL-EVKRRVGYL---SD 87
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLVfqnPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGFydTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:PRK13652 89 DQIF--SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 168 GLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-230 |
5.42e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 5.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMlAVDDISLTLNKGEIFGLLGPNGSGKTTtILMLLGLLE-PTSGSVDILG--FDPLRTP-----LEV 78
Cdd:COG4161 3 IQLKNINCFYGSHQ-ALFDINLECPSGETLVLLGPSGAGKSS-LLRVLNLLEtPDSGQLNIAGhqFDFSQKPsekaiRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYLSDTVGFYDTMTAYENL-DYTARFLGLSAKERRERILGALQRMRLEnrknDKVHTF----SHGMKQRLGLAEVL 153
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLT----DKADRFplhlSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 154 VKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEhMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQ 232
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
6-227 |
5.89e-26 |
|
urea ABC transporter, ATP-binding protein UrtD; 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: 274568 [Multi-domain] Cd Length: 242 Bit Score: 103.02 E-value: 5.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLE--VKRRVG 83
Cdd:TIGR03411 2 ILYLEGLSVSFD-GFKALNDLSLYVDPGELRVIIGPNGAGKTTMMDVITGKTRPDEGSVLFGGTDLTGLPEHqiARAGIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYTAR---------FLGLSAKERrERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLV 154
Cdd:TIGR03411 81 RKFQKPTVFENLTVFENLELALPrdksvfaslFFRLSAEEK-DRIEEVLETIGLADEADRLAGLLSHGQKQWLEIGMLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 155 KNCEIAILDEPTQGLDPESVAEFLSLITSLrdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELS 227
Cdd:TIGR03411 160 QDPKLLLLDEPVAGMTDEETEKTAELLKSL--AGKHSVVVVEHDMEFVRSIADKVTVLHQGSVLAEGSLDQVQ 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-232 |
9.15e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.53 E-value: 9.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 16 YGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGF---DPLRTPlEVKRRVGYL-----SD 87
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQ-GIRKLVGIVfqnpeTQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGfydtMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:PRK13644 90 FVG----RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 168 GLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQsVCDRVGLFYRGKLLKNGT----VAELSEQQFG 232
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEpenvLSDVSLQTLG 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-226 |
1.01e-25 |
|
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: 106.69 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQY--GKGML--------AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLePTSGSV-----DILGFD 70
Cdd:COG4172 275 LLEARDLKVWFpiKRGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIrfdgqDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 71 -----PLRtplevkRRV--------GYLS------DTVGfydtmtayENLdyTARFLGLSAKERRERILGALQRMRLENR 131
Cdd:COG4172 354 rralrPLR------RRMqvvfqdpfGSLSprmtvgQIIA--------EGL--RVHGPGLSAAERRARVAEALEEVGLDPA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 132 KNDK-VHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDpESV-AEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRV 209
Cdd:COG4172 418 ARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVqAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRV 496
|
250
....*....|....*..
gi 359351306 210 GLFYRGKLLKNGTVAEL 226
Cdd:COG4172 497 MVMKDGKVVEQGPTEQV 513
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-227 |
1.10e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 102.50 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV-----DILGFDPLRTpl 76
Cdd:COG4674 6 MHGPILYVEDLTVSFD-GFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVlfggtDLTGLDEHEI-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 eVKRRVG--YLSDTVgfYDTMTAYENLD---------YTARFLGLSAkERRERILGALQRMRLENRKNDKVHTFSHGMKQ 145
Cdd:COG4674 83 -ARLGIGrkFQKPTV--FEELTVFENLElalkgdrgvFASLFARLTA-EERDRIEEVLETIGLTDKADRLAGLLSHGQKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 146 RLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:COG4674 159 WLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLA--GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDE 236
|
..
gi 359351306 226 LS 227
Cdd:COG4674 237 VQ 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-228 |
1.52e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.23 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 12 LRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLE-----PTSGSVDILG---FDPLRTPLEVKRRVG 83
Cdd:PRK14267 10 LRVYYGSNHV-IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGrniYSPDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYTARFLGL--SAKERRERILGALQRMRL----ENRKNDKVHTFSHGMKQRLGLAEVLVKNC 157
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 158 EIAILDEPTQGLDPESVAEFLSLITSLRDteHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-221 |
2.33e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 99.69 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYL 85
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTmTAYENLDytarflglsakeRRerilgalqrmrlenrkndkvhtFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:cd03247 81 NQRPYLFDT-TLRNNLG------------RR----------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 166 TQGLDPESVAEFLSLITSLrdTEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNG 221
Cdd:cd03247 126 TVGLDPITERQLLSLIFEV--LKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-221 |
2.76e-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: 100.74 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLRT--PLEVKRRVGYLS-DTVGFYDTMtaY 98
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD-IRQldPADLRRNIGYVPqDVTLFYGTL--R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 99 ENLDYTARFlglsAKErrERILGALQRMRLENRKNDKVHTF-----------SHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:cd03245 96 DNITLGAPL----ADD--ERILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 359351306 168 GLDPESVAEFLSLITSLrdTEHMTILLSSHQLeEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03245 170 AMDMNSEERLKERLRQL--LGDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-199 |
3.61e-25 |
|
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: 105.14 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL-EVKRRVGYL 85
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTmTAYENLdytaRFLGLSAKErrERILGALQRMRLEN---RKNDKVHT--------FSHGMKQRLGLAEVLV 154
Cdd:TIGR02868 415 AQDAHLFDT-TVRENL----RLARPDATD--EELWAALERVGLADwlrALPDGLDTvlgeggarLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 359351306 155 KNCEIAILDEPTQGLDPESVAEFLSLItsLRDTEHMTILLSSHQL 199
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-234 |
8.60e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.37 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLE-----PTSGSVDILGFDPLRTPL-EVK 79
Cdd:PRK14247 3 KIEIRDLKVSFGQVEV-LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDViELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 80 RRVGYLSDTVGFYDTMTAYENLDYTARF--LGLSAKERRERILGALQRMRL----ENRKNDKVHTFSHGMKQRLGLAEVL 153
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 154 VKNCEIAILDEPTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVA--------E 225
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELK--KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRevftnprhE 239
|
....*....
gi 359351306 226 LSEQQFGGR 234
Cdd:PRK14247 240 LTEKYVTGR 248
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-211 |
8.88e-25 |
|
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: 99.10 E-value: 8.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYLSDTVGFYDTMTAYENLDYTA 105
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 106 RFLGlsakerRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLR 185
Cdd:cd03231 99 ADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170 180
....*....|....*....|....*.
gi 359351306 186 DTEHMTILLSSHQLEEVQSVCDRVGL 211
Cdd:cd03231 173 ARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-221 |
1.30e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 98.39 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEP--TSGSVDILGFDplRTPLEVKRRVGY-LSDTVgFYDTMTAYE 99
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRP--LDKRSFRKIIGYvPQDDI-LHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 100 NLDYTARFLGLSAKERRerilgalqrmrlenrkndkvhtfshgmkqRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLS 179
Cdd:cd03213 102 TLMFAAKLRGLSGGERK-----------------------------RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 359351306 180 LITSLRDTeHMTILLSSHQL-EEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03213 153 LLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-198 |
1.44e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.41 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPlrTPLEVKRRVGYLSDTVGFYDTMTAYENLDYT 104
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 105 ARFLGlsakERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLItsl 184
Cdd:PRK13539 98 AAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI--- 170
|
170
....*....|....*...
gi 359351306 185 rdTEHM----TILLSSHQ 198
Cdd:PRK13539 171 --RAHLaqggIVIAATHI 186
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-209 |
2.84e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 99.03 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilgfdplRTPlevKRRVGYLSDTVgfydtmtayeNLDYT 104
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNG---KLRIGYVPQKL----------YLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 105 -----ARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLS 179
Cdd:PRK09544 82 lpltvNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|
gi 359351306 180 LITSLRDTEHMTILLSSHQLEEVQSVCDRV 209
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-229 |
4.04e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEvKR 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 RVGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIA 160
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 161 ILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-226 |
4.36e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQYGKGMlAVDDISLTLNKGEIFGLLGPNGSGKTTTILML--LGLLEP---TSGSVDILG---FDPLRT 74
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGhniYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 75 PLEVKRRVGYLSDTVGFYdTMTAYENLDYTARFLGLSAKER-RERILGALQRMRLENRKNDKVHT----FSHGMKQRLGL 149
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDteHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-202 |
4.92e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.53 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDI-----LGFDPLRT------PLEVKRRVgylsdTVG 90
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaggarVAYVPQRSevpdslPLTVRDLV-----AMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 91 FYdtmtayenldytaRFLGLSAKERRE---RILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:NF040873 82 RW-------------ARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*
gi 359351306 168 GLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEV 202
Cdd:NF040873 149 GLDAESRERIIALLAEEHA-RGATVVVVTHDLELV 182
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-226 |
1.10e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG------------- 68
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEV-LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 69 --FDPLRTPLeVKRRVGYLSDTVGFYDTMTAYEN-LDYTARFLGLSAKERRERILGALQRMRLENRKNDK--VHtFSHGM 143
Cdd:PRK10619 80 kvADKNQLRL-LRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKypVH-LSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 144 KQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTV 223
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
...
gi 359351306 224 AEL 226
Cdd:PRK10619 237 EQL 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-217 |
1.71e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 5 QVLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGfdplrtpleVKRRVGY 84
Cdd:COG0488 314 KVLELEGLSKSYGDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLG---------ETVKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LS-DTVGFYDTMTAYENLDYTARflglsaKERRERILGALQRMRL-ENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAIL 162
Cdd:COG0488 383 FDqHQEELDPDKTVLDELRDGAP------GGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 163 DEPTQGLDPESVAeflSLITSLRDTEHmTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:COG0488 457 DEPTNHLDIETLE---ALEEALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-198 |
1.98e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 95.26 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 24 DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRtplevKRRVGYLSDTV------GFYDTMTA 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-EPIR-----RQRDEYHQDLLylghqpGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 98 YENLDYtarFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEF 177
Cdd:PRK13538 92 LENLRF---YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170 180
....*....|....*....|...
gi 359351306 178 LSLItsLRDTEH--MTIlLSSHQ 198
Cdd:PRK13538 169 EALL--AQHAEQggMVI-LTTHQ 188
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-242 |
2.40e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.11 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPL--RTPLEVKRRVGYL-------------SD 87
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLteENVWDIRHKIGMVfqnpdnqfvgatvED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGFydtmtAYENLdytarflGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:PRK13650 102 DVAF-----GLENK-------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 168 GLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVqSVCDRVglfyrgKLLKNGTVAELS--EQQFG-GRQIIELRVD 242
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRV------LVMKNGQVESTStpRELFSrGNDLLQLGLD 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-222 |
3.39e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.85 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 9 ISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRtpLEVK-RRVGYLSD 87
Cdd:PRK10851 5 IANIKKSFGRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARdRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGFYDTMTAYENLDYtarflGLSAKERRER------------ILGALQRMRLENRKNDKVhtfSHGMKQRLGLAEVLVK 155
Cdd:PRK10851 82 HYALFRHMTVFDNIAF-----GLTVLPRRERpnaaaikakvtqLLEMVQLAHLADRYPAQL---SGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 156 NCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGT 222
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-243 |
4.01e-23 |
|
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: 97.86 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 11 HLRKQYGKGMLAVDdisLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG---FD---PLRTPLEvKRRVGY 84
Cdd:COG4148 6 DFRLRRGGFTLDVD---FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDsarGIFLPPH-RRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LsdtvgFYDT-----MTAYENLDYTARFLGlsAKERRERILGALQRMRLE---NRkndKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:COG4148 82 V-----FQEArlfphLSVRGNLLYGRKRAP--RAERRISFDEVVELLGIGhllDR---RPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL-----SEQQF 231
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVlsrpdLLPLA 231
|
250
....*....|....*
gi 359351306 232 GGRQ---IIELRVDS 243
Cdd:COG4148 232 GGEEagsVLEATVAA 246
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
12-226 |
4.77e-23 |
|
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: 97.49 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 12 LRKQYGKGMLavdDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG---FDP---LRTPLEvKRRVGYL 85
Cdd:TIGR02142 5 FSKRLGDFSL---DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSrkgIFLPPE-KRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGFYDTMTAYENLDYTARFLglSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRA--RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 166 TQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-229 |
7.33e-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: 94.60 E-value: 7.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 16 YGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKR-RVGY-LSDTVGFYD 93
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRsMIGVvLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 94 TMtaYENLdytaRFLGLSAKERRERILGALQR-----MRLEN----RKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDE 164
Cdd:cd03254 92 TI--MENI----RLGRPNATDEEVIEAAKEAGahdfiMKLPNgydtVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 165 PTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAK 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
9.07e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.20 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSvdILGFDPLRTP---L 76
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE--IFYNNQAITDdnfE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 EVKRRVG---------YLSDTVGfYDTMTAYENLdytarflGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRL 147
Cdd:PRK13648 80 KLRKHIGivfqnpdnqFVGSIVK-YDVAFGLENH-------AVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 148 GLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAELS 227
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
...
