|
Name |
Accession |
Description |
Interval |
E-value |
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-333 |
0e+00 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 536.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFTAYSSRPGLKGAFRDLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPGLKGALKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNGMNPHKQREEFVRTIGVVFGQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQR 163
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVVFGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 164 MRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLD 243
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 244 NLRTQWGVEKEIHFQFVAPVSYQELSmvmpdSHVVWSKAKEENAWVAKIPNEEViiSMLISKVVQAFQIKDLKINEVSTE 323
Cdd:COG4586 241 ELKERFGPYKTIVLELAEPVPPLELP-----RGGEVIEREGNRVRLEVDPRESL--AEVLARLLARYPVRDLTIEEPPIE 313
|
330
....*....|
gi 488042473 324 EIIRNIYEEG 333
Cdd:COG4586 314 EVIRRIYKEG 323
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-240 |
3.50e-131 |
|
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: 373.59 E-value: 3.50e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFTAYSSRPGLKGAFRDLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMNPHKQREEFVRTIGVVFGQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRM 164
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 165 RCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
31-248 |
1.39e-86 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 260.38 E-value: 1.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFgQRSQL 110
Cdd:COG1131 6 LTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP-QEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:COG1131 85 YPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 191 LVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQ 248
Cdd:COG1131 165 EARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
31-250 |
4.46e-73 |
|
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: 226.28 E-value: 4.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSqL 110
Cdd:COG4555 7 LSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDERG-L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:COG4555 86 YDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 191 LVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQWG 250
Cdd:COG4555 166 MARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
31-246 |
1.98e-62 |
|
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: 197.98 E-value: 1.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSqL 110
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLS-V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 191 LVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLR 246
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
31-236 |
4.06e-62 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 195.69 E-value: 4.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFgQRSQL 110
Cdd:cd03230 6 LSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP-EEPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFrllkkvygvsdaqykehmehvietldigplldkpvrKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:cd03230 85 YENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488042473 191 LVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:cd03230 129 ESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-246 |
4.08e-60 |
|
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: 191.95 E-value: 4.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrpglkgafrdllnrNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:cd03263 1 LQIRNLTKTY-------------------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMNPHKQREEFVRTIGVVFgQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRM 164
Cdd:cd03263 62 NGYSIRTDRKAARQSLGYCP-QFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 165 RCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMneRYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDN 244
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
..
gi 488042473 245 LR 246
Cdd:cd03263 219 LK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
39-276 |
7.76e-59 |
|
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: 191.45 E-value: 7.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSqLWWDIAVQE 118
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYAS-VDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRE 198
Cdd:TIGR01188 86 NLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 199 FLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQWG---VEKEIHFQFVAPVSYQELSMVMPDS 275
Cdd:TIGR01188 166 YIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGkdtLESRPRDIQSLKVEVSMLIAELGET 244
|
.
gi 488042473 276 H 276
Cdd:TIGR01188 245 G 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-240 |
1.47e-58 |
|
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: 187.96 E-value: 1.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 22 GLKGAFRDllnrNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIG 101
Cdd:cd03266 6 ALTKRFRD----VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 102 VVFGQRSqLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFL 181
Cdd:cd03266 82 FVSDSTG-LYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 182 DEPTIGLDVLVKLKIREFLKEMNERYKtTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
38-241 |
3.45e-54 |
|
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: 177.14 E-value: 3.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPH-KQREEFVRTIGVVFgQ--RSQL---- 110
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGLVF-QnpDDQLfapt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 -WWDIAvqesFRLLKkvYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:COG1122 93 vEEDVA----FGPEN--LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488042473 190 VLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:COG1122 167 PRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-333 |
1.05e-53 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 177.99 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQR------EEfvrtigv 102
Cdd:COG4152 7 LTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLDPEDRRrigylpEE------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 103 vfgqRSqLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:COG4152 80 ----RG-LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 183 EPTIGLD-VLVKLkIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQWGVEKeihFQFVA 261
Cdd:COG4152 155 EPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNT---LRLEA 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 262 PVSYQELSMVmPDSHVVwskAKEENAWVAKIPNEEViISMLISKVVQAFQIKDLKINEVSTEEIIRNIYEEG 333
Cdd:COG4152 230 DGDAGWLRAL-PGVTVV---EEDGDGAELKLEDGAD-AQELLRALLARGPVREFEEVRPSLNEIFIEVVGEK 296
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-245 |
1.76e-53 |
|
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: 183.18 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFTAYSSRPglkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGG----------------VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNGMN----PHKQREEFVRTIGVVFgQ--RSQL--WWDIA--VQESFRLLKkvyGVSDAQYKEHMEHVIETLDIGP-LLD 152
Cdd:COG1123 324 FDGKDltklSRRSLRELRRRVQMVF-QdpYSSLnpRMTVGdiIAEPLRLHG---LLSRAERRERVAELLERVGLPPdLAD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 153 KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLD 232
Cdd:COG1123 400 RYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMY 479
|
250
....*....|...
gi 488042473 233 EGNIMYDGSLDNL 245
Cdd:COG1123 480 DGRIVEDGPTEEV 492
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
31-329 |
4.49e-52 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 174.19 E-value: 4.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVfGQRSQL 110
Cdd:TIGR03522 8 LTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYL-PEHNPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:TIGR03522 87 YLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTTGLDP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 191 LVKLKIREFLKEMNEryKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQwGVEKEIHFQFVAPVSYQELSM 270
Cdd:TIGR03522 167 NQLVEIRNVIKNIGK--DKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAA-NKKQVIEVEFEEQIDLQLFET 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 271 VmpdSHVVWSKAKEENAW-VAKIPNEEVIISMLISKVVQAFQIKDLKINEVSTEEIIRNI 329
Cdd:TIGR03522 244 L---EEISSVKNTGGNTWkLTFETPNDTRPEIFKLAQQKGLKLISLQQNEKNLEQVFREI 300
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-236 |
4.60e-51 |
|
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: 168.82 E-value: 4.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrpglkgafrdllNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:cd03255 1 IELKNLSKTY-----------------GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMNPHK----QREEFVR-TIGVVFgQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLS 159
Cdd:cd03255 64 DGTDISKlsekELAAFRRrHIGFVF-QSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 160 LGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDItDIEALCERVIMLDEGNI 236
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
39-234 |
3.60e-49 |
|
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: 163.79 E-value: 3.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQR-EEFVRTIGVVFgQ--RSQL----- 110
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVGLVF-QnpDDQFfgptv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAvqesFRLLKkvYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:cd03225 94 EEEVA----FGLEN--LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 191 LVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:cd03225 168 AGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
31-240 |
1.61e-48 |
|
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: 162.00 E-value: 1.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQrEEFVRTIGV------VF 104
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGAlieapgFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 105 GQRSqlwwdiaVQESFRLLKKVYGVSDaqyKEHMEhVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:cd03268 85 PNLT-------ARENLRLLARLLGIRK---KRIDE-VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 185 TIGLDVLVKLKIREFLKEMNErYKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
40-240 |
2.08e-48 |
|
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: 161.59 E-value: 2.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGeMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVV---FGQRSQlwwdIAV 116
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLpqeFGVYPN----FTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:cd03264 90 REFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 197 REFLKEMNEryKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03264 170 RNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-243 |
1.84e-47 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 160.25 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTAYSSRPG-LKGAFRDLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTS 79
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHEPSRsLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 80 GQITVN-----------GMNPhkqreEF-----VRTIGVvfgqrsqlwwdiavqesfrllkkVYGVSDAQYKEHMEHVIE 143
Cdd:COG1134 81 GRVEVNgrvsallelgaGFHP-----ELtgrenIYLNGR-----------------------LLGLSRKEIDEKFDEIVE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 144 TLDIGPLLDKPVRKLSLGQRMRceLA-AALIH-NPPLLFLDEptiGL---DVLVKLKIREFLKEMNERyKTTILLTTHDI 218
Cdd:COG1134 133 FAELGDFIDQPVKTYSSGMRAR--LAfAVATAvDPDILLVDE---VLavgDAAFQKKCLARIRELRES-GRTVIFVSHSM 206
|
250 260
....*....|....*....|....*
gi 488042473 219 TDIEALCERVIMLDEGNIMYDGSLD 243
Cdd:COG1134 207 GAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
39-256 |
3.18e-47 |
|
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: 159.82 E-value: 3.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQ-REEFVRTIGVVFgQRSQLWWDIAVQ 117
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLsRRELARRIAYVP-QEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRL----LKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:COG1120 94 ELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQ 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 194 LKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS----L--DNLRTQWGVEKEIH 256
Cdd:COG1120 174 LEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPpeevLtpELLEEVYGVEARVI 242
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
38-248 |
3.44e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.48 E-value: 3.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQReefvRTIGVVfGQRSQLWWD--IA 115
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR----RRIGYV-PQRAEVDWDfpIT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQE-----------SFRLLKKvygvsdaQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:COG1121 94 VRDvvlmgrygrrgLFRRPSR-------ADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488042473 185 TIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGnIMYDGSLDNLRTQ 248
Cdd:COG1121 167 FAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTP 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
38-240 |
2.18e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 156.75 E-value: 2.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFV----RTIGVVFgqrsqlwwd 113
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylrRRIGVVF--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 iavQEsFRLL--KKVY----------GVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFL 181
Cdd:COG2884 86 ---QD-FRLLpdRTVYenvalplrvtGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 182 DEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-246 |
3.06e-46 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 157.27 E-value: 3.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFTAYSSRpglkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRR-----------------VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMN-PHKQREEFVRTIGVVFgQ--------RSQLWWDIAvqESFRLLKKvygvsdAQYKEHMEHVIETLDIGP-LLDKP 154
Cdd:COG1124 65 DGRPvTRRRRKAFRRRVQMVF-QdpyaslhpRHTVDRILA--EPLRIHGL------PDREERIAELLEQVGLPPsFLDRY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 155 VRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:COG1124 136 PHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
|
250
....*....|..
gi 488042473 235 NIMYDGSLDNLR 246
Cdd:COG1124 216 RIVEELTVADLL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-241 |
5.56e-46 |
|
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: 156.74 E-value: 5.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFtayssrpglkGAFRdllnrnykivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG0411 1 SDPLLEVRGLTKRF----------GGLV-----------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNG-----MNPHK----------QR---------EEFVRtIGVVFGQRSQLWWDIavqesFRLLKkvYGVSDAQYKE 136
Cdd:COG0411 60 RILFDGrditgLPPHRiarlgiartfQNprlfpeltvLENVL-VAAHARLGRGLLAAL-----LRLPR--ARREEREARE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 137 HMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTH 216
Cdd:COG0411 132 RAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEH 211
|
250 260
....*....|....*....|....*
gi 488042473 217 DITDIEALCERVIMLDEGNIMYDGS 241
Cdd:COG0411 212 DMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-240 |
6.69e-46 |
|
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: 155.74 E-value: 6.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFTAYSSRpglkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-----------------VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNGMN----PHKQREEFVRTIGVVFgQ------------RSQLWwdiavqESFRLLKKVYGVSDAQ--YKEHMEHVIETL 145
Cdd:cd03257 64 FDGKDllklSRRLRKIRRKEIQMVF-QdpmsslnprmtiGEQIA------EPLRIHGKLSKKEARKeaVLLLLVGVGLPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 146 DIgplLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALC 225
Cdd:cd03257 137 EV---LNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIA 213
|
250
....*....|....*
gi 488042473 226 ERVIMLDEGNIMYDG 240
Cdd:cd03257 214 DRVAVMYAGKIVEEG 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
35-234 |
2.80e-45 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 153.59 E-value: 2.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 35 YKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnpHKQREEFVRTIGVVFGQRSqLWWDI 114
Cdd:cd03269 10 FGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNRIGYLPEERG-LYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV---- 190
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPvnve 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 191 LVKLKIREfLKEMNerykTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:cd03269 166 LLKDVIRE-LARAG----KTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
31-240 |
3.68e-45 |
|
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: 153.44 E-value: 3.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKqreefvRTIGVVFG 105
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgVPPER------RNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSqLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:cd03259 80 DYA-LFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 186 IGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
35-240 |
5.19e-45 |
|
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: 151.82 E-value: 5.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 35 YKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVfgqrSQlwwd 113
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV----PQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 iavqesfrllkkvygvsdaqykehmehVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488042473 194 LKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-236 |
9.80e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.50 E-value: 9.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTayssrpglKGAFRdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG1136 1 MSPLLELRNLTKSYG--------TGEGE---------VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMN----PHKQREEF-VRTIGVVFgQRSQLwwdIA---VQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLD 152
Cdd:COG1136 64 EVLIDGQDisslSERELARLrRRHIGFVF-QFFNL---LPeltALENVALPLLLAGVSRKERRERARELLERVGLGDRLD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 153 KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD------VLvklkirEFLKEMNERYKTTILLTTHDiTDIEALCE 226
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeeVL------ELLRELNRELGTTIVMVTHD-PELAARAD 212
|
250
....*....|
gi 488042473 227 RVIMLDEGNI 236
Cdd:COG1136 213 RVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
31-234 |
1.28e-43 |
|
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: 148.10 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN---PHKQREEFVRTIGVVFgQR 107
Cdd:cd03229 6 VSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdLEDELPPLRRRIGMVF-QD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 108 SQLWwdiavqesfrllkkvygvsdaqykEHMEhVIETLDIGplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:cd03229 85 FALF------------------------PHLT-VLENIALG---------LSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488042473 188 LDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:cd03229 131 LDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
1.36e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.63 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFtayssrPGLKGAfrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG1116 4 AAPALELRGVSKRF------PTGGGG-----------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMNPHKQREEfvrtIGVVFgqrsqlwwdiavQEsFRLL--KKVY----------GVSDAQYKEHMEHVIETLDIG 148
Cdd:COG1116 67 EVLVDGKPVTGPGPD----RGVVF------------QE-PALLpwLTVLdnvalglelrGVPKAERRERARELLELVGLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 149 PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITdiEA--LCE 226
Cdd:COG1116 130 GFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVD--EAvfLAD 207
|
....*...
gi 488042473 227 RVIMLDEG 234
Cdd:COG1116 208 RVVVLSAR 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-247 |
2.30e-43 |
|
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: 149.36 E-value: 2.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKeftAYSSRPGLKgafrdllnrnykivpavnDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG1127 2 SEPMIEVRNLTK---SFGDRVVLD------------------GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMN----PHKQREEFVRTIGVVFgQRSQLWWDIAVQE--SFRLLKKvYGVSDAQYKEHMEHVIETLDIGPLLDKP 154
Cdd:COG1127 61 EILVDGQDitglSEKELYELRRRIGMLF-QGGALFDSLTVFEnvAFPLREH-TDLSEAEIRELVLEKLELVGLPGAADKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 155 VRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250
....*....|...
gi 488042473 235 NIMYDGSLDNLRT 247
Cdd:COG1127 219 KIIAEGTPEELLA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-247 |
8.73e-43 |
|
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: 147.97 E-value: 8.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrpglkGAFRdllnrnykivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT- 83
Cdd:cd03219 1 LEVRGLTKRF----------GGLV-----------ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLf 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 ----VNGMNPHkqreEFVRT-IGVVFgQRSQLWWDIAVQE----------SFRLLKKVYGVSDAQYKEHMEHVIETLDIG 148
Cdd:cd03219 60 dgedITGLPPH----EIARLgIGRTF-QIPRLFPELTVLEnvmvaaqartGSGLLLARARREEREARERAEELLERVGLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 149 PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERV 228
Cdd:cd03219 135 DLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRV 213
|
250
....*....|....*....
gi 488042473 229 IMLDEGNIMYDGSLDNLRT 247
Cdd:cd03219 214 TVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
41-185 |
3.65e-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: 143.56 E-value: 3.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRT-IGVVFgQRSQLWWDIAVQES 119
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKeIGYVF-QDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 120 FRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRK----LSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
39-239 |
3.76e-42 |
|
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: 145.37 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEfvrtIGVVfGQRSQLWWD--IAV 116
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR----IGYV-PQRRSIDRDfpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QE-------SFRLLKKVYGVSDaqyKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:cd03235 88 RDvvlmglyGHKGLFRRLSKAD---KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488042473 190 VLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYD 239
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-243 |
1.30e-41 |
|
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: 151.59 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTAyssrpglkgafrdllnrnyKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPT-- 78
Cdd:COG1123 1 MTPLLEVRDLSVRYPG-------------------GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgr 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 79 -SGQITVNGMNPHKQREEF-VRTIGVVFGQ-RSQL-----WWDIAvqESFRLLkkvyGVSDAQYKEHMEHVIETLDIGPL 150
Cdd:COG1123 62 iSGEVLLDGRDLLELSEALrGRRIGMVFQDpMTQLnpvtvGDQIA--EALENL----GLSRAEARARVLELLEAVGLERR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 151 LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIM 230
Cdd:COG1123 136 LDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
250
....*....|...
gi 488042473 231 LDEGNIMYDGSLD 243
Cdd:COG1123 216 MDDGRIVEDGPPE 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
43-233 |
1.48e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 143.77 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVfGQRSQLWWDIAVQESFRL 122
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL-GHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 123 LKKVYGVSDAQykEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKE 202
Cdd:COG4133 99 WAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170 180 190
....*....|....*....|....*....|.
gi 488042473 203 MNERyKTTILLTTHDitDIEALCERVIMLDE 233
Cdd:COG4133 177 HLAR-GGAVLLTTHQ--PLELAAARVLDLGD 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-240 |
3.17e-41 |
|
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: 143.44 E-value: 3.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFTAYSSRPG-LKGAFRDLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:cd03220 1 IELENVSKSYPTYKGGSSsLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VN-----------GMNPhkqreefvrtigvvfgqrsqlwwDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLD 152
Cdd:cd03220 81 VRgrvssllglggGFNP-----------------------ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFID 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 153 KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLtTHDITDIEALCERVIMLD 232
Cdd:cd03220 138 LPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILV-SHDPSSIKRLCDRALVLE 216
|
....*...
gi 488042473 233 EGNIMYDG 240
Cdd:cd03220 217 KGKIRFDG 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
31-234 |
2.05e-40 |
|
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: 139.30 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVFGqrsq 109
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 110 lwwdiavqesfrllkkvygvsdaqykehmehvietldigplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488042473 190 VLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:cd00267 113 PASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-245 |
2.31e-39 |
|
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: 138.87 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFTAyssrpglkgafrdllnrNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:cd03258 1 MIELKNVSKVFGD-----------------TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNGMN----PHKQREEFVRTIGVVFgQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLS 159
Cdd:cd03258 64 VDGTDltllSGKELRKARRRIGMIF-QHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 160 LGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYD 239
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
....*.
gi 488042473 240 GSLDNL 245
Cdd:cd03258 223 GTVEEV 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
33-247 |
4.51e-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: 138.68 E-value: 4.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 33 RNYKIVpaVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQiTVngmnphkqreefvrtigVVFGQRSQLW- 111
Cdd:COG1119 13 RGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN-DV-----------------RLFGERRGGEd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 -WDI---------AVQESFRLLKKV--------YG-------VSDAQyKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRC 166
Cdd:COG1119 73 vWELrkriglvspALQLRFPRDETVldvvlsgfFDsiglyrePTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 167 ELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLR 246
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
.
gi 488042473 247 T 247
Cdd:COG1119 232 T 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-247 |
7.14e-39 |
|
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: 137.63 E-value: 7.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKeftAYSSRPGLKGafrdllnrnykivpavndVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:cd03261 1 IELRGLTK---SFGGRTVLKG------------------VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMNPH----KQREEFVRTIGVVFgQRSQLWWDIAVQE--SFRLLKKvYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKL 158
Cdd:cd03261 60 DGEDISglseAELYRLRRRMGMLF-QSGALFDSLTVFEnvAFPLREH-TRLSEEEIREIVLEKLEAVGLRGAEDLYPAEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 159 SLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMY 238
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
....*....
gi 488042473 239 DGSLDNLRT 247
Cdd:cd03261 218 EGTPEELRA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-231 |
7.18e-39 |
|
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: 137.22 E-value: 7.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrPGLKGAfrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:cd03293 1 LEVRNVSKTY------GGGGGA-----------VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGM---NPHKQReefvrtiGVVFGQRSQLWWdIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLG 161
Cdd:cd03293 64 DGEpvtGPGPDR-------GYVFQQDALLPW-LTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 162 QRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITdiEA--LCERVIML 231
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDID--EAvfLADRVVVL 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
41-255 |
1.50e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 138.78 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmNPHKQREEFVRT-IGVVfGQRSQLWWDIAVQES 119
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQrVGVV-PQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 120 FRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREF 199
Cdd:PRK13537 101 LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 200 LKEMNERYKtTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLrtqwgVEKEI 255
Cdd:PRK13537 181 LRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL-----IESEI 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
31-237 |
4.21e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 138.67 E-value: 4.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT-----VNGMNPHKqreefvRTIGVVFg 105
Cdd:COG3839 9 VSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdVTDLPPKD------RNIAMVF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSQLWWDIAVQE--SFRLlkKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:COG3839 82 QSYALYPHMTVYEniAFPL--KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488042473 184 PTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIM 237
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
31-237 |
9.84e-38 |
|
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: 133.92 E-value: 9.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQREefvRTIGVVFgQRS 108
Cdd:cd03301 6 VTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdVTDLPPKD---RDIAMVF-QNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 109 QLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 189 DVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIM 237
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
31-245 |
1.12e-37 |
|
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: 134.59 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKQREefvrtIGVVF- 104
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditkLPMHKRAR-----LGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 105 GQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 185 TIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-240 |
3.19e-37 |
|
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: 132.80 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKqGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----------MNPHKqreefvRTIGVVFgQRSQLW 111
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinLPPQQ------RKIGLVF-QQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 WDIAVQES--FRLLKKvygvSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:cd03297 88 PHLNVRENlaFGLKRK----RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488042473 190 VLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-261 |
4.30e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.00 E-value: 4.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTAyssrpglkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG3842 2 AMPALELENVSKRYGD---------------------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNG-----MNPHKqreefvRTIGVVFgQRSQLW-----WD-IAvqesFRLlkKVYGVSDAQYKEHMEHVIETLDIGP 149
Cdd:COG3842 61 RILLDGrdvtgLPPEK------RNVGMVF-QDYALFphltvAEnVA----FGL--RMRGVPKAEIRARVAELLELVGLEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 150 LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVI 229
Cdd:COG3842 128 LADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIA 207
|
250 260 270
....*....|....*....|....*....|....*.
gi 488042473 230 MLDEGNIMydgsldnlrtQWGVEKEIHFQ----FVA 261
Cdd:COG3842 208 VMNDGRIE----------QVGTPEEIYERpatrFVA 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
39-245 |
1.52e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 131.65 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQRE-EFVRTIGVVFgQRSQLWWDIAVQ 117
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPvELRRKIGYVI-QQIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRLLKKVYGVSDAQYKEHMEHVIETLDIGP--LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:cd03295 94 ENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488042473 196 IREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:cd03295 174 LQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-238 |
4.25e-36 |
|
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: 132.48 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFtaySSRPGlkgafrdllnrnykIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSG 80
Cdd:COG0444 1 LLEVRNLKVYF---PTRRG--------------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMN----PHKQREEF-VRTIGVVFgQ------------RSQLwwdiavQESFRLLKKVYGvsdaqyKEHMEHVIE 143
Cdd:COG0444 64 EILFDGEDllklSEKELRKIrGREIQMIF-QdpmtslnpvmtvGDQI------AEPLRIHGGLSK------AEARERAIE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 144 TLDI-GplLDKPVRK-------LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTT 215
Cdd:COG0444 131 LLERvG--LPDPERRldrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFIT 208
|
250 260
....*....|....*....|...
gi 488042473 216 HDITDIEALCERVImldegnIMY 238
Cdd:COG0444 209 HDLGVVAEIADRVA------VMY 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
36-234 |
2.75e-35 |
|
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: 126.34 E-value: 2.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 36 KIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEFVRTIGVVFgqrsqlwwdi 114
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlRDLDLESLRKNIAYVP---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 avQESFrllkkvygvsdaqykehmehvietldigpLLDKPVRK--LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:cd03228 83 --QDPF-----------------------------LFSGTIREniLSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488042473 193 KLKIREFLKEMNEryKTTILLTTHDITDIEaLCERVIMLDEG 234
Cdd:cd03228 132 EALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
40-241 |
6.87e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.43 E-value: 6.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQRE---EFVRTIGVVFGQRSQLWWDIAV 116
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESVGMVFQDPDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488042473 197 REFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
33-245 |
8.79e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 129.57 E-value: 8.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 33 RNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEFVRtIGVVfGQRSQLW 111
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvPARARLARAR-IGVV-PQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 WDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:PRK13536 127 LEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488042473 192 VKLKIREFLKEMNERYKtTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK13536 207 ARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
30-237 |
8.96e-35 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 127.61 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 30 LLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPhKQREEFVRTIGVVF 104
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqLDR-KQRRAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 105 -------GQRSQLWWDIAvqESFRLLKKVygvSDAQYKEHMEHVIETLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNP 176
Cdd:TIGR02769 95 qdspsavNPRMTVRQIIG--EPLRHLTSL---DESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 177 PLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIM 237
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
42-236 |
9.34e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 9.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKQReefvRTIGVVFgQRSQlWWDIAV 116
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsaMPPPEWR----RQVAYVP-QEPA-LWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLlkkVYGVSDAQY-KEHMEHVIETLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKL 194
Cdd:COG4619 91 RDNLPF---PFQLRERKFdRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488042473 195 KIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:COG4619 168 RVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
38-245 |
1.67e-34 |
|
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: 126.53 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRT----IGVVF--------- 104
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqIGMIFqqfnlierl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 105 -----------GQRSqLWWDIavqesFRLLKKvygvsdaQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALI 173
Cdd:cd03256 94 svlenvlsgrlGRRS-TWRSL-----FGLFPK-------EEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 174 HNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
39-251 |
1.90e-34 |
|
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: 133.42 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVFgQRSQLW------ 111
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVL-QDVFLFsgtire 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 ----WDIAVQESfRLLK--KVYGVSDaqykehmehVIETLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFL 181
Cdd:COG2274 568 nitlGDPDATDE-EIIEaaRLAGLHD---------FIEALPMG--YDTVVgeggSNLSGGQRQRLAIARALLRNPRILIL 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 182 DEPTIGLDVLVKLKIREFLKEMneRYKTTILLTTHDITDIeALCERVIMLDEGNIMYDGSLDNLRTQWGV 251
Cdd:COG2274 636 DEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
39-245 |
2.84e-34 |
|
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: 131.81 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVR-TIGVVfGQRSQLWwDIAVQ 117
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRrRIAVV-PQRPHLF-DTTLR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRLLKKvyGVSDAQykehMEHVIETLDIGPL-------LDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:COG4987 427 ENLRLARP--DATDEE----LWAALERVGLGDWlaalpdgLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 187 GLDVLVKLKI-REFLKEMNERyktTILLTTHDITDIEAlCERVIMLDEGNIMYDGSLDNL 245
Cdd:COG4987 501 GLDAATEQALlADLLEALAGR---TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-245 |
3.40e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.34 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrpglkGAFRdllnrnykivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:COG1118 3 IEVRNISKRF----------GSFT-----------LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NG------MNPHKqreefvRTIGVVFgQRSQLWWDIAVQE--SFRLlkKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVR 156
Cdd:COG1118 62 NGrdlftnLPPRE------RRVGFVF-QHYALFPHMTVAEniAFGL--RVRPPSKAEIRARVEELLELVQLEGLADRYPS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 157 KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
....*....
gi 488042473 237 MYDGSLDNL 245
Cdd:COG1118 213 EQVGTPDEV 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
31-244 |
4.28e-34 |
|
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: 125.14 E-value: 4.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKqreefvRTIGVVFg 105
Cdd:cd03299 6 LSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnLPPEK------RDISYVP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 186 IGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDN 244
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
40-241 |
4.51e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQR---EEFVRTIGVVFG-QRSQLWW--- 112
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQyPEYQLFEeti 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 --DIAVQESFRllkkvyGVSDAQYKEHMEHVIET--LDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK13637 102 ekDIAFGPINL------GLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488042473 189 DVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-245 |
1.79e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 125.96 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrPGLKGAfrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:COG1135 2 IELENLSKTF------PTKGGP-----------VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMN----PHKQREEFVRTIGVVFgqrsqlwwdiavqESFRLL--KKVY----------GVSDAQYKehmEHVIETLDIG 148
Cdd:COG1135 65 DGVDltalSERELRAARRKIGMIF-------------QHFNLLssRTVAenvalpleiaGVPKAEIR---KRVAELLELV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 149 PLLDK----PvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD------VLvklkirEFLKEMNERYKTTILLTTHDI 218
Cdd:COG1135 129 GLSDKadayP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettrsIL------DLLKDINRELGLTIVLITHEM 201
|
250 260
....*....|....*....|....*..
gi 488042473 219 TDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:COG1135 202 DVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
39-245 |
1.08e-32 |
|
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: 127.57 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRT-IGVVfGQRSQLwwdIA-- 115
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRqIAWV-PQNPYL---FAgt 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRLLKKvyGVSDAQYKE-----HMEHVIETLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:COG4988 427 IRENLRLGRP--DASDEELEAaleaaGLDEFVAALPDG--LDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 187 GLDV----LVKLKIREFLKEmnerykTTILLTTHDITDIeALCERVIMLDEGNIMYDGSLDNL 245
Cdd:COG4988 503 HLDAeteaEILQALRRLAKG------RTVILITHRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
38-236 |
1.29e-32 |
|
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: 120.59 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFV----RTIGVVFgQRSQLWWD 113
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylrRKIGVVF-QDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488042473 194 LKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:cd03292 173 WEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
32-236 |
4.52e-32 |
|
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: 118.90 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 32 NRNYKIVpavNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQReefVRTIGVVFgQ--RS 108
Cdd:cd03226 10 KKGTEIL---DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPiKAKER---RKSIGYVM-QdvDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 109 QLWWDiAVQESFRLLKKVYGvsdaQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:cd03226 83 QLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 189 DVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:cd03226 158 DYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
45-245 |
9.68e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.70 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 45 SFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKqreefvRTIGVVFgQRSQLWWDIAVQE- 118
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltaLPPAE------RPVSMLF-QENNLFPHLTVAQn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 -------SFRLlkkvygvSDAQyKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:COG3840 92 iglglrpGLKL-------TAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488042473 192 VKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:COG3840 164 LRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
40-245 |
1.01e-31 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 118.75 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGM---NPHKQReefvRTIGVVFgQRSQLWWDIAV 116
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQdatRVHARD----RKIGFVF-QHYALFKHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:TIGR00968 90 RDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 197 REFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:TIGR00968 170 RSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-216 |
3.31e-31 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 124.08 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFtayssrpglkGAFrdllnrnykivPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:NF033858 266 AIEARGLTMRF----------GDF-----------TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNG--MNPH----KQReefVrtigvvfGQRSQ---LWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKP 154
Cdd:NF033858 325 LFGqpVDAGdiatRRR---V-------GYMSQafsLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADAL 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 155 VRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD---------VLVKLKIREflkemneryKTTILLTTH 216
Cdd:NF033858 395 PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvardmfwrLLIELSRED---------GVTIFISTH 456
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-243 |
7.03e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 123.05 E-value: 7.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 11 RKEFTAYSSRPGLKGA--FRDLlNRNYK--IVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG 86
Cdd:TIGR03375 448 RPEGTRFLHRPRLQGEieFRNV-SFAYPgqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 87 MNPHK-QREEFVRTIGVVfGQRSQLWwdiavQESFR--LLKKVYGVSDAQykehmehVIETLDIGPL----------LDK 153
Cdd:TIGR03375 527 VDIRQiDPADLRRNIGYV-PQDPRLF-----YGTLRdnIALGAPYADDEE-------ILRAAELAGVtefvrrhpdgLDM 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 154 PV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNEryKTTILLTTHDITDIEaLCERVI 229
Cdd:TIGR03375 594 QIgergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLD-LVDRII 670
|
250
....*....|....
gi 488042473 230 MLDEGNIMYDGSLD 243
Cdd:TIGR03375 671 VMDNGRIVADGPKD 684
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-236 |
1.68e-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: 120.94 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFtayssrPGLKGAFRdllnRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGiLTPTSGQIT 83
Cdd:COG4172 275 LLEARDLKVWF------PIKRGLFR----RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNGMN----PHKQREEFVRTIGVVF-------------GQrsqlwwdIaVQESFRLLKKvyGVSDAqykEHMEHVIETL- 145
Cdd:COG4172 344 FDGQDldglSRRALRPLRRRMQVVFqdpfgslsprmtvGQ-------I-IAEGLRVHGP--GLSAA---ERRARVAEALe 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 146 DIGplLDKPVR-----KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITD 220
Cdd:COG4172 411 EVG--LDPAARhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAV 488
|
250
....*....|....*.
gi 488042473 221 IEALCERVIMLDEGNI 236
Cdd:COG4172 489 VRALAHRVMVMKDGKV 504
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-246 |
2.45e-30 |
|
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: 114.84 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEFVRtIGVVF-GQRS 108
Cdd:cd03224 6 LNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERAR-AGIGYvPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 109 QLWWDIAVQESFRLlkKVYGVSDAQYKEHMEHVietLDIGPLL----DKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:cd03224 85 RIFPELTVEENLLL--GAYARRRAKRKARLERV---YELFPRLkerrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 185 TIGLD-VLVKlKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLR 246
Cdd:cd03224 160 SEGLApKIVE-EIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-245 |
3.37e-30 |
|
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: 114.74 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrpglkGAFrdllnrnykivPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:cd03296 3 IEVRNVSKRF----------GDF-----------VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMNPHKQ--REefvRTIGVVFgQRSQLWWDIAVQES----FRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKL 158
Cdd:cd03296 62 GGEDATDVpvQE---RNVGFVF-QHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 159 SLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMY 238
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
....*..
gi 488042473 239 DGSLDNL 245
Cdd:cd03296 218 VGTPDEV 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-241 |
3.82e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 114.74 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 3 SVIEVQGLRKeftAYSSRPglkgafrdllnrnykivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQI 82
Cdd:COG1137 2 MTLEAENLVK---SYGKRT------------------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 83 TVNGMN----P-HkqreefvrtigvvfgQRSQL-----------WWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLD 146
Cdd:COG1137 61 FLDGEDithlPmH---------------KRARLgigylpqeasiFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 147 IGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRE---FLKEMNerykTTILLTTHDITDIEA 223
Cdd:COG1137 126 ITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKiirHLKERG----IGVLITDHNVRETLG 201
|
250
....*....|....*...