gi 359351306 228 EQQ 230
Cdd:PRK13648 231 DHA 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-234 |
1.25e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.93 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 16 YGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLR--TPLEVKRRVGYLS-DTVGFY 92
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD-IRdlTLESLRRQIGVVPqDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 93 DtmTAYENLDYtarflglsAKER--RERILGALQR-------MRLEnrknDKVHT--------FSHGMKQRLGLAEVLVK 155
Cdd:COG1132 428 G--TIRENIRY--------GRPDatDEEVEEAAKAaqahefiEALP----DGYDTvvgergvnLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 156 NCEIAILDEPTQGLDPESVAEflsLITSLRD-TEHMTILLSSHQLEEVQSvCDRVGLFYRGK---------LL-KNGTVA 224
Cdd:COG1132 494 DPPILILDEATSALDTETEAL---IQEALERlMKGRTTIVIAHRLSTIRN-ADRILVLDDGRiveqgtheeLLaRGGLYA 569
|
250
....*....|
gi 359351306 225 ELSEQQFGGR 234
Cdd:COG1132 570 RLYRLQFGEE 579
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-231 |
1.32e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-------------------------PLRTPL 76
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrfkKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 EVKRRVGylsdtVGF----YDTM--TAYENLDYTARFLGLSAKERRERILGALQRMRL-ENRKNDKVHTFSHGMKQRLGL 149
Cdd:PRK13651 102 EIRRRVG-----VVFqfaeYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG-TVAELSE 228
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGdTYDILSD 255
|
...
gi 359351306 229 QQF 231
Cdd:PRK13651 256 NKF 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-197 |
1.48e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 9 ISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtplevKRRVGYLSDT 88
Cdd:COG0488 1 LENLSKSFGGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 VGFYDTMTAYENL--------------------------------DYTARFLGLSAKERRERILGALQRMRLENRKND-K 135
Cdd:COG0488 70 PPLDDDLTVLDTVldgdaelraleaeleeleaklaepdedlerlaELQEEFEALGGWEAEARAEEILSGLGFPEEDLDrP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 136 VHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVA---EFLSlitslrdTEHMTILLSSH 197
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwleEFLK-------NYPGTVLVVSH 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-209 |
3.49e-22 |
|
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: 96.59 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLR--TPLEVKRRVGY 84
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG-VPLAdaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSDTVGFYDTMTAyENLdytaRFLGLSAKErrERILGALQR---MRLENRKNDKVHT--------FSHGMKQRLGLAEVL 153
Cdd:TIGR02857 401 VPQHPFLFAGTIA-ENI----RLARPDASD--AEIREALERaglDEFVAALPQGLDTpigeggagLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 154 VKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEhmTILLSSHQLeEVQSVCDRV 209
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRL-ALAALADRI 526
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
5.47e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.15 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQYGKG----MLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV---------DIL 67
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 68 GFDPLRTPLEVK-RRVGYLSDTVGFYDTMTAYENLDYTAR----F----LGLSAKERRERILGALQRMRLENRKNDKV-H 137
Cdd:PRK13631 96 NHELITNPYSKKiKNFKELRRRVSMVFQFPEYQLFKDTIEkdimFgpvaLGVKKSEAKKLAKFYLNKMGLDDSYLERSpF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 138 TFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
....*....
gi 359351306 218 LKNGTVAEL 226
Cdd:PRK13631 255 LKTGTPYEI 263
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-231 |
5.56e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.15 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRK--QYGKGMLAVDdisLTLNKGEIFGLLGPNGSGKTTTILMLLGLL--EPTSGS-VDILGFDPLRTP--- 75
Cdd:PRK09984 2 QTIIRVEKLAKtfNQHQALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREGrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 76 ---LEVKRRVGYLSDTVGFYDTMTAYENLDYTArfLGLS----------AKERRERILGALQRMRLENRKNDKVHTFSHG 142
Cdd:PRK09984 79 rdiRKSRANTGYIFQQFNLVNRLSVLENVLIGA--LGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 143 MKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGT 222
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
....*....
gi 359351306 223 VAELSEQQF 231
Cdd:PRK09984 237 SQQFDNERF 245
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-221 |
1.19e-21 |
|
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: 91.18 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 13 RKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEP---TSGsvDILGFDPLRTPLEVKRRVGYLSDTV 89
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSG--QILFNGQPRKPDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 90 GFYDTMTAYENLDYTARFLG---LSAKERRERI-LGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRLprkSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 166 TQGLDPESVaefLSLITSLRDTEH--MTILLSSHQ-LEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03234 171 TSGLDSFTA---LNLVSTLSQLARrnRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-226 |
1.42e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.06 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLA--------VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrTPLEV 78
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG-----EPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGY--LSDTVG--FYDTMTAYeNLDYTAR---------FLGLSAKERRERILGALQRMRLENRKNDKV-HTFSHGMK 144
Cdd:PRK10419 79 LNRAQRkaFRRDIQmvFQDSISAV-NPRKTVReiireplrhLLSLDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 145 QRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVA 224
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVG 237
|
..
gi 359351306 225 EL 226
Cdd:PRK10419 238 DK 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-240 |
1.46e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLePTSGSVDilgFD--PL-----RTPLEVKRRVgylsdTVGFYDT 94
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIW---FDgqPLhnlnrRQLLPVRHRI-----QVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 95 MTAYEN----LDYTARFL-----GLSAKERRERILGALQRMRLENRKNDKVHT-FSHGMKQRLGLAEVLVKNCEIAILDE 164
Cdd:PRK15134 372 NSSLNPrlnvLQIIEEGLrvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 165 PTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL--SEQQFGGRQIIELR 240
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVfaAPQQEYTRQLLALS 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-226 |
1.48e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPL----RTPLEVKRRVGYL---SDTVGFYDTMTAy 98
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLdyskRGLLALRQQVATVfqdPEQQIFYTDIDS- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 99 eNLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFL 178
Cdd:PRK13638 98 -DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 359351306 179 SLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK13638 177 AIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-229 |
1.50e-21 |
|
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: 91.14 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLR--TPLEVKRRVG 83
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD-VRdyTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLS-DTVGFYDTMtaYENLDYTARflglsaKERRERILGALQR---MRLENRKNDKVHTF--------SHGMKQRLGLAE 151
Cdd:cd03251 80 LVSqDVFLFNDTV--AENIAYGRP------GATREEVEEAARAanaHEFIMELPEGYDTVigergvklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 152 VLVKNCEIAILDEPTQGLDPES---VAEFLSlitslRDTEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSE 228
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESerlVQAALE-----RLMKNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLA 225
|
.
gi 359351306 229 Q 229
Cdd:cd03251 226 Q 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-209 |
2.09e-21 |
|
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: 90.57 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRK------QYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGS---------VDILGFD 70
Cdd:COG4778 4 LLEVENLSKtftlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 71 PlRTPLEVKRR-VGYLSDtvgFYDTM---TAyenLDYTARFL---GLSAKERRERILGALQRMRLENRKND-KVHTFSHG 142
Cdd:COG4778 84 P-REILALRRRtIGYVSQ---FLRVIprvSA---LDVVAEPLlerGVDREEARARARELLARLNLPERLWDlPPATFSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 143 MKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRV 209
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRV 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-225 |
2.20e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLR--TPLEVKRRVG 83
Cdd:PRK13548 2 MLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-RPLAdwSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YL--SDTVGFydtmtayenlDYTAR--------FLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVL 153
Cdd:PRK13548 80 VLpqHSSLSF----------PFTVEevvamgraPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 154 vknCEIA---------ILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVA 224
Cdd:PRK13548 150 ---AQLWepdgpprwlLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
.
gi 359351306 225 E 225
Cdd:PRK13548 227 E 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-225 |
2.48e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.84 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLR--TPLEVKRRVGY 84
Cdd:PRK11231 3 LRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD-KPISmlSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSD--------TVgfyDTMTAYENLDYTARFLGLSAKErRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:PRK11231 81 LPQhhltpegiTV---RELVAYGRSPWLSLWGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-232 |
2.61e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.94 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLR-TPLEVKRR- 81
Cdd:COG3845 255 EVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlSPRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSD------TVGfydTMTAYENL---DYT----ARFLGLSAKERRERILGALQRM--RLENRkNDKVHTFSHGMKQR 146
Cdd:COG3845 335 VAYIPEdrlgrgLVP---DMSVAENLilgRYRrppfSRGGFLDRKAIRAFAEELIEEFdvRTPGP-DTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 147 LGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
....*.
gi 359351306 227 SEQQFG 232
Cdd:COG3845 490 TREEIG 495
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-226 |
2.62e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.48 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGK---GMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEP---TSGSVDILGFDPLRTP 75
Cdd:PRK09473 8 QADALLDVKDLRVTFSTpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 76 LEVKRRVGYLSDTVGFYDTMTA---YENL-DYTARFL----GLSAKERRE---RILGALqRMRlENRKNDKV--HTFSHG 142
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDPMTSlnpYMRVgEQLMEVLmlhkGMSKAEAFEesvRMLDAV-KMP-EARKRMKMypHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 143 MKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGT 222
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
....
gi 359351306 223 VAEL 226
Cdd:PRK09473 246 ARDV 249
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-226 |
3.29e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.03 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 20 MLAVDDI-----------SLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPlEVKRRVGYLSDT 88
Cdd:PRK10771 1 MLKLTDItwlyhhlpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-PSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 VGFYDTMTAYENLDytarfLGL--------SAKERRERILgalQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIA 160
Cdd:PRK10771 80 NNLFSHLTVAQNIG-----LGLnpglklnaAQREKLHAIA---RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 161 ILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-226 |
3.53e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.15 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 14 KQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTtILMLLGLLEP-TSGSVDILGF---DPLRTPLEVKRRVGYLSDTV 89
Cdd:PRK09493 9 KHFGPTQV-LHNIDLNIDQGEVVVIIGPSGSGKST-LLRCINKLEEiTSGDLIVDGLkvnDPKVDERLIRQEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 90 GFYDTMTAYENLDY-TARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQG 168
Cdd:PRK09493 87 YLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 169 LDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
7-209 |
4.01e-21 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 89.76 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY------GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGS---------VDILGFDP 71
Cdd:TIGR02324 2 LEVEDLSKTFtlhqqgGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRilvrhegawVDLAQASP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 72 lRTPLEVKRR-VGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKND-KVHTFSHGMKQRLGL 149
Cdd:TIGR02324 82 -REVLEVRRKtIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLNIPERLWHlPPATFSGGEQQRVNI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRV 209
Cdd:TIGR02324 161 ARGFIADYPILLLDEPTASLDAANRQVVVELIAEAK-ARGAALIGIFHDEEVRELVADRV 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-201 |
4.34e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRTPlEVKRRVGYLS 86
Cdd:PRK11248 2 LQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-KPVEGP-GAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DtvGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:PRK11248 79 E--GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEE 201
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEE 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-238 |
4.87e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.19 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 9 ISHLRKQYgKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTtILMLLGLLE-PTSGSVDI--LGFDPLRTPLEVKRRVGYL 85
Cdd:PRK11264 6 VKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTT-LLRCINLLEqPEAGTIRVgdITIDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 SDTVGF-------YDTMTAYENLDYTARFLGLSAKER---RERILgaLQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVK 155
Cdd:PRK11264 84 RQHVGFvfqnfnlFPHRTVLENIIEGPVIVKGEPKEEataRAREL--LAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 156 NCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL--SEQQFGG 233
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALfaDPQQPRT 240
|
....*
gi 359351306 234 RQIIE 238
Cdd:PRK11264 241 RQFLE 245
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-230 |
7.89e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPlrTP-------LEVKRRVGYL---SDTVGFY 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI--TPetgnknlKKLRKKVSLVfqfPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 93 DTMtaYENLDYTARFLGLSAKERRERILGALQRMRL-ENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDP 171
Cdd:PRK13641 101 NTV--LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 172 ESVAEFLSLITSLRDTEHmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-226 |
1.09e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.34 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRkQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLE------PTSGSVDILGFDPLRT- 74
Cdd:PRK14246 6 SAEDVFNISRLY-LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQId 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 75 PLEVKRRVGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRM-----RLENRKNDKVHTFSHGMKQRLGL 149
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKvglwkEVYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDteHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-233 |
1.51e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.17 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRTPLEvKR 80
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG-QPTRQALQ-KN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 RVGYL--SDTVGfYDTMTAYENLDYTARF-----LGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVL 153
Cdd:PRK15056 79 LVAYVpqSEEVD-WSFPVLVEDVVMMGRYghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 154 VKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVgLFYRGKLLKNGT-----VAELSE 228
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPtettfTAENLE 235
|
....*
gi 359351306 229 QQFGG 233
Cdd:PRK15056 236 LAFSG 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-225 |
1.76e-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: 87.93 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 21 LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKR-RVGYLS-DTVGFYDTMTay 98
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRsRISIIPqDPVLFSGTIR-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 99 ENLDytarFLGLSAKerrERILGALQRMRLENR------KNDKVHT-----FSHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:cd03244 96 SNLD----PFGEYSD---EELWQALERVGLKEFveslpgGLDTVVEeggenLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 168 GLDPESVAEFLSLI-TSLRDTehmTILLSSHQLEEVQSvCDRVglfyrgKLLKNGTVAE 225
Cdd:cd03244 169 SVDPETDALIQKTIrEAFKDC---TVLTIAHRLDTIID-SDRI------LVLDKGRVVE 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-226 |
1.87e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.80 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLE-PTSGSVDILGFD--PLRTPLEVKRRvgylsDTVG------FY 92
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLEFNgqDLQRISEKERR-----NLVGaevamiFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 93 DTMTAYeNLDYTARFL---------GLSAKERRERILGALQRMRL---ENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIA 160
Cdd:PRK11022 97 DPMTSL-NPCYTVGFQimeaikvhqGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 161 ILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-236 |
3.20e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.79 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILmllglleptsgSVDILGFDPLRTPLE----- 77
Cdd:NF000106 10 ARNAVEVRGLVKHFGE-VKAVDGVDLDVREGTVLGVLGP*GAA**RGAL-----------PAHV*GPDAGRRPWRf*twc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 78 VKRRVgyLSDTVGFY--------DTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGL 149
Cdd:NF000106 78 ANRRA--LRRTIG*Hrpvr*grrESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSL-RDTEhmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELsE 228
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGA--TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL-K 232
|
....*...
gi 359351306 229 QQFGGRQI 236
Cdd:NF000106 233 TKVGGRTL 240
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-220 |
4.26e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.55 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY--GKGMLAV-DDISLTLNKGEIFGLLGPNGSGKTTtiLM-LLGLLE-PTSGSVDILGFDPL---RTPLEV 78
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVEVlKGISLDIYAGEMVAIVGASGSGKST--LMnILGCLDkPTSGTYRVAGQDVAtldADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRR--VGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:PRK10535 83 LRRehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLRDTEHmTILLSSHQlEEVQSVCDRVGLFYRGKLLKN 220
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHD-PQVAAQAERVIEIRDGEIVRN 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-226 |
6.93e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.46 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 5 QVLSISHLRKQYGK--GMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDIlgfDPLRTPLE----V 78
Cdd:PRK13642 3 KILEVENLVFKYEKesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI---DGELLTAEnvwnL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYL-SDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNC 157
Cdd:PRK13642 80 RRKIGMVfQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 158 EIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-209 |
1.36e-19 |
|
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: 83.27 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtplevKRRVGYLS 86
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 dtvgfydtmtayenldytarflglsakerrerilgalQrmrlenrkndkvhtFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:cd03221 70 -------------------------------------Q--------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 359351306 167 QGLDPESVAeflSLITSLRDTEHmTILLSSHQLEEVQSVCDRV 209
Cdd:cd03221 99 NHLDLESIE---ALEEALKEYPG-TVILVSHDRYFLDQVATKI 137
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-226 |
1.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.37 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD--------PLRTpleVKRRVGYL---SDTVG 90
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkYIRP---VRKRIGMVfqfPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 91 FYDTMTayENLDYTARFLGLSAKERRERILGALQRMRLE-NRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGL 169
Cdd:PRK13646 99 FEDTVE--REIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 170 DPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-226 |
2.10e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.30 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 19 GMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSG---SVDIL----GFDPLRTPLEVKRRVGYLSDTVGF 91
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrySGDVLlggrSIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 92 YdTMTAYENLDYTARFLGL-SAKERRERILGALQRMRL----ENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:PRK14271 113 F-PMSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 167 QGLDPESVAEFLSLITSLRDteHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-221 |
2.25e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.75 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL---- 76
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYG-PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyals 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 EVKRRvgYLSDT----V------GFYDTMTAYENLdyTARFLGLSAK---ERRERILGALQRMRLE-NRKNDKVHTFSHG 142
Cdd:PRK11701 80 EAERR--RLLRTewgfVhqhprdGLRMQVSAGGNI--GERLMAVGARhygDIRATAGDWLERVEIDaARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 143 MKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-259 |
2.80e-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: 87.94 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 18 KGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGL--LEPTSGS-------------VDILGFDPLRTPL------ 76
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhvalcekcgyVERPSKVGEPCPVcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 ---------------EVKRRVG-YLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFS 140
Cdd:TIGR03269 91 peevdfwnlsdklrrRIRKRIAiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 141 HGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKN 220
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 359351306 221 GTVAELSEQQFggRQIIELRVDSEKNLAETFAGISEVTK 259
Cdd:TIGR03269 251 GTPDEVVAVFM--EGVSEVEKECEVEVGEPIIKVRNVSK 287
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-236 |
2.94e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 19 GMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG----FDPLRTPLEVKRRVGYlsDTVGFYDT 94
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrFASTTAALAAGVAIIY--QELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 95 MTAYENLdytarFLG--------LSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:PRK11288 94 MTVAENL-----YLGqlphkggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 167 QGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKN-GTVAELSE----QQFGGRQI 236
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRA-EGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRdqlvQAMVGREI 242
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-226 |
4.52e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPL--RTPLEVKRRVGY 84
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-DDVeaLSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSD--TVGF-YDTMTAYE--NLDYTARFLGLSAKERR--ERilgALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNC 157
Cdd:PRK09536 82 VPQdtSLSFeFDVRQVVEmgRTPHRSRFDTWTETDRAavER---AMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 158 EIAILDEPTQGLDPESVAEFLSLITSLRDTEHmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-229 |
4.85e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDIlgFDPLRTPLEVKRRVGYLSDTVG----FYDTM-- 95
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV--GDIVVSSTSKQKEIKPVRKKVGvvfqFPESQlf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 96 --TAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKV-HTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPE 172
Cdd:PRK13643 99 eeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 173 SVAEFLSLITSLRDTEHmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-229 |
6.97e-19 |
|
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: 87.08 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 17 GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLR--TPLEVKRRVGYLSDTVGFYDT 94
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG-HDLAdyTLASLRRQVALVSQDVVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 95 mTAYENLDYTARflGLSAKERRERILGALQRMRLENRKNDKVHT--------FSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:TIGR02203 421 -TIANNIAYGRT--EQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 167 QGLDPESvaEFLSLITSLRDTEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:TIGR02203 498 SALDNES--ERLVQAALERLMQGRTTLVIAHRLSTIEKA-DRIVVMDDGRIVERGTHNELLAR 557
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-223 |
1.33e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD--PLRTPLEVKRRVG 83
Cdd:PRK11614 5 MLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YLSDTVGFYDTMTAYENLDYTARFLGLSA-KERRERILGALQrmRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAIL 162
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 163 DEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDrvglfyRGKLLKNGTV 223
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLAD------RGYVLENGHV 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-217 |
1.42e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.49 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLRT--PLEVKRRVGYL-SDTVGFYDTMtaye 99
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD-ISQwdPNELGDHVGYLpQDDELFSGSI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 100 nldytarflglsakerRERILgalqrmrlenrkndkvhtfSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLS 179
Cdd:cd03246 93 ----------------AENIL-------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 359351306 180 LITSLRdTEHMTILLSSHQLEEVQSvCDRVGLFYRGKL 217
Cdd:cd03246 138 AIAALK-AAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-230 |
2.23e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrTPLE------VKRRVGYLS-DTVGFYDTMTa 97
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-----VPLVqydhhyLHRQVALVGqEPVLFSGSVR- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 98 yENLDYtarflGLSAKERrERILGALQR-------MRLENRKNDKV----HTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:TIGR00958 573 -ENIAY-----GLTDTPD-EEIMAAAKAanahdfiMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 167 QGLDPESVAeflsLITSLRDTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-217 |
2.34e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLE-VKRRVGYLSDT---VGFYDTMTA 97
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPLDaVKKGMAYITESrrdNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 98 YENLDyTARFLGLSA--------KERRERILGALQRMRLE---NRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:PRK09700 359 AQNMA-ISRSLKDGGykgamglfHEVDEQRTAENQRELLAlkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 359351306 167 QGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
3.47e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.39 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTtilmLL----GL--LEP---TSGSVDILG---F 69
Cdd:COG1117 7 TLEPKIEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKST----LLrclnRMndLIPgarVEGEILLDGediY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 70 DPLRTPLEVKRRVGYLSDT-VGFydTMTAYENLDYTARFLGLSAK-ERRERILGALQRMRL----ENRKNDKVHTFSHGM 143
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKpNPF--PKSIYDNVAYGLRLHGIKSKsELDEIVEESLRKAALwdevKDRLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 144 KQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-228 |
3.99e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.71 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEP---TSGSVDILGfDPLRTPlEVKRRVGYLSDTVGFYDTMTAYENL 101
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG-MPIDAK-EMRAISAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 102 DYTARF-LG--LSAKERRERILGALQRMRLENRKN------DKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPE 172
Cdd:TIGR00955 121 MFQAHLrMPrrVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 173 SVAEFLSLITSLRdTEHMTILLSSHQ-LEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:TIGR00955 201 MAYSVVQVLKGLA-QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-226 |
4.29e-18 |
|
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: 81.51 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 10 SHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLE-VKRRVGYL-SD 87
Cdd:cd03253 4 ENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDsLRRAIGVVpQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGFYDTMtaYENLDYtARflgLSAKErrERILGALQR-------MRLENRKNDKVH----TFSHGMKQRLGLAEVLVKN 156
Cdd:cd03253 84 TVLFNDTI--GYNIRY-GR---PDATD--EEVIEAAKAaqihdkiMRFPDGYDTIVGerglKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLrdTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-226 |
4.90e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLR---KQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLE 77
Cdd:PRK10261 7 LDARDVLAVENLNiafMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 78 V----------KRRVGYLSDTVGFYDTMTAYENL----DYTARFLGLSAKERRERILGALQRMRLENRKNDKV------- 136
Cdd:PRK10261 87 VielseqsaaqMRHVRGADMAMIFQEPMTSLNPVftvgEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilsryp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 137 HTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGK 216
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250
....*....|
gi 359351306 217 LLKNGTVAEL 226
Cdd:PRK10261 247 AVETGSVEQI 256
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-229 |
6.97e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.65 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 20 MLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEP----TSGSVDILGFDPLRTPLEVKRRV------------- 82
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIigreiamifqeps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 83 GYL--SDTVGfYDTMTAYENLDYTARFLGLsAKERRERILGALQRMRLENRK---NDKVHTFSHGMKQRLGLAEVLVKNC 157
Cdd:COG4170 100 SCLdpSAKIG-DQLIEAIPSWTFKGKWWQR-FKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 158 EIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-222 |
1.47e-17 |
|
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: 80.53 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 29 TLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKrrvgylSDTvgfydTMTAYENLDYTARFL 108
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIK------ADY-----EGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 109 GLSAKERRErILGALQRMRLENRkndKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTE 188
Cdd:cd03237 90 YTHPYFKTE-IAKPLQIEQILDR---EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180 190
....*....|....*....|....*....|....
gi 359351306 189 HMTILLSSHQLEEVQSVCDRVGLFyRGKLLKNGT 222
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGV 198
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-226 |
1.52e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 81.55 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQY--GKGML-------AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL 76
Cdd:PRK11308 5 LLQAIDLKKHYpvKRGLFkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 77 EV----KRRVG------YLS----DTVGFydtmTAYENLDYTARflgLSAKERRERILGALQRMRLENRKNDKV-HTFSH 141
Cdd:PRK11308 85 EAqkllRQKIQivfqnpYGSlnprKKVGQ----ILEEPLLINTS---LSAAERREKALAMMAKVGLRPEHYDRYpHMFSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 142 GMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
....*
gi 359351306 222 TVAEL 226
Cdd:PRK11308 238 TKEQI 242
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-226 |
1.95e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQyGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEP----TSGSVDILGfdplrTPLEV 78
Cdd:PRK10418 1 MPQQIELRNIALQ-AAQPL-VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDG-----KPVAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVGYLSDTV------GFYDTMTAYENLDYTARFLGLSAKERreRILGALQRMRLENRKN-DKVHTF--SHGMKQRLGL 149
Cdd:PRK10418 74 CALRGRKIATImqnprsAFNPLHTMHTHARETCLALGKPADDA--TLTAALEAVGLENAARvLKLYPFemSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 150 AEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-230 |
1.95e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.58 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 24 DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGsvDILgFDPLRTP-------LEVKRRVGYLSDTVGFYDTMT 96
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHG--EIL-FDGENIPamsrsrlYTVRKRMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 97 AYENLDYTAR-FLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVA 175
Cdd:PRK11831 101 VFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 176 EFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-226 |
1.99e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.45 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLR---KQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLePTSGSV----DIL--GFDPL 72
Cdd:PRK15134 1 MTQPLLAIENLSvafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSPPVVypsgDIRfhGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 73 RTPLEVKRRVGYLSDTVGFYDTMTAYENLDYTARFL--------GLSAKERRERILGALQRMRLEN---RKNDKVHTFSH 141
Cdd:PRK15134 80 HASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLyevlslhrGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 142 GMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
....*
gi 359351306 222 TVAEL 226
Cdd:PRK15134 240 RAATL 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-237 |
2.37e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 8 SISHLRKQ-----YGKGMLAvDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLR-TPLEVKRR 81
Cdd:PRK10253 4 SVARLRGEqltlgYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSDTVGFYDTMTAYEnLDYTARF-----LGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKN 156
Cdd:PRK10253 83 IGLLAQNATTPGDITVQE-LVARGRYphqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 157 CEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGT-----VAELSEQQF 231
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGApkeivTAELIERIY 241
|
....*.