gi 488042473 224 LCERVIMLDEGNIMYDGS 241
Cdd:COG1137 202 ICDRAYIISEGKVLAEGT 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
41-248 |
4.13e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.51 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKqREEFVRTIGVVFgQRSQLWWDIAVQESF 120
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQRDICMVF-QSYALFPHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 121 RLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFL 200
Cdd:PRK11432 100 GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 201 KEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQ 248
Cdd:PRK11432 180 RELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
41-236 |
4.38e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.55 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK----QREEFVRTIGVVF-------GQRSQ 109
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDIQMVFqdsisavNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 110 LWWDIAvqESFRLLKkvyGVSDAQYKEHMEHVIETLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK10419 108 VREIIR--EPLRHLL---SLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 189 DVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
41-256 |
5.77e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.87 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVfGQRSQLWWDIAVQES 119
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVL-PQHSSLSFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 120 FRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALI------HNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK13548 97 VAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 194 LKIREFLKEMNERYKTTILLTTHDItDIEAL-CERVIMLDEGNIMYDGS------LDNLRTQWGVEKEIH 256
Cdd:PRK13548 177 HHVLRLARQLAHERGLAVIVVLHDL-NLAARyADRIVLLHQGRLVADGTpaevltPETLRRVYGADVLVQ 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
39-261 |
1.60e-29 |
|
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: 112.72 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-----PHKqreefvRTIGVVFgQRSQLWWD 113
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHK------RPVNTVF-QNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:cd03300 87 LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 194 LKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMydgsldnlrtQWGVEKEIHFQ----FVA 261
Cdd:cd03300 167 KDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ----------QIGTPEEIYEEpanrFVA 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-241 |
2.36e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEFVRTIGVVfGQRSQLWWDIAVQES 119
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlAAWSPWELARRRAVL-PQHSSLAFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 120 FRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAAL--IHNPP-----LLFLDEPTIGLDVLV 192
Cdd:COG4559 96 VALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdggprWLFLDEPTSALDLAH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488042473 193 KLKIREFLKEMNERyKTTILLTTHDItDIEAL-CERVIMLDEGNIMYDGS 241
Cdd:COG4559 176 QHAVLRLARQLARR-GGGVVAVLHDL-NLAAQyADRILLLHQGRLVAQGT 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-242 |
2.38e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFtayssrPGlkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG1129 1 AEPLLEMRGISKSF------GG---------------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNG-----MNPHKQREefvRTIGVVFgQRSQLWWDIAVQES-F--RLLKKvYGVSD-----AQYKEHMEHVieTLDI 147
Cdd:COG1129 60 EILLDGepvrfRSPRDAQA---AGIAIIH-QELNLVPNLSVAENiFlgREPRR-GGLIDwramrRRARELLARL--GLDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 148 GPllDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL-----DVLVKLkIREfLKEMNerykTTILLTTHDITDIE 222
Cdd:COG1129 133 DP--DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLterevERLFRI-IRR-LKAQG----VAIIYISHRLDEVF 204
|
250 260
....*....|....*....|
gi 488042473 223 ALCERVImldegnIMYDGSL 242
Cdd:COG1129 205 EIADRVT------VLRDGRL 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-240 |
2.60e-29 |
|
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: 111.82 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNpHKQREEFVRTIGVVFgQRSQLWWDIAVQESFRL 122
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD-VTAAPPADRPVSMLF-QENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 123 lkkvyGVS-----DAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIR 197
Cdd:cd03298 94 -----GLSpglklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488042473 198 EFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
42-240 |
2.92e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG------MNPHKQREEFVRTIGVVFGQRSQLWwdiA 115
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigyLPQEPPLDDDLTVLDTVLDGDAELR---A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRLLKKVYGVSDAQYK------EHMEH------------VIETLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNP 176
Cdd:COG0488 92 LEAELEELEAKLAEPDEDLErlaelqEEFEAlggweaearaeeILSGLGFPEeDLDRPVSELSGGWRRRVALARALLSEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 177 PLLFLDEPTIGLDVLVKLKIREFLKemneRYKTTILLTTHDITDIEALCERVIMLDEGNI-MYDG 240
Cdd:COG0488 172 DLLLLDEPTNHLDLESIEWLEEFLK----NYPGTVLVVSHDRYFLDRVATRILELDRGKLtLYPG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
5-261 |
4.52e-29 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 114.75 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrpglkGAFRdllnrnykivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:TIGR03265 5 LSIDNIRKRF----------GAFT-----------ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMN----PHKQREefvrtIGVVFgQRSQLWWDIAVQESFrllkkVYGVSDAQYK--EHMEHVIETLDIGPLLD---KPV 155
Cdd:TIGR03265 64 GGRDitrlPPQKRD-----YGIVF-QSYALFPNLTVADNI-----AYGLKNRGMGraEVAERVAELLDLVGLPGserKYP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 156 RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGN 235
Cdd:TIGR03265 133 GQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGV 212
|
250 260 270
....*....|....*....|....*....|
gi 488042473 236 IMydgsldnlrtQWGVEKEIHFQ----FVA 261
Cdd:TIGR03265 213 IE----------QVGTPQEIYRHpatpFVA 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-237 |
6.27e-29 |
|
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: 112.35 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtaySSRPG------LKGAFRDLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPT 78
Cdd:cd03294 1 IKIKGLYKIF---GKNPQkafkllAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 79 SGQITVNGMNPHKQREEFVR-----TIGVVFgQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDK 153
Cdd:cd03294 78 SGKVLIDGQDIAAMSRKELRelrrkKISMVF-QSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 154 PVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDE 233
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
....
gi 488042473 234 GNIM 237
Cdd:cd03294 237 GRLV 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-237 |
1.32e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 110.60 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 3 SVIEVQGLRKEFTAYSSRpglkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQI 82
Cdd:COG4181 7 PIIELRGLTKTVGTGAGE-----------------LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 83 TVNGMNPHKQREEFV-----RTIGVVFgqrsqlwwdiavqESFRL------LKKVY------GVSDAQykEHMEHVIETL 145
Cdd:COG4181 70 RLAGQDLFALDEDARarlraRHVGFVF-------------QSFQLlptltaLENVMlplelaGRRDAR--ARARALLERV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 146 DIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIeALC 225
Cdd:COG4181 135 GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARC 213
|
250
....*....|..
gi 488042473 226 ERVIMLDEGNIM 237
Cdd:COG4181 214 DRVLRLRAGRLV 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
39-241 |
1.35e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.62 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRT-IGVVFGQRSQLWWDIAVQ 117
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKkIGIIFQNPDNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 E--SFRLLKKVygVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:PRK13632 103 DdiAFGLENKK--VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488042473 196 IREFLKEMNERYKTTILLTTHDITDIeALCERVIMLDEGNIMYDGS 241
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-240 |
1.84e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.52 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFtayssrPGLKGAFRdllnRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:COG4608 7 LLEVRDLKKHF------PVRGGLFG----RTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNGMN----PHKQREEFVRTIGVVF-------------GQrsqlwwdiAVQESFRllkkVYGVSDAqyKEHMEHVIETLD 146
Cdd:COG4608 77 FDGQDitglSGRELRPLRRRMQMVFqdpyaslnprmtvGD--------IIAEPLR----IHGLASK--AERRERVAELLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 147 IGPL----LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIE 222
Cdd:COG4608 143 LVGLrpehADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVR 222
|
250
....*....|....*...
gi 488042473 223 ALCERVImldegnIMYDG 240
Cdd:COG4608 223 HISDRVA------VMYLG 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
41-264 |
3.32e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.10 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmNPHKQ--REEFVRTIGVVfGQRSQLWWDIAVQE 118
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD-KPISMlsSRQLARRLALL-PQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 sfrLLKkvYGVS---------DAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:PRK11231 96 ---LVA--YGRSpwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 190 VLVKLKIREFLKEMNERYKTTILLtTHDITDIEALCERVIMLDEGNIMYDGSLDN------LRTQWGVEKEIHFQfvaPV 263
Cdd:PRK11231 171 INHQVELMRLMRELNTQGKTVVTV-LHDLNQASRYCDHLVVLANGHVMAQGTPEEvmtpglLRTVFDVEAEIHPE---PV 246
|
.
gi 488042473 264 S 264
Cdd:PRK11231 247 S 247
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-234 |
3.99e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 107.13 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFTAyssrpglkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:cd03216 1 LELRGITKRFGG---------------------VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGmnphkQREEFvrtigvvfgqrsqlwwdiavqesfrllkkvYGVSDAQykehmEHVIETldigplldkpVRKLSLGQRM 164
Cdd:cd03216 60 DG-----KEVSF------------------------------ASPRDAR-----RAGIAM----------VYQLSVGERQ 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 165 RCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-236 |
4.45e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 108.41 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 34 NYKIVPAvnDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNpHKQREEFVRTIGVVFgQRSQLWWD 113
Cdd:TIGR01277 9 EYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS-HTGLAPYQRPVSMLF-QENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:TIGR01277 85 LTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488042473 194 LKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
40-245 |
1.33e-27 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 107.84 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP----TSGQITVNGM--NPHKQREEFVRTI--------GVVFG 105
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRplLPLSIRGRHIATImqnprtafNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSQLwwdiavQESFRLLKKVYGVSDAQYKEHMEHVieTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:TIGR02770 81 MGNHA------IETLRSLGKLSKQARALILEALEAV--GLPDPEeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 185 TIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
40-240 |
1.75e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.41 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQR---------EEFV------------- 97
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKktkekekvlEKLViqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 98 ---RTIGVVFGQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIG-PLLDKPVRKLSLGQRMRCELAAALI 173
Cdd:PRK13651 102 eirRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 174 HNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKtTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
39-240 |
1.88e-27 |
|
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: 105.86 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVfGQRSqlwwdiavqe 118
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL-NQRP---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 sfrllkkvygvsdaqykehmeHVIETldigPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI-R 197
Cdd:cd03247 85 ---------------------YLFDT----TLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLlS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488042473 198 EFLKEMNERyktTILLTTHDITDIEALcERVIMLDEGNIMYDG 240
Cdd:cd03247 140 LIFEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-240 |
1.97e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.56 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMnphKQREEFV----RTIGVVFGQRSQLWWDI 114
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVwdvrRQVGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQE--SFRLLKKvyGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK13635 98 TVQDdvAFGLENI--GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 193 KLKIREFLKEMNERYKTTILLTTHDItDIEALCERVIMLDEGNIMYDG 240
Cdd:PRK13635 176 RREVLETVRQLKEQKGITVLSITHDL-DEAAQADRVIVMNKGEILEEG 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-245 |
2.27e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.29 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVN----GMNPHKQREEfvRTIGVVfGQ 106
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdediSLLPLHARAR--RGIGYL-PQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 107 RSQLWWDIAVQESFR-LLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK10895 86 EASIFRRLSVYDNLMaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 186 IGLDVLVKLKIREFLKEMNErYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
40-218 |
2.73e-27 |
|
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: 105.97 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQRE---EFVRTIGVVFGQRSQ------L 110
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKgllERRQRVGLVFQDPDDqlfaadV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAvqesFRLLKkvYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:TIGR01166 87 DQDVA----FGPLN--LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*...
gi 488042473 191 LVKLKIREFLKEMNERyKTTILLTTHDI 218
Cdd:TIGR01166 161 AGREQMLAILRRLRAE-GMTVVISTHDV 187
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
39-231 |
3.29e-27 |
|
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: 111.61 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEFVRTIGVVfGQRSQLWWDiAVQ 117
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADADADSWRDQIAWV-PQHPFLFAG-TIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRLLKKvyGVSDAQYKEHMEHV-----IETLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:TIGR02857 414 ENIRLARP--DASDAEIREALERAgldefVAALPQG--LDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488042473 189 D----VLVKLKIREFlkeMNERyktTILLTTHDITDIEaLCERVIML 231
Cdd:TIGR02857 490 DaeteAEVLEALRAL---AQGR---TVLLVTHRLALAA-LADRIVVL 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-234 |
3.67e-27 |
|
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: 106.36 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTayssrpglkgafrdLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG4778 1 MTTLLEVENLSKTFT--------------LHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNgmnphkQREEFV---------------RTIGVVfgqrSQ----------LwwDIaVQESFRLLkkvyGVSDAQYK 135
Cdd:COG4778 67 SILVR------HDGGWVdlaqaspreilalrrRTIGYV----SQflrviprvsaL--DV-VAEPLLER----GVDREEAR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 136 EHMEHVIETLDIGPLL-DKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERyKTTILLT 214
Cdd:COG4778 130 ARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGI 208
|
250 260
....*....|....*....|
gi 488042473 215 THDITDIEALCERVIMLDEG 234
Cdd:COG4778 209 FHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-248 |
4.15e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.58 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 28 RDLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQR-EEFVRTIGVVFGQ 106
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 107 RSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:PRK13652 87 PDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 187 GLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQ 248
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
46-246 |
8.52e-27 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 105.32 E-value: 8.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 46 FTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQReefvRTIGVVfGQRSQLWWDIAVQesfrllkk 125
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGW----RHIGYV-PQRHEFAWDFPIS-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 126 VYGVSDAQYKEHM--------------EHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:TIGR03771 68 VAHTVMSGRTGHIgwlrrpcvadfaavRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 192 VKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDeGNIMYDGSLDNLR 246
Cdd:TIGR03771 148 TQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQ 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-241 |
8.74e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.57 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFtayssrPGLKGAFRDLLNRNYkivpAVNDVSFTIKQGEMVGYIGENGAGKSTT-IKMLTgiLTPTSGQI 82
Cdd:PRK15134 275 LLDVEQLQVAF------PIRKGILKRTVDHNV----VVKNISFTLRPGETLGLVGESGSGKSTTgLALLR--LINSQGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 83 TVNGMNPH----KQREEFVRTIGVVFGQ-RSQLWWDIAVQ----ESFRLLKKVygVSDAQYKEHMEHVIEtlDIGplLDK 153
Cdd:PRK15134 343 WFDGQPLHnlnrRQLLPVRHRIQVVFQDpNSSLNPRLNVLqiieEGLRVHQPT--LSAAQREQQVIAVME--EVG--LDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 154 PVR-----KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERV 228
Cdd:PRK15134 417 ETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
|
250
....*....|...
gi 488042473 229 IMLDEGNIMYDGS 241
Cdd:PRK15134 497 IVLRQGEVVEQGD 509
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
39-217 |
9.37e-27 |
|
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: 110.53 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSQLwWDIAVQE 118
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL-FDTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKvyGVSDAQYKEHMEHV-----IETLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:TIGR02868 428 NLRLARP--DATDEELWAALERVgladwLRALPDG--LDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*....
gi 488042473 190 VLVKLK-IREFLKEMNERyktTILLTTHD 217
Cdd:TIGR02868 504 AETADElLEDLLAALSGR---TVVLITHH 529
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
31-236 |
1.10e-26 |
|
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: 104.92 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGM---NPHKQREEFVRTIGVVFgQR 107
Cdd:cd03262 6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltDDKKNINELRQKVGMVF-QQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 108 SQLWWDIAVQESFRL-LKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:cd03262 85 FNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488042473 187 GLDVLVklkIREFLKEMNE--RYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:cd03262 165 ALDPEL---VGEVLDVMKDlaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
38-240 |
1.19e-26 |
|
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: 104.98 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNpHKQREEFV--RTIGVVfGQRSQLWW--- 112
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD-IRQLDPADlrRNIGYV-PQDVTLFYgtl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 --DIAvqesfrllkkvYGVSDAQYKEHMEhVIETLDIGPL-------LDKPV----RKLSLGQRMRCELAAALIHNPPLL 179
Cdd:cd03245 95 rdNIT-----------LGAPLADDERILR-AAELAGVTDFvnkhpngLDLQIgergRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 180 FLDEPTIGLDVLVKLKIREFLKEMNEryKTTILLTTHDiTDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHR-PSLLDLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
39-236 |
1.34e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnpHKQREEFV----RTIGVVFGQRSQLWWDI 114
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVwdirHKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQE--SFRLLKKvyGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK13650 98 TVEDdvAFGLENK--GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 193 KLKIREFLKEMNERYKTTILLTTHDITDIeALCERVIMLDEGNI 236
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-241 |
1.44e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 107.58 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFTAYSsrpglkgafrdllnrnyKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:PRK11153 1 MIELKNISKVFPQGG-----------------RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNGMN----PHKQREEFVRTIGVVFgqrsqlwwdiavqESFRLL--KKVY----------GVSDAQYKehmEHVIETLDI 147
Cdd:PRK11153 64 VDGQDltalSEKELRKARRQIGMIF-------------QHFNLLssRTVFdnvalplelaGTPKAEIK---ARVTELLEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 148 GPLLDKPVR---KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEAL 224
Cdd:PRK11153 128 VGLSDKADRypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRI 207
|
250
....*....|....*..