gi 359351306 232 GGRQII 237
Cdd:PRK10253 242 GLRCMI 247
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-230 |
2.48e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRTPLEVKRRVGYLSDTVG----------F 91
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDYAIPANLKKIKEVKRLRKEIGlvfqfpeyqlF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 92 YDTMTayENLDYTARFLGLSAKERRERILGALQRMRL-ENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLD 170
Cdd:PRK13645 105 QETIE--KDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 171 PESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQ 242
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
2.52e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.44 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQYGKG---MLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRTPLE 77
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVG-QPLHQMDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 78 VKR------RVGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAE 151
Cdd:PRK10584 80 EARaklrakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 152 VLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQlEEVQSVCDRVGLFYRGKL 217
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-229 |
3.33e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.86 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLrtplevkrrvgyLSDTVGFYDTMTAYENL 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL------------IAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 102 DYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLI 181
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 359351306 182 TSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:PRK13545 187 NEFKE-QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-217 |
3.61e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRTPLEVKR------ 80
Cdd:PRK11247 13 LLLNAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRlmfqda 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 ------RVgylSDTVGfydtmtayenldytarfLGLSAKeRRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLV 154
Cdd:PRK11247 91 rllpwkKV---IDNVG-----------------LGLKGQ-WRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 155 KNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-226 |
4.12e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRT--PLEVKRRVGYLSDTVGFYDTMTAYEnLDY 103
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESwsSKAFARKVAYLPQQLPAAEGMTVRE-LVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 104 TARF-----LGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFL 178
Cdd:PRK10575 108 IGRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 359351306 179 SLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK10575 188 ALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-226 |
4.38e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.52 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 15 QYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLRTPLEVKRRVGYLSDTVGFYDT 94
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD-LLGMKDDEWRAVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 95 -------MTAYENLDYTAR--FLGLSAKERRERILGALQRMRL-ENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDE 164
Cdd:PRK15079 108 laslnprMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 165 PTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-200 |
4.40e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.36 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKG----MLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPlEVKR-- 80
Cdd:COG1101 2 LELKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 ---RVgylsdtvgFYD-------TMTAYENLDYTAR-------FLGLSAKER---RERIlgALQRMRLENRKNDKVHTFS 140
Cdd:COG1101 81 yigRV--------FQDpmmgtapSMTIEENLALAYRrgkrrglRRGLTKKRRelfRELL--ATLGLGLENRLDTKVGLLS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 141 HGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLE 200
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-232 |
4.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDIlgFDPLRTPLEVKRRVGYLSDTVG----FYDTM-- 95
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV--DDTLITSTSKNKDIKQIRKKVGlvfqFPESQlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 96 --TAYENLDYTARFLGLSaKERRERIlgALQRMRL----ENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGL 169
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVS-QEEAEAL--AREKLALvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 170 DPESVAEFLSLITSLRDTeHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGT-------VAELSEQQFG 232
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKpkdifqdVDFLEEKQLG 245
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-229 |
5.29e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.57 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 24 DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGL--LEPTSGSV-----DILGFDP-----------LRTPLEVKrrvGyl 85
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSIlldgeDILELSPderaragiflaFQYPVEIP---G-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 sdtVGFYDtmtayenldytarFLGLSAKERRERILGALQRMRLENRKNDKVH------------TFSHGMKQRLGLAEVL 153
Cdd:COG0396 92 ---VSVSN-------------FLRTALNARRGEELSAREFLKLLKEKMKELGldedfldryvneGFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 154 VKNCEIAILDEPTQGLDPES---VAEflsLITSLRDtEHMTILLSSHQ---LEEVqsVCDRVGLFYRGKLLKNGTvAELS 227
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDAlriVAE---GVNKLRS-PDRGILIITHYqriLDYI--KPDFVHVLVDGRIVKSGG-KELA 228
|
..
gi 359351306 228 EQ 229
Cdd:COG0396 229 LE 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-234 |
9.54e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRvgylSDTVGFYDTM----TA 97
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR----NIAVVFQDAGlfnrSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 98 YENL-----DYTARFLGLSAKerrerilgALQRMRLENRKNDKVHTF--------SHGMKQRLGLAEVLVKNCEIAILDE 164
Cdd:PRK13657 426 EDNIrvgrpDATDEEMRAAAE--------RAQAHDFIERKPDGYDTVvgergrqlSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 165 PTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSeqQFGGR 234
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRNA-DRILVFDNGRVVESGSFDELV--ARGGR 562
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-230 |
1.02e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTtilmLLGLL----EPTSGSVDILGFD-------PLRT 74
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLtrawDPQQGEILLNGQPiadyseaALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 75 PLE-VKRRVGYLSDTVgfydtmtaYENLdytarfLGLSAKERRERILGALQRMRLENR-KNDKV---------HTFSHGM 143
Cdd:PRK11160 415 AISvVSQRVHLFSATL--------RDNL------LLAAPNASDEALIEVLQQVGLEKLlEDDKGlnawlgeggRQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 144 KQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLItsLRDTEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTV 223
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTH 557
|
....*..
gi 359351306 224 AELSEQQ 230
Cdd:PRK11160 558 QELLAQQ 564
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-226 |
1.22e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.29 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRK--QYGKGML------AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG------- 68
Cdd:PRK15112 2 ETLLEVRNLSKtfRYRTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 69 -----------FDPLRTPLEVKRRVGYLsdtvgfydtmtayenLDYTARF-LGLSAKERRERILGALQRMRL-ENRKNDK 135
Cdd:PRK15112 82 ysyrsqrirmiFQDPSTSLNPRQRISQI---------------LDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 136 VHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRG 215
Cdd:PRK15112 147 PHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
250
....*....|.
gi 359351306 216 KLLKNGTVAEL 226
Cdd:PRK15112 227 EVVERGSTADV 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-226 |
1.43e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 77.53 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 11 HLRKQY-GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLEVKRRVGY---- 84
Cdd:cd03252 5 HVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVvlqe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 -------LSDTVGFYDTMTAYENLDYTARFLG-----LSAKERRERILGalqrmrlenrknDKVHTFSHGMKQRLGLAEV 152
Cdd:cd03252 85 nvlfnrsIRDNIALADPGMSMERVIEAAKLAGahdfiSELPEGYDTIVG------------EQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 153 LVKNCEIAILDEPTQGLDPESVAeflSLITSLRD-TEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAEL 226
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEH---AIMRNMHDiCAGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-226 |
1.52e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 77.93 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 14 KQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtplevkrRVGYLSDTVGFYD 93
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 94 TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPES 173
Cdd:PRK13546 99 QLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 359351306 174 VAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK13546 179 AQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-212 |
1.62e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGKgMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILML--LGLLEPT---SGSVDILG---FDPLR 73
Cdd:PRK14243 6 GTETVLRTENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGknlYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 74 TPLEVKRRVGYLSDTVGFYDTmTAYENLDYTARFLGLSAK--ERRERilgALQRMRLENRKNDKVHT----FSHGMKQRL 147
Cdd:PRK14243 85 DPVEVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmdELVER---SLRQAALWDEVKDKLKQsglsLSGGQQQRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 148 GLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSVCDRVGLF 212
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAARVSDMTAFF 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-200 |
3.06e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.39 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGKGMLAVD---DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRT---- 74
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKlssa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 75 -PLEVK-RRVGYLSDTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEV 152
Cdd:PRK11629 80 aKAELRnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 359351306 153 LVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLE 200
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ 207
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-231 |
3.98e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 76.76 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYG-----KGmlavddISLTLNKGEIFGLLGPNGSGKTTtILMLLGLLE-PTSGSVDILGfDPLRTpleVK 79
Cdd:COG4598 8 ALEVRDLHKSFGdlevlKG------VSLTARKGDVISIIGSSGSGKST-FLRCINLLEtPDSGEIRVGG-EEIRL---KP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 80 RRVGYL--SDT---------VGF-------YDTMTAYENL-DYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFS 140
Cdd:COG4598 77 DRDGELvpADRrqlqrirtrLGMvfqsfnlWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 141 HGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKN 220
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQ 235
|
250
....*....|....*...
gi 359351306 221 GTVAEL-----SE--QQF 231
Cdd:COG4598 236 GPPAEVfgnpkSErlRQF 253
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-226 |
4.28e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 75.97 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRTPlEVKRRVGYlsDTVGFYDTMTAYEN-- 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-ILEGKQITEP-GPDRMVVF--QNYSLLPWLTVRENia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 101 LDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSL 180
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 359351306 181 ITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-230 |
5.02e-16 |
|
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: 78.33 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPT-SGSVDILGFD-PLRTPL-----------EVKRRVGYLSDT- 88
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPvDIRNPAqairagiamvpEDRKRHGIVPILg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 VGFYDTMTAyenLDYTARFLGLSAKERRERILGALQRMRLENRKND-KVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:TIGR02633 356 VGKNITLSV---LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 168 GLDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-226 |
6.68e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGS---VDILGFD-PLRTPLEVKRRVG---------YLSDT 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITlTAKTVWDIREKVGivfqnpdnqFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 VGfYDTMTAYENLdytarflGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQG 168
Cdd:PRK13640 102 VG-DDVAFGLENR-------AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 169 LDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVqSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-229 |
8.72e-16 |
|
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: 75.27 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 19 GMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLRT--PLEVKRRVGYLS-DTVGFYdtM 95
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD-IRDlnLRWLRSQIGLVSqEPVLFD--G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 96 TAYENLDYtarflGLSAKERRERILGALQR------MRLENRKN----DKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:cd03249 92 TIAENIRY-----GKPDATDEEVEEAAKKAnihdfiMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 166 TQGLDPES---VAEFLSLITSLRdtehmTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:cd03249 167 TSALDAESeklVQEALDRAMKGR-----TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-226 |
1.06e-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: 77.47 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRR-VGYL 85
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 -SDTVGFydTMTAYENLdytarFLGLSAKERRERILGALQ-----------RMRLENRKNDKVHTFSHGMKQRLGLAEVL 153
Cdd:TIGR01193 554 pQEPYIF--SGSILENL-----LLGAKENVSQDEIWAACEiaeikddienmPLGYQTELSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359351306 154 VKNCEIAILDEPTQGLDpeSVAEfLSLITSLRDTEHMTILLSSHQLeEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:TIGR01193 627 LTDSKVLILDESTSNLD--TITE-KKIVNNLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-226 |
1.13e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.83 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 21 LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDIlGfDPLRTPLEVKRRVGYLSDTVG---------- 90
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-G-ERVITAGKKNKKLKPLRKKVGivfqfpehql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 91 FYDTMTayENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKV-HTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGL 169
Cdd:PRK13634 99 FEETVE--KDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSpFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 170 DPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-252 |
1.17e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLePTSGSVDILGFDPLRTPL-EVKRRVGYLSDTVGFYDTMTAYENLDyt 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaELARHRAYLSQQQTPPFAMPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 105 arfLGLSAKERRERILGAL----QRMRLENRKNDKVHTFSHGMKQRLGLAEVLVK-------NCEIAILDEPTQGLDPES 173
Cdd:PRK03695 92 ---LHQPDKTRTEAVASALnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 174 VAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAElseqqfggrqiielrVDSEKNLAETFA 252
Cdd:PRK03695 169 QAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE---------------VLTPENLAQVFG 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-183 |
1.42e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.11 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 30 LNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRTPlEVKRRVGYLSDTVGFYDTMTAYENLDYTArflG 109
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-KTATRG-DRSRFMAYLGHLPGLKADLSTLENLHFLC---G 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 110 LSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITS 183
Cdd:PRK13543 109 LHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-244 |
1.60e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILgFD--PLrtplevkr 80
Cdd:PRK13549 2 MEYLLEMKNITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEII-FEgeEL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 RVGYLSDT-----------VGFYDTMTAYEN------------LDYTARFLglsakeRRERIlgaLQRMRLENRKNDKVH 137
Cdd:PRK13549 72 QASNIRDTeragiaiihqeLALVKELSVLENiflgneitpggiMDYDAMYL------RAQKL---LAQLKLDINPATPVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 138 TFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGRH 221
|
250 260
....*....|....*....|....*..
gi 359351306 218 LKNGTVAELSEQqfggrQIIELRVDSE 244
Cdd:PRK13549 222 IGTRPAAGMTED-----DIITMMVGRE 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-226 |
2.58e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.22 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPT-SGSVDILGFDP---LR-TPLEVKRRVGY------------ 84
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwRVTADRMRFDDidlLRlSPRERRKLVGHnvsmifqepqsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 --LSDTVGfYDTMTAYENLDYTARFLGlSAKERRERILGALQRMRLENRKnDKVHTFSH----GMKQRLGLAEVLVKNCE 158
Cdd:PRK15093 102 ldPSERVG-RQLMQNIPGWTYKGRWWQ-RFGWRKRRAIELLHRVGIKDHK-DAMRSFPYelteGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 159 IAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-226 |
2.82e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTS-----GSVDILGFDPLRTPLEV---KRRVGYLSDTVGFYdT 94
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLnrlRRQVSMVHPKPNLF-P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 95 MTAYENLDYTARFLGLSAKERRERIL-GALQRMRLENRKNDKVHT----FSHGMKQRLGLAEVLVKNCEIAILDEPTQGL 169
Cdd:PRK14258 102 MSVYDNVAYGVKIVGWRPKLEIDDIVeSALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 170 DPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYR-----GKLLKNGTVAEL 226
Cdd:PRK14258 182 DPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-229 |
3.38e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 72.94 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGL--LEPTSGSVDILGFDPLRTPLEVKRRVGYlsdTVGFydtmtayen 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGI---FLAF--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 101 lDYTARFLGLSAKERrerilgalqrMRLENRKndkvhtFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSL 180
Cdd:cd03217 84 -QYPPEIPGVKNADF----------LRYVNEG------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 359351306 181 ITSLRDtEHMTILLSSHQ---LEEVQSvcDRVGLFYRGKLLKNGTVaELSEQ 229
Cdd:cd03217 147 INKLRE-EGKSVLIITHYqrlLDYIKP--DRVHVLYDGRIVKSGDK-ELALE 194
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-197 |
5.36e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.37 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV------DILGFDPLRTPLEVKRrvgylsdtvgfydtmT 96
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklEVAYFDQHRAELDPEK---------------T 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 97 AYENLDYTARFLGLSAKERreRILGALQRMRLE-NRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESva 175
Cdd:PRK11147 400 VMDNLAEGKQEVMVNGRPR--HVLGYLQDFLFHpKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET-- 475
|
170 180
....*....|....*....|..
gi 359351306 176 efLSLITSLRDTEHMTILLSSH 197
Cdd:PRK11147 476 --LELLEELLDSYQGTVLLVSH 495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-172 |
1.70e-14 |
|
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: 73.67 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGKGMLAVDdiSLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilgfdplrTPLEVKRR 81
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFSLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--------EDLKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSdtvGFYDtMTAYENLdYTARFLGLSAKERRERIlgaLQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:COG1245 407 PQYIS---PDYD-GTVEEFL-RSANTDDFGSSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170
....*....|.
gi 359351306 162 LDEPTQGLDPE 172
Cdd:COG1245 479 LDEPSAHLDVE 489
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-227 |
2.46e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG--FDPLrTPLEVKRRVG 83
Cdd:PRK15439 11 LLCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpCARL-TPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 YL-SDTVGFYDTMTAYENLdytarFLGLSAKERRERILGAL-QRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:PRK15439 89 YLvPQEPLLFPNLSVKENI-----LFGLPKRQASMQKMKQLlAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 162 LDEPTQGLDPESVAEFLSLITSLRDTEHmTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELS 227
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGV-GIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-241 |
3.70e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRKQYgKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG----FDPLRTPLEVK 79
Cdd:PRK10762 2 QALLQLKGIDKAF-PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 80 rrVGYLSDTVGFYDTMTAYENL----DYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVK 155
Cdd:PRK10762 81 --IGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 156 NCEIAILDEPTQGL-DPESVAEFlSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQqfggr 234
Cdd:PRK10762 159 ESKVIIMDEPTDALtDTETESLF-RVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED----- 231
|
....*..
gi 359351306 235 QIIELRV 241
Cdd:PRK10762 232 SLIEMMV 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-217 |
4.20e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDD--------ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLRTpLEV 78
Cdd:PRK15439 255 LPGNRRQQAAGAPVLTVEDltgegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-MLNGKEINA-LST 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 79 KRRVG----YLSD---TVGFY-DTMTAYENLDYTARFLGLSAKERRERilGALQRMRLE-----NRKNDKVHTFSHGMKQ 145
Cdd:PRK15439 333 AQRLArglvYLPEdrqSSGLYlDAPLAWNVCALTHNRRGFWIKPAREN--AVLERYRRAlnikfNHAEQAARTLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 146 RLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-216 |
6.22e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.45 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 30 LNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVD-ILGFDPLrTPLEVKRR----VGYLSDTVGFYDTMTAYENLDYT 104
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEgVITYDGI-TPEEIKKHyrgdVVYNAETDVHFPHLTVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 105 A-------RFLGLSAKERRE-------RILGaLQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLD 170
Cdd:TIGR00956 163 ArcktpqnRPDGVSREEYAKhiadvymATYG-LSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 359351306 171 PESVAEFLSLITSLRDTEHMTILLSSHQL-EEVQSVCDRVGLFYRGK 216
Cdd:TIGR00956 242 SATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGY 288
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-172 |
7.65e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLRKQYGKGMLAVDdiSLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilgfdplrTPLEVKRR 81
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDFSLEVE--GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--------PELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYLSDTvgfYDtMTAYENLDYTARFLGlSAKERRERIlgalQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:PRK13409 406 PQYIKPD---YD-GTVEDLLRSITDDLG-SSYYKSEII----KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170
....*....|.
gi 359351306 162 LDEPTQGLDPE 172
Cdd:PRK13409 477 LDEPSAHLDVE 487
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-221 |
9.67e-14 |
|
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: 68.83 E-value: 9.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPT---SGSVDILGFDPLRTPLEVKRRVGYLSDTVGFYDTMTAYE 99
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 100 NLDYTARFLGlsakerrerilgalqrmrlenrkNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLS 179
Cdd:cd03233 103 TLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 359351306 180 LITSLRDTEHMTILLSSHQL-EEVQSVCDRVGLFYRGKLLKNG 221
Cdd:cd03233 160 CIRTMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-172 |
1.38e-13 |
|
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: 71.12 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 4 EQVLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdilgfdplrtplevkrRVG 83
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLL-IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI----------------EIG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 ylsDTV--GFYDTMTayENLDytarflglSAKERRERILGALQRMRLENRK--------------ND---KVHTFSHGMK 144
Cdd:TIGR03719 383 ---ETVklAYVDQSR--DALD--------PNKTVWEEISGGLDIIKLGKREipsrayvgrfnfkgSDqqkKVGQLSGGER 449
|
170 180
....*....|....*....|....*...
gi 359351306 145 QRLGLAEVLVKNCEIAILDEPTQGLDPE 172
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-230 |
1.64e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.03 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 19 GMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLePTSGSVDILGFdPLRTpLEVKRRVGYLSdTVG-----FYD 93
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGI-ELRE-LDPESWRKHLS-WVGqnpqlPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 94 TMTayENLdytarFLG-LSAKErrERILGALQRMRLE---NRKNDKVHT--------FSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:PRK11174 438 TLR--DNV-----LLGnPDASD--EQLQQALENAWVSeflPLLPQGLDTpigdqaagLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 162 LDEPTQGLDPESVAEFLSLITSLrdTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-239 |
2.41e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILgFD--PL--RTPLEVKRR 81
Cdd:TIGR02633 1 LLEMKGIVKTFG-GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIY-WSgsPLkaSNIRDTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 -VGYLSDTVGFYDTMTAYENLdytarFLG---------LSAKERRERILGALQRMRLENRKNDK-VHTFSHGMKQRLGLA 150
Cdd:TIGR02633 79 gIVIIHQELTLVPELSVAENI-----FLGneitlpggrMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 151 EVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLsSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYI-SHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDD 232
|
250
....*....|...
gi 359351306 231 ----FGGRQIIEL 239
Cdd:TIGR02633 233 iitmMVGREITSL 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-221 |
4.84e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG----------FDPLRTPLEVKRRVGYLS----D 87
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlspgkLQALRRDIQFIFQDPYASldprQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGfYDTMtayENLdytaRFLGL-SAKERRERILGALQRMRLENRKNDKV-HTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:PRK10261 419 TVG-DSIM---EPL----RVHGLlPGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 166 TQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNG 221
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-217 |
5.33e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 66.67 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAV-DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLE-VKRRVGY 84
Cdd:cd03369 7 IEVENLSVRYAPDLPPVlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 L-SDTVGFYDTMTAyeNLDYTARFlglsakeRRERILGALqrmrlenRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:cd03369 87 IpQDPTLFSGTIRS--NLDPFDEY-------SDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 359351306 164 EPTQGLDPESVAEFLSLITSLrdTEHMTILLSSHQLEEVQSvCDRVGLFYRGKL 217
Cdd:cd03369 151 EATASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIID-YDKILVMDAGEV 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-201 |
7.87e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.50 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 24 DDISLTLNKGEIFGLLGPNGSGKTTtilmLLGLL---EPTSGSVDILGFDPLR----TPLEVKRRVGYLSDTV------- 89
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKST----LLSLItgdHPQGYSNDLTLFGRRRgsgeTIWDIKKHIGYVSSSLhldyrvs 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 90 ---------GFYDTMTAYEnldytarflglsAKERRERILGA--LQRMRLENRKNDK-VHTFSHGmKQRLGL-AEVLVKN 156
Cdd:PRK10938 353 tsvrnvilsGFFDSIGIYQ------------AVSDRQQKLAQqwLDILGIDKRTADApFHSLSWG-QQRLALiVRALVKH 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 359351306 157 CEIAILDEPTQGLDP---ESVAEFLSLITSLRDTEhmtILLSSHQLEE 201
Cdd:PRK10938 420 PTLLILDEPLQGLDPlnrQLVRRFVDVLISEGETQ---LLFVSHHAED 464
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-203 |
1.22e-12 |
|
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: 65.96 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 21 LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdILGFDPLrTPLEVK---RRVGYLS-DTVGFYDTMT 96
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKPI-SQYEHKylhSKVSLVGqEPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 97 ayENLDYtarflGLSAKERrERILGALQR-------MRLEN----RKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:cd03248 106 --DNIAY-----GLQSCSF-ECVKEAAQKahahsfiSELASgydtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 359351306 166 TQGLDPESVAEFLSLITSlrDTEHMTILLSSHQLEEVQ 203
Cdd:cd03248 178 TSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVE 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-217 |
1.50e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.67 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 11 HLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPlevKRRVGYLSDTVG 90
Cdd:PRK10908 6 HVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLK---NREVPFLRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 91 --FYD-----TMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILD 163
Cdd:PRK10908 83 miFQDhhllmDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 359351306 164 EPTQGLDPESVAEFLSLITSLRDTeHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-209 |
3.80e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKR 80
Cdd:PRK10247 2 QENSPLLQLQNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 81 R-VGYLSDT-VGFYDTMtaYENL--DYTARflglSAKERRERILGALQRMRL-ENRKNDKVHTFSHGMKQRLGLAEVLVK 155
Cdd:PRK10247 81 QqVSYCAQTpTLFGDTV--YDNLifPWQIR----NQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 359351306 156 NCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSvCDRV 209
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-233 |
8.40e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.81 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 17 GKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLR--TPLEVKRRVGYLSDTVG-FYD 93
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD-LRdyTLASLRNQVALVSQNVHlFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 94 TMTayENLDYTARflglsAKERRERILGALQR---MRLENRKNDKVHT--------FSHGMKQRLGLAEVLVKNCEIAIL 162
Cdd:PRK11176 432 TIA--NNIAYART-----EQYSREQIEEAARMayaMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 163 DEPTQGLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQS-----VCDRVGLFYRGK----LLKNGTVAELSEQQFGG 233
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEKadeilVVEDGEIVERGThaelLAQNGVYAQLHKMQFGQ 582
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-200 |
8.58e-12 |
|
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: 63.26 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdilgfdplrtplEVKRRVGYLSDTvGFYDTMTAYENLDYT 104
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV------------SVPGSIAYVSQE-PWIQNGTIRENILFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 105 ARFLglsaKERRERILGA--LQR--MRLENRKNDKVH----TFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPEsVAE 176
Cdd:cd03250 90 KPFD----EERYEKVIKAcaLEPdlEILPDGDLTEIGekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH-VGR 164
|
170 180
....*....|....*....|....*..