gi 488042473 225 CERVIMLDEGNIMYDGS 241
Cdd:PRK11153 208 CDRVAVIDAGRLVEQGT 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
31-236 |
2.02e-26 |
|
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: 104.57 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGIL-----TPTSGQITVNGMN---PHKQREEFVRTIGV 102
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiydLDVDVLELRRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 103 VFGQRSQLwwDIAVQESFRLLKKVYGVSDAqyKEHMEHVIETLDIGPLLDK-----PVRKLSLGQRMRCELAAALIHNPP 177
Cdd:cd03260 86 VFQKPNPF--PGSIYDNVAYGLRLHGIKLK--EELDERVEEALRKAALWDEvkdrlHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 178 LLFLDEPTIGLDVLVKLKIREFLKEMNERYktTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-245 |
2.21e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.66 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 45 SFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNpHKQREEFVRTIGVVFgQRSQLWWDIAVQESFRL-- 122
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLF-QENNLFSHLTVAQNIGLgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 123 ---LKkvygVSDAQyKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREF 199
Cdd:PRK10771 97 npgLK----LNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488042473 200 LKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
39-239 |
2.42e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 105.94 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKQReefvRTIGVVFgQRSQLW-- 111
Cdd:COG1125 16 VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGedirdLDPVELR----RRIGYVI-QQIGLFph 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 WDIA-----VQesfRLLkkvyGVSDAQYKEHMEHVIET--LDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:COG1125 91 MTVAeniatVP---RLL----GWDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 185 TIGLDVLVKLKIREFLKEMNERYKTTILLTTHDItDiEA--LCERVIMLDEGNIM-YD 239
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDI-D-EAlkLGDRIAVMREGRIVqYD 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-243 |
2.79e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 2 KSVIEVQGLRKeftAYSSRPGLKgafrdllnrnykivpavnDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQ 81
Cdd:COG0488 313 KKVLELEGLSK---SYGDKTLLD------------------DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 82 ITVnGMNphkqreefVRtIGVvFGQRsqlwwdiavQESFRLLKKVYG-VSDAQYKEHMEHVIETLdiGPLL------DKP 154
Cdd:COG0488 372 VKL-GET--------VK-IGY-FDQH---------QEELDPDKTVLDeLRDGAPGGTEQEVRGYL--GRFLfsgddaFKP 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 155 VRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDvlvkLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:COG0488 430 VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDG 505
|
250
....*....|
gi 488042473 235 NI-MYDGSLD 243
Cdd:COG0488 506 GVrEYPGGYD 515
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
42-244 |
3.35e-26 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 103.59 E-value: 3.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK----QREEFV-RTIGVVFgQRSQLWWDIAV 116
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssnERAKLRnKKLGFIY-QFHHLLPDFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:TIGR02211 101 LENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKII 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 197 REFLKEMNERYKTTILLTTHDITDIEALcERVImldegnIMYDGSLDN 244
Cdd:TIGR02211 181 FDLMLELNRELNTSFLVVTHDLELAKKL-DRVL------EMKDGQLFN 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
35-246 |
5.56e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.52 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 35 YKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQR-EEFVRtIGV--------VFG 105
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIAR-LGIgyvpegrrIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSqlwwdiaVQESFRLlkKVYGVSD-AQYKEHMEHVietLDIGPLL----DKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:COG0410 92 SLT-------VEENLLL--GAYARRDrAEVRADLERV---YELFPRLkerrRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 181 LDEPTIGLD-VLVKlKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLR 246
Cdd:COG0410 160 LDEPSLGLApLIVE-EIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-240 |
1.13e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.47 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 17 YSSRPGLKGAFRDLLNrnykivpavnDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP--TSGQITVNGMNPHKQre 94
Cdd:cd03213 11 VTVKSSPSKSGKQLLK----------NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 95 EFVRTIGVVfgqrsqlwwdiaVQESFrllkkvygvsdaqykeHMEH--VIETLDIGPLLdkpvRKLSLGQRMRCELAAAL 172
Cdd:cd03213 79 SFRKIIGYV------------PQDDI----------------LHPTltVRETLMFAAKL----RGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 173 IHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKtTILLTTHDI-TDIEALCERVIMLDEGNIMYDG 240
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
39-256 |
1.36e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVFgqrsqlwwdiavQ 117
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVP------------Q 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESF----------RLLKKvyGVSDAQYKE-----HMEHVIETLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPL 178
Cdd:COG1132 422 DTFlfsgtireniRYGRP--DATDEEVEEaakaaQAHEFIEALPDG--YDTVVgergVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 179 LFLDEPTIGLDVLVKLKIREFLKEMNERyKTTIL----LTThdITDiealCERVIMLDEGNIMYDGSLDNLRTQWGVEKE 254
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMKG-RTTIViahrLST--IRN----ADRILVLDDGRIVEQGTHEELLARGGLYAR 570
|
..
gi 488042473 255 IH 256
Cdd:COG1132 571 LY 572
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
44-236 |
3.28e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.39 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREE-----FVRTIGVVFgQRSQLWWDIAVQE 118
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraklRAKHVGFVF-QSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRE 198
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 488042473 199 FLKEMNERYKTTILLTTHDITdIEALCERVIMLDEGNI 236
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHDLQ-LAARCDRRLRLVNGQL 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-245 |
3.41e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.20 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVFgQRSQLwWDIAVQ 117
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVF-QDAGL-FNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRLlkkvyGVSDAQYKEHMEHV--------IETLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK13657 427 DNIRV-----GRPDATDEEMRAAAeraqahdfIERKPDG--YDTVVgergRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 186 IGLDVLVKLKIREFLKE-MNERyktTILLTTHDITDI-EAlcERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK13657 500 SALDVETEAKVKAALDElMKGR---TTFIIAHRLSTVrNA--DRILVFDNGRVVESGSFDEL 556
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-239 |
3.58e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.09 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 5 IEVQGLRKEFtayssrpglkgaFRDLLNRNYkivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV 84
Cdd:COG1101 2 LELKNLSKTF------------NPGTVNEKR----ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 85 NGMNPHKQReEFVRT--IGVVF-----------------------GQRSQLwwdiavqeSFRLLKKVYgvsdAQYKEHme 139
Cdd:COG1101 66 DGKDVTKLP-EYKRAkyIGRVFqdpmmgtapsmtieenlalayrrGKRRGL--------RRGLTKKRR----ELFREL-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 140 hvIETLDIGpL---LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTH 216
Cdd:COG1101 131 --LATLGLG-LenrLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTH 207
|
250 260
....*....|....*....|...
gi 488042473 217 DITDIEALCERVIMLDEGNIMYD 239
Cdd:COG1101 208 NMEQALDYGNRLIMMHEGRIILD 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
40-245 |
5.66e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 5.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEFVRTI----GVVFG-QRSQLWWD 113
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITiTHKTKDKYIRPVrkriGMVFQfPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 iAVQESFRLLKKVYGVSDAQYKEHMEHVIetLDIG---PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 191 LVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
38-224 |
5.86e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.48 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG---MNPHKQReefvrtiGVVFGQRSQLWWdI 114
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvTGPGADR-------GVVFQKDALLPW-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKL 194
Cdd:COG4525 92 NVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180 190
....*....|....*....|....*....|
gi 488042473 195 KIREFLKEMNERYKTTILLTTHDITdiEAL 224
Cdd:COG4525 172 QMQELLLDVWQRTGKGVFLITHSVE--EAL 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
35-236 |
8.08e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.19 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 35 YKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MN---PHKqreefvRTIGVVFgQRSQ 109
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrMNdvpPAE------RGVGMVF-QSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 110 LWWDIAVQE--SFRLlkKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK11000 86 LYPHLSVAEnmSFGL--KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 188 LDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
40-241 |
8.56e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.31 E-value: 8.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmNPHKQRE----EFVRTIGVVFGQRSQLWWDIA 115
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKYDKksllEVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488042473 196 IREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13639 176 IMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
33-240 |
1.05e-24 |
|
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: 99.65 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 33 RNYKIVpaVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGQITVNGMNPHkqREEFVRTIGVVfGQRSQ 109
Cdd:cd03234 17 NKYARI--LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK--PDQFQKCVAYV-RQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 110 LWWDIAVQES------FRLLKKVygvSDAQYKEHMEHVIET-LDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:cd03234 92 LLPGLTVRETltytaiLRLPRKS---SDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 183 EPTIGLDVLVKLKIREFLKEMNERYKtTILLTTHDIT-DIEALCERVIMLDEGNIMYDG 240
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNR-IVILTIHQPRsDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
42-234 |
1.23e-24 |
|
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: 97.13 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnphkqreefvrtiGVVFGQRSQLwwdiavqesfr 121
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------TVKIGYFEQL----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 122 llkkvygvsdaqykehmehvietldigplldkpvrklSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLK 201
Cdd:cd03221 72 -------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|...
gi 488042473 202 EmnerYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:cd03221 115 E----YPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
41-234 |
1.31e-24 |
|
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: 99.85 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnphKQREEFVRTIGVVFGQRSQLWWDIAVQESF 120
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG----KQITEPGPDRMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 121 RLLKKV-YGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREF 199
Cdd:TIGR01184 77 LAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 488042473 200 LKEMNERYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
39-236 |
2.75e-24 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 97.29 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQ-REEFVRTIGVVfgqrsqlwwdiavq 117
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDHVGYL-------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 esfrllkkvygvsdaqykehMEHVIetldigpLLDKPVRK--LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:cd03246 82 --------------------PQDDE-------LFSGSIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488042473 196 IREFLKEMNERYKTTILLtTHDITDIEAlCERVIMLDEGNI 236
Cdd:cd03246 135 LNQAIAALKAAGATRIVI-AHRPETLAS-ADRILVLEDGRV 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
42-243 |
4.14e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.98 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQItVNGMNP-HKQREEfvrtIGVVFgqrsqlwwdiavQESf 120
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPlAEARED----TRLMF------------QDA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 121 RLL--KKV-----YGVSdAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK11247 91 RLLpwKKVidnvgLGLK-GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488042473 194 LKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLD 243
Cdd:PRK11247 170 IEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
38-252 |
7.26e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPH-KQREEFVRTIGVVfGQRSQLWWDIAV 116
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASV-PQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKV----YGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK09536 95 RQVVEMGRTPhrsrFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 193 KLKIREFLKEMNERYKTTIlLTTHDITDIEALCERVIMLDEGNIMYDG------SLDNLRTQWGVE 252
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAV-AAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAFDAR 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
8.93e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.64 E-value: 8.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFtayssrPGLKgafrdllnrnykivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG3845 2 MPPALELRGITKRF------GGVV---------------ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNG-----MNPHKQREefvRTIGVVF-------------------GQRSQLWWDIAvqesfRLLKKVYGVSDaQYKe 136
Cdd:COG3845 61 EILIDGkpvriRSPRDAIA---LGIGMVHqhfmlvpnltvaenivlglEPTKGGRLDRK-----AARARIRELSE-RYG- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 137 hmehvietLDIGPllDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTiglDVLVKLKIREFLKEMnERYK---TTILL 213
Cdd:COG3845 131 --------LDVDP--DAKVEDLSVGEQQRVEILKALYRGARILILDEPT---AVLTPQEADELFEIL-RRLAaegKSIIF 196
|
250
....*....|....*
gi 488042473 214 TTHDITDIEALCERV 228
Cdd:COG3845 197 ITHKLREVMAIADRV 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
40-246 |
9.73e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 97.75 E-value: 9.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT-----VNGMNPHK-QREEFVRTIgvvfgQRSQLWWD 113
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhIEGLPGHQiARMGVVRTF-----QHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESFR--------------LLK-KVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPL 178
Cdd:PRK11300 95 MTVIENLLvaqhqqlktglfsgLLKtPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 179 LFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLR 246
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
39-255 |
1.37e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.24 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQRE--EFVRTIGVVF-GQRSQLWWDIa 115
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFqNPDNQIVATI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 196 IREFLKEMNERYKTTILLTTHDITD-IEAlcERVIMLDEGNIMYDGSLDNLRTQWGVEKEI 255
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITHYMEEaVEA--DRIIVMDSGKVVMEGTPKEIFKEVEMMKKI 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
40-241 |
1.40e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.17 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV------NGMNPhKQREEFVRTIGVVFgQ--RSQLW 111
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKN-KKLKPLRKKVGIVF-QfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 wDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK13634 100 -EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488042473 191 LVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
35-231 |
1.61e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 35 YKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMnphkqreefvRTIGVVFgQRSQLWWD- 113
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVP-QRSEVPDSl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 -IAVQESFRL----LKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:NF040873 71 pLTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488042473 189 DVLVKLKIREFLKEMNERyKTTILLTTHDITDIeALCERVIML 231
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
40-240 |
1.70e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.88 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRT-IGVVFGQ------RSQLWW 112
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkVGLVFQDpddqvfSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAvqesFRLLKKvyGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK13647 100 DVA----FGPVNM--GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 193 KLKIREFLKEMNERYKtTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:PRK13647 174 QETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
39-256 |
2.14e-23 |
|
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: 96.53 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnpHKQRE----EFVRTIGVVfGQRSQLWWDi 114
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---HDVRDytlaSLRRQIGLV-SQDVFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFRllkkvYGVSDAQYKE--------HMEHVIETLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:cd03251 91 TVAENIA-----YGRPGATREEveeaaraaNAHEFIMELPEG--YDTVIgergVKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488042473 183 EPTIGLDVLVKLKIREFLKEMNERyKTTILLtTHDITDIEAlCERVIMLDEGNIMYDGSLDNLRTQWGVEKEIH 256
Cdd:cd03251 164 EATSALDTESERLVQAALERLMKN-RTTFVI-AHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
38-236 |
2.65e-23 |
|
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: 96.00 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSQLWWDiAVQ 117
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 E--SFRLLKKVYG-VSDAQYKEHMEHVIETLDIGPLLDKPVR--KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:cd03248 106 DniAYGLQSCSFEcVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 193 KLKIREFLKEMNERykTTILLTTHDITDIEAlCERVIMLDEGNI 236
Cdd:cd03248 186 EQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
44-230 |
5.25e-23 |
|
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: 94.48 E-value: 5.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIgVVFGQRSQLWWDIAVQESFRLL 123
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-LYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 124 KKVYGvsdaqyKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEM 203
Cdd:cd03231 98 HADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170 180
....*....|....*....|....*..
gi 488042473 204 NERYKTTILLTTHDITDIEALCERVIM 230
Cdd:cd03231 172 CARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
31-241 |
5.43e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.98 E-value: 5.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNpHKQREEFVRTIGVVFgQRSQL 110
Cdd:PRK11607 25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINMMF-QSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK11607 103 FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488042473 191 LVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK11607 183 KLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
37-264 |
7.27e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 97.10 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 37 IVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGQITVNGMN----PHKQ----REEfvrTIGVVFG 105
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREilnlPEKElnklRAE---QISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 Q-RSQLWWDIAVQESFR---LLKKVYGVSDAqykehMEHVIETLDI--GPLLDKPVR----KLSLGQRMRCELAAALIHN 175
Cdd:PRK09473 105 DpMTSLNPYMRVGEQLMevlMLHKGMSKAEA-----FEESVRMLDAvkMPEARKRMKmyphEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 176 PPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVImldegnIMYDGsldnlRT-QWGVEKE 254
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL------VMYAG-----RTmEYGNARD 248
|
250
....*....|
gi 488042473 255 IHFQFVAPVS 264
Cdd:PRK09473 249 VFYQPSHPYS 258
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-253 |
1.89e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.26 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLrkEFtAYSSRPGlkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:TIGR00958 475 LEGLIEFQDV--SF-SYPNRPD---------------VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMnPHKQRE-EFVRTIGVVFGQRSQLW-----WDIAVQESFRLLKKVYGVSDA----QYKEHMEHVIETlDIGPl 150
Cdd:TIGR00958 537 QVLLDGV-PLVQYDhHYLHRQVALVGQEPVLFsgsvrENIAYGLTDTPDEEIMAAAKAanahDFIMEFPNGYDT-EVGE- 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 151 ldkPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVlvklKIREFLKEMNERYKTTILLTTHDITDIEAlCERVIM 230
Cdd:TIGR00958 614 ---KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILV 685
|
250 260
....*....|....*....|...