gi 359351306 177 FL--SLITS-LRDteHMTILLSSHQLE 200
Cdd:cd03250 165 HIfeNCILGlLLN--NKTRILVTHQLQ 189
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-204 |
8.92e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.97 E-value: 8.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPlevKRRVGYLSDTVGFYDTMTAYENLDYT 104
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA---KPYCTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 105 ARFLGLSakerrERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITsL 184
Cdd:PRK13541 95 SEIYNSA-----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV-M 168
|
170 180
....*....|....*....|
gi 359351306 185 RDTEHMTILLSSHQLEEVQS 204
Cdd:PRK13541 169 KANSGGIVLLSSHLESSIKS 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-217 |
9.50e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLE-VKRRVGYLSDTV---GFYDTMTA 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvVTRSPQDgLANGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 98 YEN-----LDYTARFLGlSAKERRERILgALQRMRLENRK----NDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQG 168
Cdd:PRK10762 348 KENmsltaLRYFSRAGG-SLKHADEQQA-VSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 359351306 169 LDPESVAEFLSLITSLRdTEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK10762 426 VDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-217 |
1.54e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLE-PTSGSVDILGfDPL--RTPL-----------EVKRRVGYLSD- 87
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDG-KPVkiRNPQqaiaqgiamvpEDRKRDGIVPVm 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 88 TVGFYDTMTAYEnldytaRFLGLS----AKERRErILGALQRMRLENRKND-KVHTFSHGMKQRLGLAEVLVKNCEIAIL 162
Cdd:PRK13549 357 GVGKNITLAALD------RFTGGSriddAAELKT-ILESIQRLKVKTASPElAIARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 163 DEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-170 |
1.56e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.28 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 14 KQYGkGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGsvDILGFDPLRTPLE-VKRRVGYLSDTVGFY 92
Cdd:PRK11000 11 KAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG--DLFIGEKRMNDVPpAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 93 DTMTAYENLDYTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLD 170
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-244 |
3.82e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.58 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfDPLRTPLEVKRRVG--- 83
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG-RPLSSLSHSVLRQGvam 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 84 ------YLSDTvgFYDTMTayenldytarfLGLSAKErrERILGALQRMRL-----------ENRKNDKVHTFSHGMKQR 146
Cdd:PRK10790 420 vqqdpvVLADT--FLANVT-----------LGRDISE--EQVWQALETVQLaelarslpdglYTPLGEQGNNLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 147 LGLAEVLVKNCEIAILDEPTQGLDP---ESVAEFLSLItslrdTEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTV 223
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSgteQAIQQALAAV-----REHTTLVVIAHRLSTIVEA-DTILVLHRGQAVEQGTH 558
|
250 260
....*....|....*....|...
gi 359351306 224 AELSEQQfgGR--QIIELRVDSE 244
Cdd:PRK10790 559 QQLLAAQ--GRywQMYQLQLAGE 579
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-172 |
7.45e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 5 QVLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDI-----LGF--------DP 71
Cdd:PRK11819 323 KVIEAENLSKSFGDRLL-IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvkLAYvdqsrdalDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 72 LRTPLEVkrrvgyLSD-----TVGFYDTMT-AyenldYTARFlGLSakerrerilGALQrmrlenrkNDKVHTFSHGMKQ 145
Cdd:PRK11819 402 NKTVWEE------ISGgldiiKVGNREIPSrA-----YVGRF-NFK---------GGDQ--------QKKVGVLSGGERN 452
|
170 180
....*....|....*....|....*..
gi 359351306 146 RLGLAEVLVKNCEIAILDEPTQGLDPE 172
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-170 |
1.05e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtplevkRRVGYLS 86
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG-----------RVVNELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 ----------DTVGFYDTMTAYENLDYTARFLGLSAKERRERILGALQRMRLE---NRKNDKVhtfSHGMKQRLGLAEVL 153
Cdd:PRK11650 73 padrdiamvfQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEpllDRKPREL---SGGQRQRVAMGRAI 149
|
170
....*....|....*..
gi 359351306 154 VKNCEIAILDEPTQGLD 170
Cdd:PRK11650 150 VREPAVFLFDEPLSNLD 166
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-244 |
1.07e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 19 GMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG----FDPLRTPLE------------VKRRV 82
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidFKSSKEALEngismvhqelnlVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 83 -------------GYLSDTVGFY-DTMTAYENLDytarflglsakerrerilgalqrmrLENRKNDKVHTFSHGMKQRLG 148
Cdd:PRK10982 90 vmdnmwlgryptkGMFVDQDKMYrDTKAIFDELD-------------------------IDIDPRAKVATLSVSQMQMIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 149 LAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSE 228
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKE-RGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTM 223
|
250
....*....|....*.
gi 359351306 229 QqfggrQIIELRVDSE 244
Cdd:PRK10982 224 D-----KIIAMMVGRS 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-218 |
1.09e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 33 GEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDplRTPL-EVKRRVGYLSDTVGFYDTMTAYENLDYTARFLGLS 111
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN--RKPTkQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 112 AKERRERILGA------LQRMRLENR--KNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITS 183
Cdd:PLN03211 172 SLTKQEKILVAesviseLGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190
....*....|....*....|....*....|....*.
gi 359351306 184 LRDtEHMTILLSSHQ-LEEVQSVCDRVGLFYRGKLL 218
Cdd:PLN03211 252 LAQ-KGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCL 286
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-239 |
1.39e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLEVKRRVGYL------SDtvGFYDTMTAY 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPiDIRSPRDAIRAGIMLcpedrkAE--GIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 99 ENLDYTAR----FLGLSAKERRERILGA--LQRMRLENRKND-KVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDP 171
Cdd:PRK11288 350 DNINISARrhhlRAGCLINNRWEAENADrfIRSLNIKTPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 172 ESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRVGLFYRGKLlkngtVAELSEQQFGGRQIIEL 239
Cdd:PRK11288 430 GAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRI-----AGELAREQATERQALSL 491
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-164 |
1.81e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 61.74 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdilgfdplrtplevkrrvgYLSDTVGFYDTMTAYENL---- 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI-------------------LLDGQPVTADNREAYRQLfsav 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 102 --DY--TARFLGLSAKERRERILGALQRMRLENR---KNDKVHT--FSHGMKQRLGLAEVLVKNCEIAILDE 164
Cdd:COG4615 412 fsDFhlFDRLLGLDGEADPARARELLERLELDHKvsvEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-200 |
1.91e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAV-DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEpTSGSVDILGFDPLRTPLEVKRRV-GY 84
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAfGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSDTVgFYDTMTAYENLDYTARFLGLSAKERRERIlgALQRM------RLENRKNDKVHTFSHGMKQRLGLAEVLVKNCE 158
Cdd:TIGR01271 1297 IPQKV-FIFSGTFRKNLDPYEQWSDEEIWKVAEEV--GLKSVieqfpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 359351306 159 IAILDEPTQGLDPESvaeFLSLITSLRDT-EHMTILLSSHQLE 200
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVT---LQIIRKTLKQSfSNCTVILSEHRVE 1413
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-198 |
3.21e-10 |
|
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: 58.41 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 24 DDISLTLNKGEIFGLLGPNGSGKTTtilmLLGLL--EPTSGSV--DILgFDPLRTPLEVKRRVGYLSDTVGFYDTMTAYE 99
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTT----LLDVLagRKTAGVItgEIL-INGRPLDKNFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 100 NLDYTARFLGLSAKERRerilgalqrmrlenrkndkvhtfshgmkqRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLS 179
Cdd:cd03232 99 ALRFSALLRGLSVEQRK-----------------------------RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170
....*....|....*....
gi 359351306 180 LITSLRDTeHMTILLSSHQ 198
Cdd:cd03232 150 FLKKLADS-GQAILCTIHQ 167
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-198 |
3.26e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 21 LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVGYLSDTVGFYDTMTAYEN 100
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 101 LDYTARFLGLSAKerrerILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSL 180
Cdd:PRK13540 95 CLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*...
gi 359351306 181 ITSLRdTEHMTILLSSHQ 198
Cdd:PRK13540 170 IQEHR-AKGGAVLLTSHQ 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-232 |
4.28e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGL--LEPTSGSVDILGFDPLRtpLEVKRRVG--------YLSDTVGFYDTM 95
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLE--LSPEDRAGegifmafqYPVEIPGVSNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 96 tayenldytarFLGLSAKERRE-RILGALQRMRLENRKNDKVHT---------------FSHGMKQRLGLAEVLVKNCEI 159
Cdd:PRK09580 98 -----------FLQTALNAVRSyRGQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 160 AILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQ--LEEVQSvcDRVGLFYRGKLLKNGT---VAELSEQQFG 232
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQriLDYIKP--DYVHVLYQGRIVKSGDftlVKQLEEQGYG 242
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
25-229 |
4.49e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGllEP----TSGSV-----DILGFDPlrtplEVKRRVGYLsdtVGF-YD- 93
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDIlfkgeSILDLEP-----EERAHLGIF---LAFqYPi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 94 TMTAYENLDytarFLGLSAKERRERI----LGALQRMRLENRKNDKVHT------------FSHGMKQRLGLAEVLVKNC 157
Cdd:CHL00131 95 EIPGVSNAD----FLRLAYNSKRKFQglpeLDPLEFLEIINEKLKLVGMdpsflsrnvnegFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359351306 158 EIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQ--LEEVQSvcDRVGLFYRGKLLKNGTvAELSEQ 229
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQrlLDYIKP--DYVHVMQNGKIIKTGD-AELAKE 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-209 |
8.83e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 5 QVLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilgfdplrtpLEVKRRVGY 84
Cdd:PRK15064 318 NALEVENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK----------WSENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSD--TVGFYDTMTAYenlDYTARFLGLSAKERRERilGALQRMRL-ENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAI 161
Cdd:PRK15064 387 YAQdhAYDFENDLTLF---DWMSQWRQEGDDEQAVR--GTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 359351306 162 LDEPTQGLDPESVAeflSLITSLRDTEHmTILLSSHQLEEVQSVCDRV 209
Cdd:PRK15064 462 MDEPTNHMDMESIE---SLNMALEKYEG-TLIFVSHDREFVSSLATRI 505
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-175 |
1.10e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 3 SEQVLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSG--------SVDILG----FD 70
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpgiKVGYLPqepqLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 71 PLRTPLE-VKRRVGYLSDTVGFYDTMTAYENlDYTARFLGLSAKERR-ERILGALQRMRLENR------------KNDKV 136
Cdd:TIGR03719 81 PTKTVREnVEEGVAEIKDALDRFNEISAKYA-EPDADFDKLAAEQAElQEIIDAADAWDLDSQleiamdalrcppWDADV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 359351306 137 HTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVA 175
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-230 |
1.24e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtplevkrRVGYlSDTVGFYDTMTAYENLdyt 104
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISF-SPQTSWIMPGTIKDNI--- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 105 arFLGLSAKERRER-ILGALQR----MRLENRKN----DKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVA 175
Cdd:TIGR01271 508 --IFGLSYDEYRYTsVIKACQLeediALFPEKDKtvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 176 E-FLSLITSLRDTEhmTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:TIGR01271 586 EiFESCLCKLMSNK--TRILVTSKLEHLKKA-DKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-197 |
1.70e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 5 QVLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrTPLEVKRRVGY 84
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG-----KPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSDtvgFYDTMTAYENLDytaRFLGLSAKERRERILGA-LQRMRLENR---KNDKVHT--FSHGMKQRLGLAEVLVKNCE 158
Cdd:PRK10522 396 RKL---FSAVFTDFHLFD---QLLGPEGKPANPALVEKwLERLKMAHKlelEDGRISNlkLSKGQKKRLALLLALAEERD 469
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 359351306 159 IAILDEPTQGLDPESVAEF-LSLITSLRDTEHmTILLSSH 197
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFyQVLLPLLQEMGK-TIFAISH 508
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-203 |
1.88e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV--------------------DILGFDPLRTPLEVKRRVGY 84
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkwwrskiGVVSQDPLLFSNSIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSDTVGFYDTMTAYENLDYTARFLGLSAKER-RERILGALQRMR--------LENRKN---------------------- 133
Cdd:PTZ00265 483 SLYSLKDLEALSNYYNEDGNDSQENKNKRNScRAKCAGDLNDMSnttdsnelIEMRKNyqtikdsevvdvskkvlihdfv 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 134 ----DKVHTF--------SHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEE 201
Cdd:PTZ00265 563 salpDKYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLST 642
|
..
gi 359351306 202 VQ 203
Cdd:PTZ00265 643 IR 644
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-209 |
2.06e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEifGLL--GPNGSGKTTTILMLLGLLEPTSGSVDilgfdplRTPLEvkrRVGYLSdtvgfydtMTAY-- 98
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIA-------RPAGA---RVLFLP--------QRPYlp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 99 -----ENLDYTARFLGLSakerRERILGALQRMRLE------NRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:COG4178 439 lgtlrEALLYPATAEAFS----DAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 359351306 168 GLDPESVAEFLSLitsLRDTEHMTILLS-SHQlEEVQSVCDRV 209
Cdd:COG4178 515 ALDEENEAALYQL---LREELPGTTVISvGHR-STLAAFHDRV 553
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
12-222 |
7.46e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.50 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 12 LRKQYGKGMLAVD--DISltlnKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKrrvgylsdtv 89
Cdd:cd03222 6 CVKRYGVFFLLVElgVVK----EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 90 gfydtmtayenldytarflglsakerrerilgalqrmrlenrkndkvhtFSHGMKQRLGLAEVLVKNCEIAILDEPTQGL 169
Cdd:cd03222 72 -------------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 359351306 170 DPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYrGKLLKNGT 222
Cdd:cd03222 103 DIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGI 154
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-209 |
9.75e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 19 GMLAVDDISLTLNKGEIFGLLGPNGSGKTTtiLM--LLGLLEPTSGSVDILgfdplrtplevkrrvgYLSDTVGFYDT-- 94
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKST--LMkvLSGVYPHGSYEGEIL----------------FDGEVCRFKDIrd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 95 ------------------MTAYENLdytarFLG--------LSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLG 148
Cdd:NF040905 75 sealgiviihqelalipyLSIAENI-----FLGnerakrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 149 LAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDtEHMTILLSSHQLEEVQSVCDRV 209
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSI 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-230 |
1.20e-08 |
|
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: 55.25 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 2 NSEQVLSISHLrKQYGKGMLavDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGfdplrtplevkrR 81
Cdd:cd03291 35 SDDNNLFFSNL-CLVGAPVL--KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------R 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 82 VGYlSDTVGFYDTMTAYENLdytarFLGLSAKERRERilGALQRMRLEN------RKNDKVH-----TFSHGMKQRLGLA 150
Cdd:cd03291 100 ISF-SSQFSWIMPGTIKENI-----IFGVSYDEYRYK--SVVKACQLEEditkfpEKDNTVLgeggiTLSGGQRARISLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 151 EVLVKNCEIAILDEPTQGLDPESVAE-FLSLITSLRDTEhmTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVFTEKEiFESCVCKLMANK--TRILVTSKMEHLKKA-DKILILHEGSSYFYGTFSELQSL 248
|
.
gi 359351306 230 Q 230
Cdd:cd03291 249 R 249
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-199 |
1.86e-08 |
|
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: 55.60 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 24 DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDpLR--TPLEVKRRVGYL-SDTVGFYDTMtaYEN 100
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD-IRdvTQASLRAAIGIVpQDTVLFNDTI--AYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 101 LDYtARfLGLSakerRERILGALQRMRLenrkndkvHTF-------------------SHGMKQRLGLAEVLVKNCEIAI 161
Cdd:COG5265 452 IAY-GR-PDAS----EEEVEAAARAAQI--------HDFieslpdgydtrvgerglklSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190
....*....|....*....|....*....|....*....
gi 359351306 162 LDEPTQGLDPESVAEFLSlitSLRD-TEHMTILLSSHQL 199
Cdd:COG5265 518 FDEATSALDSRTERAIQA---ALREvARGRTTLVIAHRL 553
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-200 |
2.61e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.09 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 7 LSISHLRKQYGKGMLAV-DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEpTSGSVDILGFDPLRTPLEVKRRV-GY 84
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAfGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LSDTVgFYDTMTAYENLD-----------YTARFLGLsaKERRERILGALQRMRLenrknDKVHTFSHGMKQRLGLAEVL 153
Cdd:cd03289 82 IPQKV-FIFSGTFRKNLDpygkwsdeeiwKVAEEVGL--KSVIEQFPGQLDFVLV-----DGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 359351306 154 VKNCEIAILDEPTQGLDPESvaeFLSLITSLRDT-EHMTILLSSHQLE 200
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPIT---YQVIRKTLKQAfADCTVILSEHRIE 198
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-229 |
2.91e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.72 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSV---DI----LGFDPLRTPLEVKRRVGYL-SDTV---- 89
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhDIpltkLQLDSWRSRLAVVSQTPFLfSDTVanni 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 90 --GFYDTMTayENLDYTARFLGLsakerRERILGALQRMRLEnrKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQ 167
Cdd:PRK10789 410 alGRPDATQ--QEIEHVARLASV-----HDDILRLPQGYDTE--VGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 168 GLDPESVAEFLSLITSLRdtEHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWG--EGRTVIISAHRLSALTEA-SEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-228 |
4.25e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 22 AVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFD-PLRTPLEV-----------KRRVG-YLSDT 88
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKiNNHNANEAinhgfalvteeRRSTGiYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 89 VGFYDTMTayeNLD-YTARFLGLSAKERRERILGALQRMRLEN-RKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:PRK10982 343 IGFNSLIS---NIRnYKNKVGLLDNSRMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 167 QGLDPESVAEFLSLITSLRDTEHMTILLSShQLEEVQSVCDRVglfyrgKLLKNGTVAELSE 228
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKKDKGIIIISS-EMPELLGITDRI------LVMSNGLVAGIVD 474
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-214 |
5.93e-08 |
|
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: 52.22 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 40 GPNGSGKTTTILMLL----GLLEPTSGSVDILGfDPLRTPlEVKRRVgYLSDTVGFYDTMTAYENLDY--TARFLglsak 113
Cdd:cd03240 29 GQNGAGKTTIIEALKyaltGELPPNSKGGAHDP-KLIREG-EVRAQV-KLAFENANGKKYTITRSLAIleNVIFC----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 114 eRRERILGALQRMRlenrkndkvHTFSHGMKQ------RLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLS-LITSLRD 186
Cdd:cd03240 101 -HQGESNWPLLDMR---------GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAeIIEERKS 170
|
170 180
....*....|....*....|....*...
gi 359351306 187 TEHMTILLSSHQlEEVQsvcDRVGLFYR 214
Cdd:cd03240 171 QKNFQLIVITHD-EELV---DAADHIYR 194
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
11-225 |
1.08e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.57 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 11 HLRKQYGKGMLAVDdisLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG---FDPLRT---PLEvKRRVGY 84
Cdd:PRK11144 5 NFKQQLGDLCLTVN---LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGiclPPE-KRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 LsdtvgFYDT-----MTAYENLDYtarflGLSAKERRE--RILGALQRMRLENRKNdkvHTFSHGMKQRLGLAEVLVKNC 157
Cdd:PRK11144 81 V-----FQDArlfphYKVRGNLRY-----GMAKSMVAQfdKIVALLGIEPLLDRYP---GSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 158 EIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAE 225
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-229 |
1.78e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 27 SLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRVgyLSDTVGFYDTMTAYENLDYTAR 106
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL--VSDEWQRNNTDMLSPGEDDTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 107 F------LGLSAKERRERILGALQRMRLENRKNDKVHTfshGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSL 180
Cdd:PRK10938 101 TtaeiiqDEVKDPARCEQLAQQFGITALLDRRFKYLST---GETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 359351306 181 ITSLrDTEHMTILLSSHQLEEVQSVCDRVGLFYRGKLLKNGTVAELSEQ 229
Cdd:PRK10938 178 LASL-HQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-230 |
2.36e-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: 52.26 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 21 LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDI-------LGFDPLRTPLEVKRRvgylsDTVGFYD 93
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdglniakIGLHDLRFKITIIPQ-----DPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 94 TMTAyeNLD----YTARFLGLSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGL 169
Cdd:TIGR00957 1375 SLRM--NLDpfsqYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 170 DPESVAEFLSLITSLRDTehMTILLSSHQLEEVQSVCdRVGLFYRGKLLKNGTVAELSEQQ 230
Cdd:TIGR00957 1453 DLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQR 1510
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-170 |
4.54e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 32 KGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilgfdplrTPLEVKRRVGYLSDTvGFYDTMTA-YEN---------- 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD--------EEPSWDEVLKRFRGT-ELQDYFKKlANGeikvahkpqy 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359351306 101 LDYTARFLGLSAKE------RRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLD 170
Cdd:COG1245 169 VDLIPKVFKGTVREllekvdERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-170 |
7.70e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilgfdplrtpLEVKRRVGYL 85
Cdd:PRK10636 312 LLKMEKVSAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG----------LAKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 sdtvgfydtmtAYENLDYtarflgLSAKERRERILGALQRMRLENR----------KNDKV----HTFSHGMKQRLGLAE 151
Cdd:PRK10636 381 -----------AQHQLEF------LRADESPLQHLARLAPQELEQKlrdylggfgfQGDKVteetRRFSGGEKARLVLAL 443
|
170
....*....|....*....
gi 359351306 152 VLVKNCEIAILDEPTQGLD 170
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLD 462
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-267 |
9.76e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 133 NDKVHTFSHGMKQRLGLAEVLvkNCEIA----ILDEPTQGLDPESVAEFLSLITSLRDTEHmTILLSSHQlEEVQSVCDR 208
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADR 546
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359351306 209 V-------GLFyRGKLLKNGTVAE-------LSEQQFGGRQIIELRVDSEKNLA------ETFAGISEVTKVLPAGRQT 267
Cdd:PRK00635 547 IidigpgaGIF-GGEVLFNGSPREflaksdsLTAKYLRQELTIPIPEKRTNSLGtltlskATKHNLKDLTISLPLGRLT 624
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-226 |
1.26e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 11 HLRkqYGKGMLAV-DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKRRV------- 82
Cdd:PLN03232 1241 HLR--YRPGLPPVlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVlsiipqs 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 83 -GYLSDTVGF-YDTMTAYENLDytarflgLSAKERRERILGALQR--MRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCE 158
Cdd:PLN03232 1319 pVLFSGTVRFnIDPFSEHNDAD-------LWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 159 IAILDEPTQGLDPESVaeflSLI--TSLRDTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PLN03232 1392 ILVLDEATASVDVRTD----SLIqrTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-226 |
2.20e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 26 ISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPL-EVKRRVGYL-------SDTVGFydtmta 97
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLmDLRKVLGIIpqapvlfSGTVRF------ 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 98 yeNLDytaRFLGLSAKERRErilgALQRMRLEN--RKNDKV---------HTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:PLN03130 1332 --NLD---PFNEHNDADLWE----SLERAHLKDviRRNSLGldaevseagENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359351306 167 QGLDPESVAeflsLI--TSLRDTEHMTILLSSHQLEEVQSvCDRVGLFYRGKLLKNGTVAEL 226
Cdd:PLN03130 1403 AAVDVRTDA----LIqkTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-175 |
2.75e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 1 MNSEQVLSISHLRKQYGKGMLAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSG--------SVDILG---- 68
Cdd:PRK11819 1 MMAQYIYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGearpapgiKVGYLPqepq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 69 FDPLRTPLE-VKRRVGYLSDTVGFYD-TMTAYENLDytARFLGLSAKERR-ERILGALQRMRLENR------------KN 133
Cdd:PRK11819 81 LDPEKTVREnVEEGVAEVKAALDRFNeIYAAYAEPD--ADFDALAAEQGElQEIIDAADAWDLDSQleiamdalrcppWD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 359351306 134 DKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVA 175
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA 200
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-206 |
2.78e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 6 VLSISHLRKQYGKGMLaVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilgfdplrtpLEVKRRVGYL 85
Cdd:PRK15064 1 MLSTANITMQFGAKPL-FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS----------LDPNERLGKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 86 S------------DTVGFYDT-MTA--------YENLDYT--------------ARFLGLSAKERR-ERILGALQRMRLE 129
Cdd:PRK15064 70 RqdqfafeeftvlDTVIMGHTeLWEvkqerdriYALPEMSeedgmkvadlevkfAEMDGYTAEARAgELLLGVGIPEEQH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 130 NRKNDKVhtfSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDpesvaeflslITSLRDTEHM------TILLSSHQLEEVQ 203
Cdd:PRK15064 150 YGLMSEV---APGWKLRVLLAQALFSNPDILLLDEPTNNLD----------INTIRWLEDVlnernsTMIIISHDRHFLN 216
|
...
gi 359351306 204 SVC 206
Cdd:PRK15064 217 SVC 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-204 |
3.49e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLgllePTSGSVDILGFDPL--RTPLEVKRRVGYLSDTvgfydtmtayeNLD 102
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPKfsRNKLIFIDQLQFLIDV-----------GLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 103 YtarflglsakerrerilgalqrMRLenrkNDKVHTFSHGMKQRLGLAEVLVKNCE--IAILDEPTQGLDPESVAEFLSL 180
Cdd:cd03238 78 Y----------------------LTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180
....*....|....*....|....
gi 359351306 181 ITSLRDTEHmTILLSSHQLEEVQS 204
Cdd:cd03238 132 IKGLIDLGN-TVILIEHNLDVLSS 154
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-204 |
3.61e-06 |
|
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: 46.21 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 32 KGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVdilgfdplrtplevkrrvgylsdtvgFYDTMtayenldytarflgls 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDG---------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 112 akerrERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPES-----VAEFLSLITSLRD 186
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQealllLLEELRLLLLLKS 113
|
170
....*....|....*...