gi 488042473 231 LDEGNIMYDGSLDNLRTQWGVEK 253
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
40-236 |
2.58e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.40 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFV----RTIGVVFgQRSQLWWDIA 115
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflrRQIGMIF-QDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRLLKKVYGVSDAQYKehmEHVIETLDIGPLLDK----PVrKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIR---RRVSAALDKVGLLDKaknfPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488042473 192 VKLKIREFLKEMNeRYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK10908 172 LSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
36-250 |
2.65e-22 |
|
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: 93.44 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 36 KIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRT-IGVVFgQRSQLWWDi 114
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSmIGVVL-QDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFRllkkvYGVSDAQYKE--------HMEHVIETLDIGplLDKPVRK----LSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:cd03254 92 TIMENIR-----LGRPNATDEEvieaakeaGAHDFIMKLPNG--YDTVLGEnggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 183 EPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEAlcERVIMLDEGNIMYDGSLDNLRTQWG 250
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMKG-RTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-250 |
2.66e-22 |
|
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: 98.16 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVV--FGQRSQLwwdIAV 116
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCpqFDAIDDL---LTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:TIGR01257 2030 REHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488042473 197 REFLKEMnERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQWG 250
Cdd:TIGR01257 2110 WNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-234 |
3.27e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.90 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmNPHK---QREEFVRTIGVVFgQRSQLWWDI 114
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-QEMRfasTTAALAAGVAIIY-QELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFRL--LKKVYGVSDaqYKEHMEHVIETL-----DIGPllDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK11288 95 TVAENLYLgqLPHKGGIVN--RRLLNYEAREQLehlgvDIDP--DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488042473 188 L-----DVLVKLkIREFLKEmneryKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:PRK11288 171 LsareiEQLFRV-IRELRAE-----GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-250 |
3.28e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.20 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSQLWWDiAVQE 118
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKvyGVSDaqykEHMEHVIETLDIGPLL--DKPV--------RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK11160 433 NLLLAAP--NASD----EALIEVLQQVGLEKLLedDKGLnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 189 DVLVKLKIREFLKE-MNERyktTILLTTHDITDIEALcERVIMLDEGNIMYDGSLDNLRTQWG 250
Cdd:PRK11160 507 DAETERQILELLAEhAQNK---TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
38-241 |
3.51e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTS---GQITVNGMNPHKQREEFVR-TIGVVFGQRSQLWWD 113
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIReKVGIVFQNPDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 194 LKIREFLKEMNERYKTTILLTTHDItDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDI-DEANMADQVLVLDDGKLLAQGS 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-240 |
4.38e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG------MNPH-KQREEFVRTIGVV 103
Cdd:PRK11124 8 INCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSdKAIRELRRNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 104 FgQRSQLWWDIAVQESfrLLK---KVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:PRK11124 88 F-QQYNLWPHLTVQQN--LIEapcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 181 LDEPTIGLDVLVKLKIREFLKEMNERYKTTILLtTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIV-THEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
38-236 |
5.56e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.91 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT-----VNGMNPhkqREefvRTIGVVFgQRSQLWW 112
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvVNELEP---AD---RDIAMVF-QNYALYP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLD-KPvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDvl 191
Cdd:PRK11650 90 HMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDrKP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD-- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 192 VKLKI--REFLKEMNERYKTTILLTTHDitDIEA--LCERVIMLDEGNI 236
Cdd:PRK11650 167 AKLRVqmRLEIQRLHRRLKTTSLYVTHD--QVEAmtLADRVVVMNGGVA 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
42-236 |
8.03e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.38 E-value: 8.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK--QREefvRTIGVVFgQRSQLWWDIAVQE- 118
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhARD---RKVGFVF-QHYALFRHMTVFDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 -SF--RLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:PRK10851 95 iAFglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488042473 196 IREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK10851 175 LRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
31-243 |
9.56e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 92.59 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN---------PHKQREEFVRT-I 100
Cdd:TIGR02323 9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqlSEAERRRLMRTeW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 101 GVVF-----GQRSQLWWDIAVQEsfRLL---KKVYGVSDAQYKEHMEHVieTLDIGPLLDKPvRKLSLGQRMRCELAAAL 172
Cdd:TIGR02323 89 GFVHqnprdGLRMRVSAGANIGE--RLMaigARHYGNIRATAQDWLEEV--EIDPTRIDDLP-RAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 173 IHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLD 243
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTD 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-241 |
9.71e-22 |
|
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: 96.62 E-value: 9.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVfGQRSQLWWDIAVQE 118
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC-PQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRE 198
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488042473 199 FLkeMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:TIGR01257 1103 LL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
43-232 |
1.08e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.80 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQI-----TVNGMNPHKQREEFVRTIGVVFgQRSQLWWDIAVQ 117
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqPMSKLSSAAKAELRNQKLGFIY-QFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIR 197
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*
gi 488042473 198 EFLKEMNERYKTTILLTTHDITDIEALCERVIMLD 232
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
38-240 |
1.68e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN----PHKQREEFvrTIGVVFgQRSQLWWD 113
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynklDHKLAAQL--GIGIIY-QELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESF---RLL-KKVYGVSDAQYKEHMEHVIETLDIGPL---LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:PRK09700 95 LTVLENLyigRHLtKKVCGVNIIDWREMRVRAAMMLLRVGLkvdLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 187 GL-----DVLVkLKIREFLKEmneryKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:PRK09700 175 SLtnkevDYLF-LIMNQLRKE-----GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
39-245 |
2.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNP--HKQREEFVRTIGVVFGQRSQLWWDIAV 116
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 197 REFLKEMNERYKtTILLTTHDITDIEAlCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK13644 176 LERIKKLHEKGK-TIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
39-234 |
2.27e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.30 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGM---NPHKQReefvrtiGVVFGQRSQLWWDiA 115
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpveGPGAER-------GVVFQNEGLLPWR-N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 488042473 196 IREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-245 |
3.87e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.34 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 33 RNYKIVpaVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGQITVNGM--NPHKQRE--EFVRTIGVVFG 105
Cdd:TIGR00955 35 RPRKHL--LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMpiDAKEMRAisAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 Q---RSQLwwdiAVQESFRLLKKVYgvsdaqYKEHMEHVIETLDIGPLLD---------KPVRKLSLGQRMRCELAAALI 173
Cdd:TIGR00955 113 TltvREHL----MFQAHLRMPRRVT------KKEKRERVDEVLQALGLRKcantrigvpGRVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 174 HNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKtTILLTTHDIT-DIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHQPSsELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-240 |
5.00e-21 |
|
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: 93.71 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 28 RDLLNRNYKI----VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVngmnphKQREEFV------ 97
Cdd:TIGR03269 283 RNVSKRYISVdrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV------RVGDEWVdmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 98 --------RTIGVVFGQRS---------QLWWDIAVQ--ESFRLLKKVYGVSDAQYKEHMEHVIetldigplLDKPVRKL 158
Cdd:TIGR03269 357 pdgrgrakRYIGILHQEYDlyphrtvldNLTEAIGLElpDELARMKAVITLKMVGFDEEKAEEI--------LDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 159 SLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMY 238
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
..
gi 488042473 239 DG 240
Cdd:TIGR03269 509 IG 510
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
42-236 |
8.15e-21 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 89.31 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPH----KQREEFVRTIGVVFGQRSQLWWDIA-- 115
Cdd:TIGR02982 22 FDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHgaskKQLVQLRRRIGYIFQAHNLLGFLTArq 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 -VQESFRLLKkvyGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKL 194
Cdd:TIGR02982 102 nVQMALELQP---NLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 195 KIREFLKEMNERYKTTILLTTHD--ITDIealCERVIMLDEGNI 236
Cdd:TIGR02982 179 DVVELMQKLAKEQGCTILMVTHDnrILDV---ADRILQMEDGKL 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
38-259 |
8.28e-21 |
|
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: 93.24 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnpHKQREEFVRTIGVVFGQRSQ--LWWDIA 115
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG---HDLADYTLASLRRQVALVSQdvVLFNDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRllkkvYG----VSDAQYKE-----HMEHVIETLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:TIGR02203 422 IANNIA-----YGrteqADRAEIERalaaaYAQDFVDKLPLG--LDTPIgengVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 183 EPTIGLDVLVKLKIREFLKE-MNERyktTILLTTHDITDIEAlCERVIMLDEGNIMYDGSLDNLRTQWGVEKEIH-FQF 259
Cdd:TIGR02203 495 EATSALDNESERLVQAALERlMQGR---TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARNGLYAQLHnMQF 569
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-232 |
1.76e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.01 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnpHKQREEFVRTIGVVFGQRSQLWWDIAVQESFRL 122
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHRNAMKPALTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 123 LKKVYGvsdaQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV-LVKLkireFLK 201
Cdd:PRK13539 97 WAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaAVAL----FAE 168
|
170 180 190
....*....|....*....|....*....|...
gi 488042473 202 EMNERYKT--TILLTTHdiTDIEALCERVIMLD 232
Cdd:PRK13539 169 LIRAHLAQggIVIAATH--IPLGLPGARELDLG 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
39-241 |
1.97e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 88.44 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVfGQRSQLWWDiAVQ 117
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV-PQDTVLFND-TIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRllkkvYGVSDAQykehMEHVIETLDIGPLLDKPVR--------------KLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:cd03253 93 YNIR-----YGRPDAT----DEEVIEAAKAAQIHDKIMRfpdgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 184 PTIGLDVLVKLKIREFLKEMNERyKTTILLtTHDITDIeALCERVIMLDEGNIMYDGS 241
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSKG-RTTIVI-AHRLSTI-VNADKIIVLKDGRIVERGT 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
40-257 |
2.86e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTS-----GQITVNGMNPHKQREEFVRTIGVVFGQRSQLWWDI 114
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEgkvtvGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 194 LKIREFLKEMNERYKtTILLTTHDITDIEALCERVIMLDEGNIMYDGS-------LDNLRT-QWGVEKEIHF 257
Cdd:PRK13643 181 IEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTpsdvfqeVDFLKAhELGVPKATHF 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
39-241 |
3.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.03 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGM---NPHKQRE-EFVR-TIGVVFG-QRSQLwW 112
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitSTSKNKDiKQIRkKVGLVFQfPESQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAVQESFRLLKKVYGVSD------AQYKEHMEHVIETldigpLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:PRK13649 100 EETVLKDVAFGPQNFGVSQeeaealAREKLALVGISES-----LFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 187 GLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-251 |
3.06e-20 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 87.98 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 16 AYSSRPGlkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREE 95
Cdd:cd03249 9 RYPSRPD---------------VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 96 FVRT-IGVVfGQRSQLwWDIAVQESFRllkkvYGVSDAQYKEHME-------H-VIETLDIGplLDKPV----RKLSLGQ 162
Cdd:cd03249 74 WLRSqIGLV-SQEPVL-FDGTIAENIR-----YGKPDATDEEVEEaakkaniHdFIMSLPDG--YDTLVgergSQLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 163 RMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFL-KEMNERyktTILLTTHDITDIEAlCERVIMLDEGNIMYDGS 241
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALdRAMKGR---TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
250
....*....|
gi 488042473 242 LDNLRTQWGV 251
Cdd:cd03249 221 HDELMAQKGV 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
44-223 |
3.38e-20 |
|
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: 87.03 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIgVVFGQRSQLWWDIAVQESFRLL 123
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI-LYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 124 KKVYGVSDAQykehMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEM 203
Cdd:TIGR01189 98 AAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170 180
....*....|....*....|
gi 488042473 204 NERYKTTILLTTHDITDIEA 223
Cdd:TIGR01189 174 LARGGIVLLTTHQDLGLVEA 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
29-253 |
5.36e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 29 DLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnPHKQR---EEFVRTIGVVfG 105
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG--EHIQHyasKEVARRIGLL-A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSQLWWDIAVQESfrllkkvygVSDAQY----------KEHMEHV---IETLDIGPLLDKPVRKLSLGQRMRCELAAAL 172
Cdd:PRK10253 88 QNATTPGDITVQEL---------VARGRYphqplftrwrKEDEEAVtkaMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 173 IHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQWGVE 252
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIE 238
|
.
gi 488042473 253 K 253
Cdd:PRK10253 239 R 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
57-241 |
6.21e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 88.70 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 57 IGENGAGKSTTIKMLTGILTPTSGQITVNGMN-----PHKqreefvRTIGVVFgQRSQLWWDIAVQESFRLLKKVYGVSD 131
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDvtnvpPHL------RHINMVF-QSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 132 AQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTI 211
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|
gi 488042473 212 LLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
58-250 |
7.22e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.78 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 58 GENGAGKSTTIKMLTGILTPTSGQITVNG-----------MNPHKQReefvrtIGVVFgQRSQLWWDIAVQESFRllkkv 126
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgicLPPEKRR------IGYVF-QDARLFPHYKVRGNLR----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 127 YGVSdAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNER 206
Cdd:PRK11144 99 YGMA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 207 YKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLrtqWG 250
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV---WA 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-241 |
7.71e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.48 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEftaYSSRpglKGAFRDllnrnYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:PRK11308 2 QQPLLQAIDLKKH---YPVK---RGLFKP-----ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMN----PHKQREEFVRTIGVVFgqrsqlwwdiavQESFRLL---KKVygvsdAQYKEhmehviETLDIGPLLDK 153
Cdd:PRK11308 71 ELYYQGQDllkaDPEAQKLLRQKIQIVF------------QNPYGSLnprKKV-----GQILE------EPLLINTSLSA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 154 PVRK-----------------------LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTT 210
Cdd:PRK11308 128 AERRekalammakvglrpehydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLS 207
|
250 260 270
....*....|....*....|....*....|.
gi 488042473 211 ILLTTHDITDIEALCERVImldegnIMYDGS 241
Cdd:PRK11308 208 YVFISHDLSVVEHIADEVM------VMYLGR 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
44-250 |
8.41e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGILtPTSGQITVNG-----MNPHKQReefvRTIGVVfGQRSQLwwdiaVQE 118
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreLDPESWR----KHLSWV-GQNPQL-----PHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFR---LLKKVyGVSDAQYKEHME--HVIETLDIGPL-LDKPVRK----LSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK11174 438 TLRdnvLLGNP-DASDEQLQQALEnaWVSEFLPLLPQgLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 189 DVLVKLKIREFLKEMNERyKTTILLtTHDITDIEAlCERVIMLDEGNIMYDGSLDNLRTQWG 250
Cdd:PRK11174 517 DAHSEQLVMQALNAASRR-QTTLMV-THQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
41-225 |
1.03e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.71 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQItvngmnphkQREEFVRtIGVVfgqRSQLWWDIAVQ--- 117
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR-IGYV---PQKLYLDTTLPltv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRLLKKvyGVSDAQYKEHMEHVietlDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIR 197
Cdd:PRK09544 87 NRFLRLRP--GTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190
....*....|....*....|....*....|....
gi 488042473 198 EFLKEMNERYKTTILLTTHDI------TDiEALC 225
Cdd:PRK09544 161 DLIDQLRRELDCAVLMVSHDLhlvmakTD-EVLC 193
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
38-243 |
1.07e-19 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 89.81 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVfGQRSQLWwDIAV 116
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYL-PQDVELF-DGTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESF-RLLK----KVY------GVSDAqykehmehvIETL------DIGPLLdkpvRKLSLGQRMRCELAAALIHNPPLL 179
Cdd:COG4618 423 AENIaRFGDadpeKVVaaaklaGVHEM---------ILRLpdgydtRIGEGG----ARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488042473 180 FLDEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDiTDIEALCERVIMLDEGNIMYDGSLD 243
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHR-PSLLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
40-240 |
1.54e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.73 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRT-IGVVFGQR------SQLWW 112
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKhIGIVFQNPdnqfvgSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAvqesFRLlkKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK13648 104 DVA----FGL--ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 193 KLKIREFLKEMNERYKTTILLTTHDITdiEAL-CERVIMLDEGNIMYDG 240
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEG 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-232 |
1.85e-19 |
|
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: 85.92 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 47 TIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQItvngmnphkqrEEFVRTIGVVfGQRSQLWWDIAVQEsfRLLKKV 126
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----------EIELDTVSYK-PQYIKADYEGTVRD--LLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 127 YGV-SDAQYKEHmehVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNE 205
Cdd:cd03237 87 KDFyTHPYFKTE---IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....*..
gi 488042473 206 RYKTTILLTTHDITDIEALCERVIMLD 232
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
41-237 |
2.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.42 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPH---KQREEFVRTIGVVFG-QRSQLWWDi 114
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPEtgnKNLKKLRKKVSLVFQfPEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 194 LKIREFLKEMnERYKTTILLTTHDITDIEALCERVIMLDEGNIM 237
Cdd:PRK13641 182 KEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-245 |
4.19e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.40 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTAYSSRPGL---KGAFRDLLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP 77
Cdd:PRK10070 1 MAIKLEIKNLYKIFGEHPQRAFKyieQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 78 TSGQITVNGMNPHK-----QREEFVRTIGVVFgQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLD 152
Cdd:PRK10070 81 TRGQVLIDGVDIAKisdaeLREVRRKKIAMVF-QSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 153 KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLD 232
Cdd:PRK10070 160 SYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
250
....*....|...
gi 488042473 233 EGNIMYDGSLDNL 245
Cdd:PRK10070 240 NGEVVQVGTPDEI 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
40-245 |
4.79e-19 |
|
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: 84.85 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVR-TIGVVfgqrsqlwwdiaVQE 118
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrQVGVV------------LQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKVY-GVSDAQYKEHMEHVIET--------------LDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:cd03252 85 NVLFNRSIRdNIALADPGMSMERVIEAaklagahdfiselpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 184 PTIGLDVLVKLKIREFLKEMNEryKTTILLTTHDITDIEAlCERVIMLDEGNIMYDGSLDNL 245
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-229 |
4.82e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.94 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 47 TIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVN----------GMNPHKQREEFVRTIGVVFGqrSQLWWdiav 116
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyiKPDYDGTVEDLLRSITDDLG--SSYYK---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 qesfrllkkvygvsdaqykehmEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK13409 435 ----------------------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180 190
....*....|....*....|....*....|...
gi 488042473 197 REFLKEMNERYKTTILLTTHDITDIEALCERVI 229
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
40-236 |
6.12e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 82.87 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFgqrsqlwwdiaVQES 119
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY-----------VPED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 120 frllKKVYGVsdaqykeHMEH-VIETLDIGPLLdkpvrklSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRE 198
Cdd:cd03215 84 ----RKREGL-------VLDLsVAENIALSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 488042473 199 FLKEMNERYKTTILLTThDITDIEALCERVIMLDEGNI 236
Cdd:cd03215 146 LIRELADAGKAVLLISS-ELDELLGLCDRILVMYEGRI 182
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-232 |
6.43e-19 |
|
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: 87.53 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 47 TIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVN---GMNPHKQREEFvrtigvvfgqrsqlwwDIAVQEsfrLL 123
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkiSYKPQYISPDY----------------DGTVEE---FL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 124 KKVYG--VSDAQYKEHmehVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLK 201
Cdd:COG1245 423 RSANTddFGSSYYKTE---IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|.
gi 488042473 202 EMNERYKTTILLTTHDITDIEALCERVIMLD 232
Cdd:COG1245 500 RFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-249 |
7.34e-19 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 84.87 E-value: 7.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTAYSSRpglKGAFRDLL--NRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPT 78
Cdd:PRK13546 1 MNVSVNIKNVTKEYRIYRTN---KERMKDALipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 79 SGQITVNGMnphkqreefVRTIGVVFGQRSQLwwdIAVQE-SFRLLkkVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRK 157
Cdd:PRK13546 78 VGKVDRNGE---------VSVIAISAGLSGQL---TGIENiEFKML--CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 158 LSLGQRMRCELAAALIHNPPLLFLDEP-TIGLDVLVKL---KIREFlKEMNEryktTILLTTHDITDIEALCERVIMLDE 233
Cdd:PRK13546 144 YSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKcldKIYEF-KEQNK----TIFFVSHNLGQVRQFCTKIAWIEG 218
|
250
....*....|....*.
gi 488042473 234 GNIMYDGSLDNLRTQW 249
Cdd:PRK13546 219 GKLKDYGELDDVLPKY 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-237 |
7.91e-19 |
|
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: 87.05 E-value: 7.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 22 GLKGAFRDllnrNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTT----IKMLTGILTPTSGQITVNG-----MNPHKQ 92
Cdd:COG4172 11 DLSVAFGQ----GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGqdllgLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 93 REefVR--TIGVVF-------------GQrsQlwwdiaVQESFRLLKkvyGVSDAQYKEHmehVIETLD-IGplLDKPVR 156
Cdd:COG4172 87 RR--IRgnRIAMIFqepmtslnplhtiGK--Q------IAEVLRLHR---GLSGAAARAR---ALELLErVG--IPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 157 K-------LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVI 229
Cdd:COG4172 149 RldayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVA 228
|
....*...
gi 488042473 230 MLDEGNIM 237
Cdd:COG4172 229 VMRQGEIV 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
31-241 |
1.40e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.59 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQR-EEFVRTIGVVfGQRSQ 109
Cdd:COG4604 7 VSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsRELAKRLAIL-RQENH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 110 LWWDIAVQE--SF--------RLlkkvygvsDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLL 179
Cdd:COG4604 86 INSRLTVRElvAFgrfpyskgRL--------TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 180 FLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
31-250 |
1.94e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 84.79 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTiKMLTGILTPTSGQITVNGMNPHKQREEFVRTIG----VVFGQ 106
Cdd:NF000106 19 LVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*hrpVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 107 RSQLwwdiAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:NF000106 98 RESF----SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488042473 187 GLDVLVKLKIREFLKEMnERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQWG 250
Cdd:NF000106 174 GLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-250 |
2.12e-18 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 86.10 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTAYSSR-PGLKGAFRDLLNRNYKIvpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTS 79
Cdd:PRK13545 1 MNYKVKFEHVTKKYKMYNKPfDKLKDLFFRSKDGEYHY--ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 80 GQITVNGMnphkqreefVRTIGVVFGQRSQLwwdiAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLS 159
Cdd:PRK13545 79 GTVDIKGS---------AALIAISSGLNGQL----TGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 160 LGQRMRCELAAALIHNPPLLFLDEptiGLDVLVKLKIREFLKEMNErYK---TTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK13545 146 SGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMNE-FKeqgKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
250
....*....|....
gi 488042473 237 MYDGSLDNLRTQWG 250
Cdd:PRK13545 222 KEYGDIKEVVDHYD 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
44-265 |
2.19e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVFGQRSQlwwdiAVQESFRL 122
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPA-----AEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 123 LKKV-----------YGVSDaqyKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:PRK10575 105 LVAIgrypwhgalgrFGAAD---REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 192 VKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSL------DNLRTQWGVEKEI--HFQFVAPV 263
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPaelmrgETLEQIYGIPMGIlpHPAGAAPV 261
|
..
gi 488042473 264 SY 265
Cdd:PRK10575 262 SF 263
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
38-245 |
2.28e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQRE-EFVRTIGVVFGQRSQLWWDIAV 116
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKVYGVSDaqyKEHMEHVIETLDIGPLLDKPVR---KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK13642 100 EDDVAFGMENQGIPR---EEMIKRVDEALLAVNMLDFKTRepaRLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488042473 194 LKIREFLKEMNERYKTTILLTTHDItDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDL-DEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
43-190 |
3.51e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.39 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFvrtigvvfgqRSQLWW---------D 113
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY----------HQDLLYlghqpgiktE 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 114 IAVQESFRLLKKVYGVSDAqykEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK13538 89 LTALENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-241 |
4.74e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFtaySSRPGLkgaFRdllnRNYkiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:PRK15112 1 VETLLEVRNLSKTF---RYRTGW---FR----RQT--VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMNPH----KQREEFVRTI------GVVFGQRSQLWWDIAVQESFRLlkkvygvsDAQYKEhmEHVIETL-DIGP 149
Cdd:PRK15112 69 ELLIDDHPLHfgdySYRSQRIRMIfqdpstSLNPRQRISQILDFPLRLNTDL--------EPEQRE--KQIIETLrQVGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 150 LLDKPV---RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCE 226
Cdd:PRK15112 139 LPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISD 218
|
250
....*....|....*
gi 488042473 227 RVIMLDEGNIMYDGS 241
Cdd:PRK15112 219 QVLVMHQGEVVERGS 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-246 |
5.74e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFtayssrpglkgafrdllNRNykivPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILT-PTS 79
Cdd:PRK09984 1 MQTIIRVEKLAKTF-----------------NQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgDKS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 80 GQITVNGMNPHKQRE-EFVRTI-------GVVFgQRSQLWWDIAVQE--------SFRLLKKVYGVSDAQYKEHMEHVIE 143
Cdd:PRK09984 60 AGSHIELLGRTVQREgRLARDIrksrantGYIF-QQFNLVNRLSVLEnvligalgSTPFWRTCFSWFTREQKQRALQALT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 144 TLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEA 223
Cdd:PRK09984 139 RVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALR 218
|
250 260
....*....|....*....|....*.
gi 488042473 224 LCERVIMLDEGNIMYDGS---LDNLR 246
Cdd:PRK09984 219 YCERIVALRQGHVFYDGSsqqFDNER 244
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
36-259 |
5.93e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 36 KIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSQLWWD-- 113
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDti 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 ---IAvqesfrllkkvYGVSDAQYKEHMEHV---------IETLDIGplLDKPVRK----LSLGQRMRCELAAALIHNPP 177
Cdd:PRK11176 434 annIA-----------YARTEQYSREQIEEAarmayamdfINKMDNG--LDTVIGEngvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 178 LLFLDEPTIGLDVLVKLKIREFLKEMneRYKTTILLTTHDITDIEALCErVIMLDEGNIMYDGSLDNLRTQWGVEKEIH- 256
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADE-ILVVEDGEIVERGTHAELLAQNGVYAQLHk 577
|
...
gi 488042473 257 FQF 259
Cdd:PRK11176 578 MQF 580
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
39-233 |
7.91e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.60 E-value: 7.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGQITVNG-----MNPHKqreefvRTIGVVFgQRSQL 110
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltaLPAEQ------RRIGILF-QDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 W--WDIAVQESFRLLKkvyGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:COG4136 88 FphLSVGENLAFALPP---TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488042473 189 DVLVKLKIREFLKEMNERYKTTILLTTHDITDIEAlCERVIMLDE 233
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
44-241 |
9.92e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 9.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGiLTPTSGQITVNGMN-PHKQREEFVRtigvvfgQRSQLwwdiAVQESFRL 122
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPlSDWSAAELAR-------HRAYL----SQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 123 LKKVY---------GVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLG--QRMRceLAAAL--IH---NPP--LLFLDEP 184
Cdd:COG4138 83 AMPVFqylalhqpaGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGewQRVR--LAAVLlqVWptiNPEgqLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 185 TIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
31-243 |
1.26e-17 |
|
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: 83.70 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGI--LTPTSGQITVN-GMNP---HKQREEFVRTIGVVF 104
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvALCEkcgYVERPSKVGEPCPVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 105 GQRSQL----WWDIAVQESFRLLKKV---YGVSDAQYKEH--MEHVIETL-DIGPLLDKPV------------------- 155
Cdd:TIGR03269 86 GGTLEPeevdFWNLSDKLRRRIRKRIaimLQRTFALYGDDtvLDNVLEALeEIGYEGKEAVgravdliemvqlshrithi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 156 -RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:TIGR03269 166 aRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENG 245
|
....*....
gi 488042473 235 NIMYDGSLD 243
Cdd:TIGR03269 246 EIKEEGTPD 254
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
39-240 |
1.65e-17 |
|
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: 79.61 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPT---SGQITVNGMNPHKQREEFVRTIgvvfgqrsqlwwdIA 115
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI-------------IY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESfrllkkvygvsdaqyKEHMEH--VIETLDIGPLL--DKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:cd03233 88 VSEE---------------DVHFPTltVRETLDFALRCkgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488042473 192 VKLKIREFLKEMNERYKTTILLTTHDITD-IEALCERVIMLDEGNIMYDG 240
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQIYYG 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
44-236 |
1.92e-17 |
|
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: 82.92 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHkQREEFVRTIGVVFGQrsqlwwdiavqesFR 121
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpVTAD-NREAYRQLFSAVFSD-------------FH 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 122 LLKKVYGVSDAQYKEHMEHVIETLDigplLDKPVR---------KLSLGQRMRCELAAALIHNPPLLFLDE------PTI 186
Cdd:COG4615 417 LFDRLLGLDGEADPARARELLERLE----LDHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPEF 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 187 GldvlvklKI--REFLKEMNERYKtTILLTTHDitdiEA---LCERVIMLDEGNI 236
Cdd:COG4615 493 R-------RVfyTELLPELKARGK-TVIAISHD----DRyfdLADRVLKMDYGKL 535
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
38-240 |
2.12e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.49 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGIlTPTSGQITV-----NG-----MNPHKQREEFVRTIGVVFGQR 107
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTAdrfrwNGidllkLSPRERRKIIGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 108 S-----------QL------------WWDIAV---QESFRLLKKVyGVsdaqyKEHmEHVIETLdigPLldkpvrKLSLG 161
Cdd:COG4170 99 SscldpsakigdQLieaipswtfkgkWWQRFKwrkKRAIELLHRV-GI-----KDH-KDIMNSY---PH------ELTEG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 162 QRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVimldegNIMYDG 240
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI------TVLYCG 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
38-245 |
2.21e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.14 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN---PHKQREEFVRTIGVVFgQRSQLWWDI 114
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndPKVDERLIRQEAGMVF-QQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFRL-LKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK09493 93 TALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488042473 194 LKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK09493 173 HEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
40-241 |
2.44e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.82 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVN------GMNPHKQREEFVRTIGVVFG-QRSQLWW 112
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DiAVQESFRLLKKVYGvsdAQYKEHMEHVIETLDIGPLLDKPVRK----LSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK13645 106 E-TIEKDIAFGPVNLG---ENKQEAYKKVPELLKLVQLPEDYVKRspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488042473 189 DVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-240 |
2.48e-17 |
|
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: 78.82 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 27 FRDLlnrNYKI-VPAV-----NDVSFTIKQGEMVGYIGENGAGKSTTIKML-----TGILTptsGQITVNGmnpHKQREE 95
Cdd:cd03232 6 WKNL---NYTVpVKGGkrqllNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILING---RPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 96 FVRTIGvvfgqrsqlwwdiavqesfrllkkvygvsdaqYKEHME-H-----VIETLDIGPLLdkpvRKLSLGQRMRCELA 169
Cdd:cd03232 77 FQRSTG--------------------------------YVEQQDvHspnltVREALRFSALL----RGLSVEQRKRLTIG 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 170 AALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKtTILLTTHD-ITDIEALCERVIMLDE-GNIMYDG 240
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ-AILCTIHQpSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
39-234 |
5.46e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.46 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGIL--TPTSGQITVngmnphkQREEFVRTIGVVfgqrSQLWWDIAV 116
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV-------PDNQFGREASLI----DAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFRLLKKVyGVSDAqykehmehvietldigPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL----V 192
Cdd:COG2401 113 KDAVELLNAV-GLSDA----------------VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488042473 193 KLKIREFLKemneRYKTTILLTTHDITDIEALC-ERVIMLDEG 234
Cdd:COG2401 176 ARNLQKLAR----RAGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
39-236 |
5.75e-17 |
|
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: 78.30 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-----PHKQReefvRTIGVV---------- 103
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskigLHDLR----SRISIIpqdpvlfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 104 -------FGQRS--QLWwdiavqesfRLLKKVygvsdaqykeHMEHVIETLDIGplLDKPV----RKLSLGQRMRCELAA 170
Cdd:cd03244 94 irsnldpFGEYSdeELW---------QALERV----------GLKEFVESLPGG--LDTVVeeggENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 171 ALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEmnERYKTTILLTTHDITDIeALCERVIMLDEGNI 236
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTI-IDSDRILVLDKGRV 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
38-239 |
6.37e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.69 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN---------PHKQREEFvrtiGVVFgQRS 108
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldadalAQLRREHF----GFIF-QRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 109 QLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK10535 96 HLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488042473 189 DVLVKLKIREFLKEMNERYKTTILLtTHDiTDIEALCERVIMLDEGNIMYD 239
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGHTVIIV-THD-PQVAAQAERVIEIRDGEIVRN 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
40-253 |
8.21e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQ-REEFVRTIgvvfGQRSQLWWDIAVQE 118
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlQKNLVAYV----PQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKVYG------VSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK15056 98 EDVVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 193 KLKIREFLKEMNERYKtTILLTTHDITDIEALCERVIMLdEGNIMYDGSLDNLRTQWGVEK 253
Cdd:PRK15056 178 EARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLEL 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-236 |
8.47e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQREEFVRTI----------GVVFGq 106
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQDGLANGIvyisedrkrdGLVLG- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 107 rsqlwwdIAVQE-----SFRLLKKVYGVSDAQyKEHM--EHVIETLDI-GPLLDKPVRKLSLGQRMRCELAAALIHNPPL 178
Cdd:PRK10762 345 -------MSVKEnmsltALRYFSRAGGSLKHA-DEQQavSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 179 LFLDEPTIGLDVLVKLKIREFLKemneRYKT---TILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLIN----QFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
31-216 |
1.78e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.53 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVfGQRSQL 110
Cdd:PRK13540 7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFV-GHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFrllkkVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK13540 86 NPYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 488042473 191 LVKLKIREFLKEmNERYKTTILLTTH 216
Cdd:PRK13540 161 LSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
39-236 |
2.43e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 79.70 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHK-QREEFVRTIGVVfGQRSQLW-----W 112
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFGKHIGYL-PQDVELFpgtvaE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIA-VQESFRLLKKVYGVSDAQYKEhmehVIETL------DIGPlldkPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:TIGR01842 411 NIArFGENADPEKIIEAAKLAGVHE----LILRLpdgydtVIGP----GGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488042473 186 IGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALcERVIMLDEGNI 236
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRI 531
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
31-243 |
3.07e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.27 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT----------VNGMNPHKQReEFVRT- 99
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlrdLYALSEAERR-RLLRTe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 100 IGVVF-----GQRSQLWWDIAVQEsfRLL---KKVYGVSDAQYKEHMEHVieTLDIGPLLDKPvRKLSLGQRMRCELAAA 171
Cdd:PRK11701 91 WGFVHqhprdGLRMQVSAGGNIGE--RLMavgARHYGDIRATAGDWLERV--EIDAARIDDLP-TTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 172 LIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLD 243
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTD 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-245 |
3.26e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQ-RSQLWWDIAV 116
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQmRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 --QESFRLLKKVYGVSD-----------AQYKEHMEHVIETLDI------GPLLDKPVRKLSLGQRMRCELAAALIHNPP 177
Cdd:PRK10261 109 ifQEPMTSLNPVFTVGEqiaesirlhqgASREEAMVEAKRMLDQvripeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 178 LLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-236 |
3.64e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 33 RNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKQREE---FV----RTI 100
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvriRSPRDAIRAgiaYVpedrKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 101 GVVFGQrsqlwwdiAVQE-----SFRLLKKVYGVSDAQYKEHMEHVIETLDI-GPLLDKPVRKLSLGQRMRCELAAALIH 174
Cdd:COG1129 340 GLVLDL--------SIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 175 NPPLLFLDEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:COG1129 412 DPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
38-245 |
3.83e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP----TSGQITVNGM-----------------NPhkqREEF 96
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKpvapcalrgrkiatimqNP---RSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 97 --VRTIGVvfgqrsqlwwdiAVQESFRLLKKVygVSDAQYKEHMEHVietldiGplLDKPVRKLSL-------G--QRMR 165
Cdd:PRK10418 93 npLHTMHT------------HARETCLALGKP--ADDATLTAALEAV------G--LENAARVLKLypfemsgGmlQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 166 ceLAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK10418 151 --IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-241 |
4.23e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV------------NGMNPHKQR-----EEFVRTI 100
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhELITNPYSKkiknfKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 101 GVVFG-QRSQLWWDiAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIG-PLLDKPVRKLSLGQRMRCELAAALIHNPPL 178
Cdd:PRK13631 119 SMVFQfPEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 179 LFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLtTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVI-THTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-241 |
5.06e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 26 AFRDLLNRnYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQREEFVRT-IGV 102
Cdd:PRK13638 3 ATSDLWFR-YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQqVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 103 VFGQRSQ--LWWDIAVQESFRLlkKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:PRK13638 82 VFQDPEQqiFYTDIDSDIAFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 181 LDEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-247 |
8.92e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 8.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFTAyssrpglkgafrdllnrnykiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:PRK15439 8 APPLLCARSISKQYSG---------------------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMNPHKQREEFVRTIGV-VFGQRSQLWWDIAVQES--FRLLKKvygvsdAQYKEHMEHVIETLDIGPLLDKPVRK 157
Cdd:PRK15439 67 TLEIGGNPCARLTPAKAHQLGIyLVPQEPLLFPNLSVKENilFGLPKR------QASMQKMKQLLAALGCQLDLDSSAGS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 158 LSLGQRMRCELAAALIHNPPLLFLDEPTIGL-----DVLVKlKIREFLKEmneryKTTILLTTHDITDIEALCERVIMLD 232
Cdd:PRK15439 141 LEVADRQIVEILRGLMRDSRILILDEPTASLtpaetERLFS-RIRELLAQ-----GVGIVFISHKLPEIRQLADRISVMR 214
|
250
....*....|....*
gi 488042473 233 EGNIMYDGSLDNLRT 247
Cdd:PRK15439 215 DGTIALSGKTADLST 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-259 |
1.58e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.30 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--------MNPHKQRE--------EFVRTIGV 102
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqQDPPRNVEgtvydfvaEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 103 VFGQRSQLWWDIAVQESFRLLKKVygvsdAQYKEHMEH------------VIETLDIGPllDKPVRKLSLGQRMRCELAA 170
Cdd:PRK11147 97 YLKRYHDISHLVETDPSEKNLNEL-----AKLQEQLDHhnlwqlenrineVLAQLGLDP--DAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 171 ALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEmnerYKTTILLTTHDITDIEALCERVIMLDEGNIM-----YDGSLD-- 243
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMATRIVDLDRGKLVsypgnYDQYLLek 245
|
250
....*....|....*...