gi 359351306 187 TEHMTILLSSHQLEEVQS 204
Cdd:smart00382 114 EKNLTVILTTNDEKDLGP 131
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-200 |
3.71e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.26 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 24 DDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLE--PTSGSVDIL------------GFDPLRTPLEVKR---RVGyLS 86
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPdnqfgreaslidAIGRKGDFKDAVEllnAVG-LS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 87 DTVGFydtmtayenldytarflglsakeRRerilgalqrmrlenrkndKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:COG2401 126 DAVLW-----------------------LR------------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|....*
gi 359351306 167 QGLDPEsVAEFLSLITSLRDTEH-MTILLSSHQLE 200
Cdd:COG2401 165 SHLDRQ-TAKRVARNLQKLARRAgITLVVATHHYD 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-215 |
3.77e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 33 GEIFGLLGPNGSGKTTTILMLLGLLepTSGSVD----ILGFDPLRTPLEvkRRVGYLSDTVGFYDTMTAYENLDYTARFL 108
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERV--TTGVITggdrLVNGRPLDSSFQ--RSIGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 109 ---GLSAKERRERILGALQRMRLENRKNDKVHTFSHGM----KQRLGLAEVLVKNCEIAI-LDEPTQGLDPESVAEFLSL 180
Cdd:TIGR00956 865 qpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKL 944
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 359351306 181 ITSLRDTEHmTILLSSHQ-----LEEVqsvcDRVGLFYRG 215
Cdd:TIGR00956 945 MRKLADHGQ-AILCTIHQpsailFEEF----DRLLLLQKG 979
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-198 |
4.78e-06 |
|
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: 45.99 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILG-----FDPLRTplevkrrvgYLSDTvgfydtmta 97
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEgedllFLPQRP---------YLPLG--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 98 yeNLdytarflglsakerRERILGALQRmrlenrkndkvhTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEF 177
Cdd:cd03223 79 --TL--------------REQLIYPWDD------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170 180
....*....|....*....|..
gi 359351306 178 LSLItslrdTEHMTILLS-SHQ 198
Cdd:cd03223 131 YQLL-----KELGITVISvGHR 147
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-271 |
6.36e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGllEPTSGSVD----ILGFdPLRTplEVKRRV-GYLSDTVGFYDTMTAYE 99
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdirISGF-PKKQ--ETFARIsGYCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 100 NLDYTArFLGLsAKE--RRERILGALQRMRLENRKNDK--------VHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGL 169
Cdd:PLN03140 973 SLIYSA-FLRL-PKEvsKEEKMMFVDEVMELVELDNLKdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 170 DPESVAEFLSLITSLRDTEHmTILLSSHQLE-EVQSVCDRVGLFYR-GKLLKNGTVAELSEqqfggrQIIElrvdseknL 247
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGR-TVVCTIHQPSiDIFEAFDELLLMKRgGQVIYSGPLGRNSH------KIIE--------Y 1115
|
250 260
....*....|....*....|....*
gi 359351306 248 AETFAGISEVT-KVLPAgrqTWNLE 271
Cdd:PLN03140 1116 FEAIPGVPKIKeKYNPA---TWMLE 1137
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-170 |
1.02e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 29 TLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilgfDPLrTPLEVKRRV------GYLSDTvgfydtmtaYEN-- 100
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE----EEP-SWDEVLKRFrgtelqNYFKKL---------YNGei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 101 --------LDYTARFLGLSAKERRERI--LGAL----QRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPT 166
Cdd:PRK13409 161 kvvhkpqyVDLIPKVFKGKVRELLKKVdeRGKLdevvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
....
gi 359351306 167 QGLD 170
Cdd:PRK13409 241 SYLD 244
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-232 |
1.29e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 45.67 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 30 LNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPLRTPLEVKR-RVGY-LSDTVGFYDTMTAyeNLDytarf 107
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRsRLSIiLQDPILFSGSIRF--NLD----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 108 lgLSAKERRERILGALQRMRLENRKN------DKVHT-----FSHGMKQRLGLAEVLVKNCEIAILDEPTQGLD--PESV 174
Cdd:cd03288 117 --PECKCTDDRLWEALEIAQLKNMVKslpgglDAVVTeggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDmaTENI 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 175 AEFLsLITSLRDTEHMTIllsSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELSEQQFG 232
Cdd:cd03288 195 LQKV-VMTAFADRTVVTI---AHRVSTILDA-DLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-170 |
1.38e-05 |
|
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: 45.82 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 33 GEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDilGFDPLRTPLEVKRRV---GYLSDTVGfyDTMTAYENLDYT----A 105
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD--DPPDWDEILDEFRGSelqNYFTKLLE--GDVKVIVKPQYVdlipK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 106 RFLG-----LSAKERRERILGALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLD 170
Cdd:cd03236 102 AVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-198 |
1.98e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPT---SGSVDILG-----FDPLRTPlevkrrvGYLSDTVGFYDTMT 96
Cdd:PLN03140 183 DASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGyrlneFVPRKTS-------AYISQNDVHVGVMT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 97 AYENLDYTARFLG-------LSAKERRERILGALQR------MR---LENRKN-----------------------DKVH 137
Cdd:PLN03140 256 VKETLDFSARCQGvgtrydlLSELARREKDAGIFPEaevdlfMKataMEGVKSslitdytlkilgldickdtivgdEMIR 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359351306 138 TFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQ 198
Cdd:PLN03140 336 GISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQ 396
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-174 |
4.72e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGSVDILGFDPL-----RTPLEVKRRVGYLSDTVGFYDTM-- 95
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLawvnqETPALPQPALEYVIDGDREYRQLea 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 96 ---TAYENLDYTA------RFLGLSAKERRERILGALQRMRLENRKNDK-VHTFSHGMKQRLGLAEVLVKNCEIAILDEP 165
Cdd:PRK10636 97 qlhDANERNDGHAiatihgKLDAIDAWTIRSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
....*....
gi 359351306 166 TQGLDPESV 174
Cdd:PRK10636 177 TNHLDLDAV 185
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-185 |
9.55e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 28 LTLNKGeIFGLLGPNGSGKtTTIL--MLLGLLEPTSGSVDI---------------LGFDPLRTPLEVKRRVGylsDTVG 90
Cdd:COG0419 19 IDFDDG-LNLIVGPNGAGK-STILeaIRYALYGKARSRSKLrsdlinvgseeasveLEFEHGGKRYRIERRQG---EFAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 91 FYDTmTAYENLDYTARFLGLSAKERRERILGALQRmRLENRKN-------------------DKVHTFSHGMKQRLGLAE 151
Cdd:COG0419 94 FLEA-KPSERKEALKRLLGLEIYEELKERLKELEE-ALESALEelaelqklkqeilaqlsglDPIETLSGGERLRLALAD 171
|
170 180 190
....*....|....*....|....*....|....
gi 359351306 152 VLVknceiAILDepTQGLDPESVAEFLSLITSLR 185
Cdd:COG0419 172 LLS-----LILD--FGSLDEERLERLLDALEELA 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-232 |
1.54e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 138 TFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSSHQLEEVQ--------SVCDRV 209
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKrsdkivvfNNPDRT 1437
|
90 100
....*....|....*....|...
gi 359351306 210 GLFYRGKllknGTVAELSEQQFG 232
Cdd:PTZ00265 1438 GSFVQAH----GTHEELLSVQDG 1456
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-200 |
2.42e-04 |
|
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: 40.81 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 24 DDISLTLNKGEIFGLLGPNGSGKTTtILMLLGLleptsgsvdILGFDPLRTPLEVKRRVGYLSdtvgfydtmtAYENLDY 103
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKST-ILDAIGL---------ALGGAQSATRRRSGVKAGCIV----------AAVSAEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 104 TARFLGLSakerrerilgalqrmrlenrkndkvhtfsHGMKQRLGLAEVL----VKNCEIAILDEPTQGLDPESVAEFLS 179
Cdd:cd03227 72 IFTRLQLS-----------------------------GGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180
....*....|....*....|.
gi 359351306 180 LITSLRDTEHMTILLsSHQLE 200
Cdd:cd03227 123 AILEHLVKGAQVIVI-THLPE 142
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
72-204 |
2.59e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 72 LRTPLEVKrrvgYLSDTVGFYDTMTAYENLDYtarFLGLSAKERRERILG--ALQRMRLenrkNDKVHTFSHGMKQRLGL 149
Cdd:TIGR00630 772 NRETLEVK----YKGKNIADVLDMTVEEAYEF---FEAVPSISRKLQTLCdvGLGYIRL----GQPATTLSGGEAQRIKL 840
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 359351306 150 AEVLVKNCE---IAILDEPTQGLDPESVAEFLSLITSLRDTEHmTILLSSHQLEEVQS 204
Cdd:TIGR00630 841 AKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKT 897
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-227 |
2.75e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 25 DISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTS-GSVDILGfdplrtplevkrRVGYLSDtVGFYDTMTAYENLDY 103
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG------------TVAYVPQ-VSWIFNATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 104 TARFlglsAKERRERIL--GALQRmRLE-------NRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESV 174
Cdd:PLN03130 702 GSPF----DPERYERAIdvTALQH-DLDllpggdlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 359351306 175 AEFLSliTSLRDT-EHMTILLSSHQLEEVQSVcDRVGLFYRGKLLKNGTVAELS 227
Cdd:PLN03130 777 RQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELS 827
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
95-207 |
3.04e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 95 MTAYENLDYTARFLGLSAKerreriLGALQRMRLENRK-NDKVHTFSHGMKQRLGLAEVLVKNCE---IAILDEPTQGLD 170
Cdd:cd03271 131 MTVEEALEFFENIPKIARK------LQTLCDVGLGYIKlGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLH 204
|
90 100 110
....*....|....*....|....*....|....*..
gi 359351306 171 PESVAEFLSLITSLRDTEHmTILLSSHQLeEVQSVCD 207
Cdd:cd03271 205 FHDVKKLLEVLQRLVDKGN-TVVVIEHNL-DVIKCAD 239
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
21-217 |
5.38e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 40.43 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 21 LAVDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLLEPTSGsvDILGFDPLRTPLEVKRRVgylsdtvgfYDTMTAYEN 100
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEG--DFIGLRGDALPLGANSFI---------LPGLTGEEN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 101 LDYTARFLGLSAKERRERilgALQRMRLENRKNDKVHTFSHGMKQRLGLAEVLVKNCEIAILDEPTQGLDPESVAEFLSL 180
Cdd:PRK15177 70 ARMMASLYGLDGDEFSHF---CYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAA 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 359351306 181 ITSLRDTEHMTILlsSHQLEEVQSVCDRVGLFYRGKL 217
Cdd:PRK15177 147 LACQLQQKGLIVL--THNPRLIKEHCHAFGVLLHGKI 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-209 |
9.30e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 23 VDDISLTLNKGEIFGLLGPNGSGKTTTILMLLGLL--EPTSGSVDILGfdplrTPLEVKR---------------RVGY- 84
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDG-----KEVDVSTvsdaidaglayvtedRKGYg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 85 --LSDTVGFYDTMTayeNLDYTARFLGLSakERRERILGALQRMRLENRKND---KVHTFSHGMKQRLGLAEVLVKNCEI 159
Cdd:NF040905 351 lnLIDDIKRNITLA---NLGKVSRRGVID--ENEEIKVAEEYRKKMNIKTPSvfqKVGNLSGGNQQKVVLSKWLFTDPDV 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 359351306 160 AILDEPTQGLDPESVAEFLSLITSLRDTEHMTILLSShQLEEVQSVCDRV 209
Cdd:NF040905 426 LILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISS-ELPELLGMCDRI 474
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
95-209 |
1.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359351306 95 MTAYEnldytARFLGLSAKERRERIlGALQRMRLENRKNDK-VHTFSHGMKQRLGLA-EVL--VKNCEIAILDEPTQGLD 170
Cdd:PRK00635 771 MTAYE-----AEKFFLDEPSIHEKI-HALCSLGLDYLPLGRpLSSLSGGEIQRLKLAyELLapSKKPTLYVLDEPTTGLH 844
|
90 100 110
....*....|....*....|....*....|....*....
gi 359351306 171 PESVAEFLSLITSLRDTEHmTILLSSHQLEEVQsVCDRV 209
Cdd:PRK00635 845 THDIKALIYVLQSLTHQGH-TVVIIEHNMHVVK-VADYV 881
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
146-214 |
1.34e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 1.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359351306 146 RLGLAEVLVKNCEIAILDEPTQGLDPESVAE----FLSLITSLRDTEHMTILLSSH--QLEEVQSVCDRVGLFYR 214
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESlahaLVEIIKSRSQQRNFQLLVITHdeDFVELLGRSEYVEKFYR 1287
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
129-202 |
2.19e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 2.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359351306 129 ENRKNDKVHTFSHGMKQRLGLAEVLVKNCE---IAILDEPTQGLDPESVAEFLSLITSLRDTEHmTILLSSHQLEEV 202
Cdd:pfam13304 227 GGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGA-QLILTTHSPLLL 302
|
|
| |