gi 488042473 244 --NLRtqwgVEKEIHFQF 259
Cdd:PRK11147 246 eeALR----VEELQNAEF 259
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-241 |
2.52e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.14 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN----PHKQREefVRTigvVFgQ 106
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvPAENRH--VNT---VF-Q 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 107 RSQLWWDIAVQE--SFRL-LKKVygvSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:PRK09452 94 SYALFPHMTVFEnvAFGLrMQKT---PAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 184 PTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
34-245 |
3.69e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 34 NYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEFVRTIGVVFGQRSQLWW 112
Cdd:PRK11614 14 HYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAVQESfrLLKKVYGVSDAQYKEHMEHVietLDIGP-LLDKPVRK---LSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK11614 94 RMTVEEN--LAMGGFFAERDQFQERIKWV---YELFPrLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 189 DVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
40-237 |
3.80e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLT--GILTP---TSGQITVNGMNPHKQREEFV---RTIGVVFGQRSQLW 111
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPRTDTVdlrKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 WDIAVQESFRLlkKVYGVSDaqyKEHMEHVIETLDIGPLLDKPVRK--------LSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:PRK14239 100 MSIYENVVYGL--RLKGIKD---KQVLDEAVEKSLKGASIWDEVKDrlhdsalgLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488042473 184 PTIGLDVLVKLKIREFLKEMNERYktTILLTTHDITDIEALCERVIMLDEGNIM 237
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
39-236 |
7.48e-15 |
|
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: 72.44 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNphkqreefVRTIGVVfGQRSQLwwDIAVQE 118
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID--------ISTIPLE-DLRSSL--TIIPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKVYGVSDAQYKEHMEHVIETLDI--GPLldkpvrKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:cd03369 91 PTLFSGTIRSNLDPFDEYSDEEIYGALRVseGGL------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488042473 197 REFLKEmnERYKTTILLTTHDITDIeALCERVIMLDEGNI 236
Cdd:cd03369 165 QKTIRE--EFTNSTILTIAHRLRTI-IDYDKILVMDAGEV 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-248 |
9.99e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGiLTPTSGQITVNGMN----PHKqreEFVRtigvvfgQRSQLwwdiAVQES 119
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawSAA---ELAR-------HRAYL----SQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 120 FRLLKKVY---------GVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLG--QRMRceLAAAL--IH---NP--PLLFL 181
Cdd:PRK03695 80 PPFAMPVFqyltlhqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVR--LAAVVlqVWpdiNPagQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 182 DEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRTQ 248
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-217 |
1.43e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 6 EVQGLRKEFTAYSSRPGlKGAFrDLLNRNYKIVPA--VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:PRK11147 300 EVMGTAKMQVEEASRSG-KIVF-EMENVNYQIDGKqlVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VngmnphkqreefvrtiGV-----VFGQ-RSQLWWDIAVQESFRLLKK---VYGVSdaqykehmEHVietldIGPLLD-- 152
Cdd:PRK11147 378 C----------------GTklevaYFDQhRAELDPEKTVMDNLAEGKQevmVNGRP--------RHV-----LGYLQDfl 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 153 -------KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVlvklKIREFLKEMNERYKTTILLTTHD 217
Cdd:PRK11147 429 fhpkramTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-245 |
1.54e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPH-------------KQREEFV 97
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 98 RT-IGVVFgQRSQLWWDIAVQES-FRLLKKVYGVSDAQYKEHMEHVIETLDI-GPLLDKPVRKLSLGQRMRCELAAALIH 174
Cdd:PRK10619 91 RTrLTMVF-QHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 175 NPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLtTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVV-THEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
42-216 |
1.58e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.76 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGQITVNGmnpHKQREEFVRTIGVVFGQrsqlwwDI---- 114
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNG---RPLDSSFQRSIGYVQQQ------DLhlpt 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 -AVQESFRL---LKKVYGVSDAQYKEHMEHVIETLDIGPLLDK----PVRKLSLGQRMRCELAAALIHNPPLL-FLDEPT 185
Cdd:TIGR00956 851 sTVRESLRFsayLRQPKSVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLlFLDEPT 930
|
170 180 190
....*....|....*....|....*....|.
gi 488042473 186 IGLDVLVKLKIREFLKEMNErYKTTILLTTH 216
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLAD-HGQAILCTIH 960
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-240 |
2.59e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.70 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 3 SVIEVQGLRKEFTAYSSrpgLKGafrdllnrnykivpavndVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQI 82
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTV---LHG------------------IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 83 -----TVNGMNPHKQREEFVRT----IGVVFgqrsqlwwdiavqESFRLLKkvygvsdaqYKEHMEHVIEtldiGPLLDK 153
Cdd:PRK11264 61 rvgdiTIDTARSLSQQKGLIRQlrqhVGFVF-------------QNFNLFP---------HRTVLENIIE----GPVIVK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 154 PV--------------------------RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD------VLVklKIREFLK 201
Cdd:PRK11264 115 GEpkeeatararellakvglagketsypRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgeVLN--TIRQLAQ 192
|
250 260 270
....*....|....*....|....*....|....*....
gi 488042473 202 EmneryKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:PRK11264 193 E-----KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
40-240 |
2.63e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.47 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILT-P---TSGQITVNGMN----PHKQREEFVRT-IGVVFgQRSQL 110
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDlqriSEKERRNLVGAeVAMIF-QDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETL------DIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLnqvgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 185 TIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDG 240
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
33-234 |
2.83e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.58 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 33 RNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmnphkqreefvrTIGVVfgqrSQLWW 112
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYV----SQEPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 diAVQESFR---LLKKVYgvsDAQ-YKEhmehVIET------LDIGPLLDKPV-----RKLSLGQRMRCELAAALIHNPP 177
Cdd:cd03250 77 --IQNGTIReniLFGKPF---DEErYEK----VIKAcalepdLEILPDGDLTEigekgINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 178 LLFLDEPTIGLDVLVKLKIRE--FLKEMneRYKTTILLTTHDITDIEAlCERVIMLDEG 234
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-250 |
3.15e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 35 YKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQREEFVRTI-------Gvvfg 105
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdMADARHRRAVCPRIaympqglG---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 qrSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:NF033858 87 --KNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 186 IGLDVLVK-----L--KIREflkemnERYKTTILLTTHDITdiEA-LCERVIMLDEGNIMYDGSLDNLRTQWG 250
Cdd:NF033858 165 TGVDPLSRrqfweLidRIRA------ERPGMSVLVATAYME--EAeRFDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-190 |
3.90e-14 |
|
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: 73.05 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKeftAYSSRpglkgafrdLLnrnykivpaVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT 83
Cdd:TIGR03719 322 VIEAENLTK---AFGDK---------LL---------IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 84 VNgmnphkqreEFVRtIGVVFGQRSQLWWDIAVQESfrllkkvygVSDAQykEHMEhvIETLDI------------GPLL 151
Cdd:TIGR03719 381 IG---------ETVK-LAYVDQSRDALDPNKTVWEE---------ISGGL--DIIK--LGKREIpsrayvgrfnfkGSDQ 437
|
170 180 190
....*....|....*....|....*....|....*....
gi 488042473 152 DKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:TIGR03719 438 QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
40-218 |
4.22e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGI--LTPT---SGQITVNGMN---PHKQREEFVRTIGVVFgQR---- 107
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNlyaPDVDPVEVRRRIGMVF-QKpnpf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 108 -SQLWWDIAvqesfrllkkvYGVSDAQYKEHMEHVIET-LDIGPLLDKPVRKL-------SLGQRMRCELAAALIHNPPL 178
Cdd:PRK14243 104 pKSIYDNIA-----------YGARINGYKGDMDELVERsLRQAALWDEVKDKLkqsglslSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488042473 179 LFLDEPTIGLDVLVKLKIREFLKEMNERYktTILLTTHDI 218
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
41-241 |
5.25e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPT--------SGQITVNGMNPHKQREEFVRTIGVVFGQRSQLWW 112
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAVQESFRLLK----KVYGVSDAQYKEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAAL---------IHNPPLL 179
Cdd:PRK13547 97 AFSAREIVLLGRyphaRRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 180 FLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGS 241
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-243 |
5.84e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 23 LKGAFRDLLNRNY-KIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLT----GILTPTSGQITVNGMNPHKQREEFv 97
Cdd:TIGR00956 58 LTRGFRKLKKFRDtKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHY- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 98 rTIGVVF-GQRSQLWWDIAVQESFRLLKK-------VYGVSDAQYKEHMEHVIET---LDI------GpllDKPVRKLSL 160
Cdd:TIGR00956 137 -RGDVVYnAETDVHFPHLTVGETLDFAARcktpqnrPDGVSREEYAKHIADVYMAtygLSHtrntkvG---NDFVRGVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 161 GQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDIT-DIEALCERVIMLDEGNIMYD 239
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSqDAYELFDKVIVLYEGYQIYF 292
|
....
gi 488042473 240 GSLD 243
Cdd:TIGR00956 293 GPAD 296
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
40-217 |
6.42e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPH-KQREEFVRTIGVVFgqrsqlwwdiavqE 118
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRKLFSAVF-------------T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKVYG-----VSDAQYKE-----HMEHVIEtLDIGPLLDKpvrKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK10522 405 DFHLFDQLLGpegkpANPALVEKwlerlKMAHKLE-LEDGRISNL---KLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180 190
....*....|....*....|....*....|
gi 488042473 189 D-VLVKLKIREFLKEMNERYKtTILLTTHD 217
Cdd:PRK10522 481 DpHFRREFYQVLLPLLQEMGK-TIFAISHD 509
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
39-216 |
8.79e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.97 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGIlTPT--SGQITVNGmnphKQRE------EFVRTIGVVfgqRSQL 110
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQgySNDLTLFG----RRRGsgetiwDIKKHIGYV---SSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFR--LLKK------VY-GVSDAQYKEHMEHvietLDI----GPLLDKPVRKLSLGQRMRCELAAALIHNPP 177
Cdd:PRK10938 346 HLDYRVSTSVRnvILSGffdsigIYqAVSDRQQKLAQQW----LDIlgidKRTADAPFHSLSWGQQRLALIVRALVKHPT 421
|
170 180 190
....*....|....*....|....*....|....*....
gi 488042473 178 LLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTH 216
Cdd:PRK10938 422 LLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
40-245 |
1.25e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 40 AVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN----PHKQREEFVRTIGVVF-------GQRS 108
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgmKDDEWRAVRSDIQMIFqdplaslNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 109 QLWWDIAvqESFRLLKKvyGVSDAQYKEHMEHVIETLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK15079 116 TIGEIIA--EPLRTYHP--KLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 188 LDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-190 |
2.29e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKeftayssrpglkgAFRD-LLnrnykivpaVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQI 82
Cdd:PRK11819 324 VIEAENLSK-------------SFGDrLL---------IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 83 TVNgmnphkqreEFVRtIGVVFGQRSQLWWDIAVQESfrllkkvygVSDAQykEHMEhvIETLDI------------GPL 150
Cdd:PRK11819 382 KIG---------ETVK-LAYVDQSRDALDPNKTVWEE---------ISGGL--DIIK--VGNREIpsrayvgrfnfkGGD 438
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488042473 151 LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK11819 439 QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
39-236 |
2.67e-13 |
|
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: 70.62 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEFVRTIGVVfGQRSQLWWD---- 113
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDiRDVTQASLRAAIGIV-PQDTVLFNDtiay 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 -IAvqesfrllkkvYGVSDAQYKE--------HMEHVIETLDIGplLDKPV--R--KLSLGQRMRCELAAALIHNPPLLF 180
Cdd:COG5265 451 nIA-----------YGRPDASEEEveaaaraaQIHDFIESLPDG--YDTRVgeRglKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 181 LDEPTIGLDVLVKLKIREFLKEMNERyKTTIL----LTThdITDiealCERVIMLDEGNI 236
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARG-RTTLViahrLST--IVD----ADEILVLEAGRI 570
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-219 |
3.01e-13 |
|
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: 70.20 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 47 TIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITvngmnphkqreefvrtigvvfgqrSQLWWDiAVQESFR----- 121
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD------------------------EEPSWD-EVLKRFRgtelq 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 122 -LLKKVYG----------------------VSD--AQYKEH--MEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIH 174
Cdd:COG1245 150 dYFKKLANgeikvahkpqyvdlipkvfkgtVREllEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 175 NPPLLFLDEPTIGLDVLVKLK----IREFLKEmneryKTTILLTTHDIT 219
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNvarlIRELAEE-----GKYVLVVEHDLA 273
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-237 |
3.53e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 30 LLNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN----PHKQREEFVRTIGVVFG 105
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidtlSPGKLQALRRDIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 Q-RSQLWWDIAVQESFRLLKKVYGVSDAqyKEHMEHVIETLD-IGPLLDKPVR---KLSLGQRMRCELAAALIHNPPLLF 180
Cdd:PRK10261 409 DpYASLDPRQTVGDSIMEPLRVHGLLPG--KAAAARVAWLLErVGLLPEHAWRyphEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 181 LDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIM 237
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
41-234 |
3.67e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKS-TTIKMLTGILTP----TSGQITVNGMNPHKQREefvRTIGVVFGQRsqlwwdIA 115
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASE---QTLRGVRGNK------IA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 V--QESFRLL-------KKVYGV--------SDAQYKEhmehVIETLD-------IGPLLDKPvRKLSLGQRMRCELAAA 171
Cdd:PRK15134 96 MifQEPMVSLnplhtleKQLYEVlslhrgmrREAARGE----ILNCLDrvgirqaAKRLTDYP-HQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 172 LIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-234 |
7.31e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILtPT---SGQITVNG--MNPHKQREEFVRTIgVVFGQRSQLWW 112
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGeeLQASNIRDTERAGI-AIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAVQESFRLLKKV--YGVSD-----AQYKEHMEHVieTLDIGPllDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK13549 96 ELSVLENIFLGNEItpGGIMDydamyLRAQKLLAQL--KLDINP--ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488042473 186 IGL---DVLVKLKIREFLKEMNerykTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:PRK13549 172 ASLtesETAVLLDIIRDLKAHG----IACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
39-231 |
9.66e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKQREE--FVRTIGVVFGQ--RSQ 109
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistLKPEIYRQQvsYCAQTPTLFGDtvYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 110 LW--WDIAVQ--ESFRLLKkvygvsDAQYKEHMEHvietldigpLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK10247 101 LIfpWQIRNQqpDPAIFLD------DLERFALPDT---------ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488042473 186 IGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEAlCERVIML 231
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-245 |
1.03e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 27 FRDLLNRnYK--IVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNphkqreefVRTIGVvf 104
Cdd:PLN03130 1240 FEDVVLR-YRpeLPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCD--------ISKFGL-- 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 105 gqrsqlwWDiavqesfrlLKKVYGV----------------------SDAQYKEHME--HVIETLDIGPL-LDKPV---- 155
Cdd:PLN03130 1309 -------MD---------LRKVLGIipqapvlfsgtvrfnldpfnehNDADLWESLEraHLKDVIRRNSLgLDAEVseag 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 156 RKLSLGQRMRCELAAALIHNPPLLFLDEPT----IGLDVLVKLKIREFLKEmnerykTTILLTTHDI-TDIEalCERVIM 230
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATaavdVRTDALIQKTIREEFKS------CTMLIIAHRLnTIID--CDRILV 1444
|
250
....*....|....*
gi 488042473 231 LDEGNIMYDGSLDNL 245
Cdd:PLN03130 1445 LDAGRVVEFDTPENL 1459
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
41-236 |
1.10e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQREEFVRTIGVVFGQRSQ--------L 110
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdISPRSPLDAVKKGMAYITESRRDngffpnfsI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFRL--LKKVYG-VSDAQYKEHMEHVIETLDIG-PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:PRK09700 359 AQNMAISRSLKDggYKGAMGlFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488042473 187 GLDVLVKLKIREFLKEMNERYKtTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-216 |
1.34e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 18 SSRPGLKGAFRDLLNRNYkiVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMnpHKQREEFV 97
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNE--EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 98 RTIGVVfGQRSQLWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIGPLLdkpVRKLSLGQRMRCELAAALIHNPP 177
Cdd:PRK13543 82 RFMAYL-GHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTL---VRQLSAGQKKRLALARLWLSPAP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488042473 178 LLFLDEPTIGLDV----LVKLKIREFLkemneRYKTTILLTTH 216
Cdd:PRK13543 158 LWLLDEPYANLDLegitLVNRMISAHL-----RGGGAALVTTH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-238 |
1.49e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 47 TIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGmNPHKQREEFVRTigvvfgqrsqlwwdiAVQESFRLL--K 124
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEP-SWDEVLKRFRGT---------------ELQNYFKKLynG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 125 KVYGVSDAQYKEH---------------------MEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:PRK13409 159 EIKVVHKPQYVDLipkvfkgkvrellkkvdergkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 184 PTIGLDVLVKLKIREFLKEMNEryKTTILLTTHDITDIEALCERVimldegNIMY 238
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNV------HIAY 285
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-262 |
2.57e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.84 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFV-------RTIGVVFgQRSQLWWD 113
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQidaiklrKEVGMVF-QQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESFRLLKKVYGVSDA-QYKEHMEHVIETL----DIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488042473 189 DVLVKLKIREFLKEMneRYKTTILLTTHDITDIEALCERVIMLdegnimYDGSLdnlrTQWGVEKEIhfqFVAP 262
Cdd:PRK14246 185 DIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFL------YNGEL----VEWGSSNEI---FTSP 243
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
49-218 |
2.61e-12 |
|
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: 65.85 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 49 KQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQItvngmnphkqreefvrtigvvfgQRSQLWWDI-------AVQESFR 121
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF-----------------------DDPPDWDEIldefrgsELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 122 LLK--KVYGVSDAQY---------------------KEHMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPL 178
Cdd:cd03236 81 KLLegDVKVIVKPQYvdlipkavkgkvgellkkkdeRGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488042473 179 LFLDEPTIGLDVLVKLK----IREFLKEMNeryktTILLTTHDI 218
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNaarlIRELAEDDN-----YVLVVEHDL 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
48-232 |
2.78e-12 |
|
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: 64.52 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 48 IKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPhkqreefvrtigvvfgqrsqlwwdiavqesfrllkkvy 127
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 128 gVSDAQYKehmehvietldigplldkpvrKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERY 207
Cdd:cd03222 64 -VYKPQYI---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....*
gi 488042473 208 KTTILLTTHDITDIEALCERVIMLD 232
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
38-240 |
4.27e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.98 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGIlTPTSGQITVNGM----------NPHKQREEFVRTIGVVFgQR 107
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMrfddidllrlSPRERRKLVGHNVSMIF-QE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 108 SQLWWDIAVQESFRLLKKVYGVSdaqYKEH--------MEHVIETL------DIGPLLDKPVRKLSLGQRMRCELAAALI 173
Cdd:PRK15093 98 PQSCLDPSERVGRQLMQNIPGWT---YKGRwwqrfgwrKRRAIELLhrvgikDHKDAMRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 174 HNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVimldegNIMYDG 240
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI------NVLYCG 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
38-237 |
4.44e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG-----MNPHKQREEFVRTI-------GVVFg 105
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGeditgLSPRERRRLGVAYIpedrlgrGLVP- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 qrsqlwwDIAVQESFrLLKKVYG--------VSDAQYKEHMEHVIETLDI-GPLLDKPVRKLSLG--QRMRceLAAALIH 174
Cdd:COG3845 350 -------DMSVAENL-ILGRYRRppfsrggfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGnqQKVI--LARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 175 NPPLLFLDEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIM 237
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
41-242 |
4.99e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTS--GQITVNGMNPHKQreeFVRTIGVVfGQRSQLWWDIAVQE 118
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQ---ILKRTGFV-TQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SF---RLLKKVYGVSDAQYKEHMEHVIETLDIGP-----LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PLN03211 160 TLvfcSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488042473 191 LVKLKIREFLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSL 242
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKG 291
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-217 |
5.59e-12 |
|
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: 66.50 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPA----VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQ------ITVnGM---NPHKQREEFV 97
Cdd:TIGR03719 7 MNRVSKVVPPkkeiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgIKV-GYlpqEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 98 RtiGVVFgqrsqlwwdIAVQESFRLLKKV------YGVSDAQY------KEHMEHVIET---------LDIG------PL 150
Cdd:TIGR03719 86 R--ENVE---------EGVAEIKDALDRFneisakYAEPDADFdklaaeQAELQEIIDAadawdldsqLEIAmdalrcPP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 151 LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEmnerYKTTILLTTHD 217
Cdd:TIGR03719 155 WDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE----YPGTVVAVTHD 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-239 |
8.76e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSQLWwdiavQE 118
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLF-----SG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRL-LKKVYGVSDAQYKEHME--HVIETLDIGPL-LDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PLN03232 1325 TVRFnIDPFSEHNDADLWEALEraHIKDVIDRNPFgLDAEVseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488042473 191 LVKLKIREFLKEmnERYKTTILLTTHDITDIeALCERVIMLDEGNIM-YD 239
Cdd:PLN03232 1405 RTDSLIQRTIRE--EFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLeYD 1451
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
41-242 |
9.07e-12 |
|
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: 63.31 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGI--LTPTSGQITVNG-----MNPHkqreefvrtigvvfgQRSQLWWD 113
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGeditdLPPE---------------ERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESFRllkkVYGVSdaqykehMEHVIETLDIGplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV--- 190
Cdd:cd03217 81 LAFQYPPE----IPGVK-------NADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdal 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 191 -LVKLKIREFLKEmneryKTTILLTTHDitdiealcERVIML---DEGNIMYDGSL 242
Cdd:cd03217 141 rLVAEVINKLREE-----GKSVLIITHY--------QRLLDYikpDRVHVLYDGRI 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-248 |
1.37e-11 |
|
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: 65.23 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 29 DLLNRNYKivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPT-SGQITVNG-----------------MNPH 90
Cdd:TIGR02633 267 DVINPHRK---RVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpvdirnpaqairagiaMVPE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 91 -KQREEFVRTIGVvfGQRSQLwwdiAVQESFRLLKKVygvSDAQYKEHMEHVIETLDI---GPLLdkPVRKLSLGQRMRC 166
Cdd:TIGR02633 344 dRKRHGIVPILGV--GKNITL----SVLKSFCFKMRI---DAAAELQIIGSAIQRLKVktaSPFL--PIGRLSGGNQQKA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 167 ELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLr 246
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL- 490
|
..
gi 488042473 247 TQ 248
Cdd:TIGR02633 491 TQ 492
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
39-248 |
1.90e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 63.72 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITvngmnpHKQREEFVrtigvvfgqrSQLWWDI--AV 116
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK------HSGRISFS----------SQFSWIMpgTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 117 QESFrllkkVYGVSDAQYKehMEHVIETL----DIGPLLDKPVR-------KLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:cd03291 115 KENI-----IFGVSYDEYR--YKSVVKACqleeDITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 186 IGLDVLVKLKIRE--FLKEMNEryKTTILLTthdiTDIEAL--CERVIMLDEGNIMYDGSLDNLRTQ 248
Cdd:cd03291 188 GYLDVFTEKEIFEscVCKLMAN--KTRILVT----SKMEHLkkADKILILHEGSSYFYGTFSELQSL 248
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-246 |
2.25e-11 |
|
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: 64.93 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 32 NRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITvngmnpHKQREEFVrtigvvfgqrSQLW 111
Cdd:TIGR01271 433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK------HSGRISFS----------PQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 WDI--AVQESFrllkkVYGVSDAQYKE-------HMEHVIETL---DIGPLLDKPVrKLSLGQRMRCELAAALIHNPPLL 179
Cdd:TIGR01271 497 WIMpgTIKDNI-----IFGLSYDEYRYtsvikacQLEEDIALFpekDKTVLGEGGI-TLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 180 FLDEPTIGLDVLVKLKIRE--FLKEMNEryKTTILLTthdiTDIEAL--CERVIMLDEGNIMYDGSLDNLR 246
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFEscLCKLMSN--KTRILVT----SKLEHLkkADKILLLHEGVCYFYGTFSELQ 635
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-226 |
2.64e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 35 YKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGiLTPTSGQITVNG------MNPHKQR---EEFVRTIGVVFG 105
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGrveffnQNIYERRvnlNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSqlWWDIAVQESFrllkkVYGVSDAQYKEHME--HVIETL--------DIGPLLDKPVRKLSLGQRMRCELAAALIHN 175
Cdd:PRK14258 96 KPN--LFPMSVYDNV-----AYGVKIVGWRPKLEidDIVESAlkdadlwdEIKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488042473 176 PPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTTHDITDIEALCE 226
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
41-248 |
3.62e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT---------VNGMNPHKQRE--EFVRTIGVVFGQRSQ 109
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETPALPQPalEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 110 LWWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDIG-----PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:PRK10636 97 QLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGlgfsnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 185 TIGLDVLVKLKIREFLKEmnerYKTTILLTTHDITDIEALCERVIMLDEGNIM-YDGSLDNLRTQ 248
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLKS----YQGTLILISHDRDFLDPIVDKIIHIEQQSLFeYTGNYSSFEVQ 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-245 |
3.86e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG-----QITVNGMNPHKQRE--EFVRTIGVVFGQRSQLWWD 113
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 I-----AVQESFRLL--KKVYGVSDAQYKE--HMEHVIETLDigpllDKPVRkLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:PRK14271 117 ImdnvlAGVRAHKLVprKEFRGVAQARLTEvgLWDAVKDRLS-----DSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 185 TIGLDVLVKLKIREFLKEMNERYktTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNL 245
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-234 |
4.20e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 26 AFRDL--LNRNYKIVpaVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVngmnPHKQReefvrtigVV 103
Cdd:COG4178 364 ALEDLtlRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR----PAGAR--------VL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 104 F-GQRSQLwwdiaVQESFR--LLkkvY-----GVSDAQYKE-----HMEHVIETLDIGPLLDkpvRKLSLGQRMRCELAA 170
Cdd:COG4178 430 FlPQRPYL-----PLGTLReaLL---YpataeAFSDAELREaleavGLGHLAERLDEEADWD---QVLSLGEQQRLAFAR 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488042473 171 ALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEmnERYKTTILLTTHDITdIEALCERVIMLDEG 234
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRST-LAAFHDRVLELTGD 559
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-251 |
6.30e-11 |
|
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: 63.81 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 11 RKEFTAYS--SRPGLkgafrDLLNRnykivpavnDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN 88
Cdd:TIGR00957 1284 RVEFRNYClrYREDL-----DLVLR---------HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 89 phkqreefVRTIGvVFGQRSQLwwDIAVQE------SFRLLKKVYGvsdaQYKEhmEHVIETLDIGPLLD----KPVR-- 156
Cdd:TIGR00957 1350 --------IAKIG-LHDLRFKI--TIIPQDpvlfsgSLRMNLDPFS----QYSD--EEVWWALELAHLKTfvsaLPDKld 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 157 --------KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV----LVKLKIREFLKEmnerykTTILLTTHDITDIEAL 224
Cdd:TIGR00957 1413 hecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnLIQSTIRTQFED------CTVLTIAHRLNTIMDY 1486
|
250 260
....*....|....*....|....*..
gi 488042473 225 cERVIMLDEGNIMYDGSLDNLRTQWGV 251
Cdd:TIGR00957 1487 -TRVIVLDKGEVAEFGAPSNLLQQRGI 1512
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
55-243 |
6.45e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 55 GYIGENGAGKSTTIKMLTGILTPTSGQITvngMNPH----KQR------EEFvRTIGVVFGQRSQLWwdIAVQESFRllk 124
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVS---LDPNerlgKLRqdqfafEEF-TVLDTVIMGHTELW--EVKQERDR--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 125 kVYGVSDAQYKEHM-----EHVIETLD-------IGPLL----------DKPVRKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:PRK15064 102 -IYALPEMSEEDGMkvadlEVKFAEMDgytaearAGELLlgvgipeeqhYGLMSEVAPGWKLRVLLAQALFSNPDILLLD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 183 EPTIGLDVLVklkIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNI-MYDGSLD 243
Cdd:PRK15064 181 EPTNNLDINT---IRWLEDVLNER-NSTMIIISHDRHFLNSVCTHMADLDYGELrVYPGNYD 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
42-236 |
6.59e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQREEFVRTI----------GVVFGQRSQ 109
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGImlcpedrkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 110 LWWDIAVQESFRLLKKVygVSDAQYKEHMEHVIETLDI-GPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK11288 350 DNINISARRHHLRAGCL--INNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 189 DVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-236 |
6.69e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQIT-----VNGMNPhKQREEfvrtIGVVF----GQRSQLWWD 113
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeINALST-AQRLA----RGLVYlpedRQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVqeSFRLLKKVYG-----VSDAQYKEHMEHVIETLDIG-PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK15439 356 APL--AWNVCALTHNrrgfwIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 188 LDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
42-216 |
8.76e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.24 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 42 NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGI--LTPTSGQITVNG-----MNPHK----------QR---------EE 95
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGedileLSPDEraragiflafQYpveipgvsvSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 96 FVRTIgvvfgqrsqlwwdiavqesfrlLKKVYG--VSDAQYKEHMEHVIETLDIGP-LLDKPV-RKLSLGQRMRCELAAA 171
Cdd:COG0396 97 FLRTA----------------------LNARRGeeLSAREFLKLLKEKMKELGLDEdFLDRYVnEGFSGGEKKRNEILQM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488042473 172 LIHNPPLLFLDEPTIGLDV----LVKLKIREFLKEmneryKTTILLTTH 216
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIdalrIVAEGVNKLRSP-----DRGILIITH 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
45-233 |
1.22e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 45 SFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQitvngmnphkQREEFVRTIGVVFGQRSQLwwdiaVQESF---- 120
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE----------RQSQFSHITRLSFEQLQKL-----VSDEWqrnn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 121 ------------RLLKKVY--GVSDAQYKEHMEhviETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:PRK10938 88 tdmlspgeddtgRTTAEIIqdEVKDPARCEQLA---QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488042473 187 GLDVLVKLKIREFLKEMNERyKTTILLTTHDITDIEALCERVIMLDE 233
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-234 |
1.23e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.15 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILT--PTSGQITVNGmNPHKQR--EEFVRTIGVVFGQRSQLWWD 113
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSG-SPLKASniRDTERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 114 IAVQESFRLLKKV--------YGVSDAQYKEHMEHVieTLDIGPlLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:TIGR02633 93 LSVAENIFLGNEItlpggrmaYNAMYLRAKNLLREL--QLDADN-VTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488042473 186 IGL---DVLVKLKIREFLKemneRYKTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:TIGR02633 170 SSLtekETEILLDIIRDLK----AHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
43-247 |
2.83e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMN-PHKQREEF--VRTIGVVFGQRSQLWWDIAVQE- 118
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENiPAMSRSRLytVRKRMSMLFQSGALFTDMNVFDn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 -SFRLlkkvygvsdaqyKEHM---EHVIETLDIGPLLDKPVR--------KLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:PRK11831 105 vAYPL------------REHTqlpAPLLHSTVMMKLEAVGLRgaaklmpsELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 187 GLD-----VLVKLkirefLKEMNERYKTTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLRT 247
Cdd:PRK11831 173 GQDpitmgVLVKL-----ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-255 |
3.89e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.54 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 44 VSFTIKQGEMVGYIGENGAGKSTTIKMLTGI--LTP---TSGQITVNGMNPHKQR-EEFVRTIGVVFgQRSQLWWDIAVQ 117
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIFKMDvIELRRRVQMVF-QIPNPIPNLSIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ESFRLLKKVYGVSDAQyKEHMEHVIETLDIGPL-------LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK14247 101 ENVALGLKLNRLVKSK-KELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488042473 191 LVKLKIREFLKEMNEryKTTILLTTHDITDIEALCERVIMLDEGNIMydgsldnlrtQWGVEKEI 255
Cdd:PRK14247 180 ENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIV----------EWGPTREV 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-234 |
6.92e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQREEFVRTIGVVFGQRSQL----WW 112
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkINNHNANEAINHGFALVTEERRSTgiyaYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAV----------QESFRLLKKVYGVSDAQYkehmehVIETLDIG-PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFL 181
Cdd:PRK10982 342 DIGFnslisnirnyKNKVGLLDNSRMKSDTQW------VIDSMRVKtPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488042473 182 DEPTIGLDVLVKLKIREFLKEMNERYKTTILLTThDITDIEALCERVIMLDEG 234
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISS-EMPELLGITDRILVMSNG 467
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-234 |
8.51e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG--MNPHKQREEFVRTIGVVFgQRSQLWWDIA 115
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEALENGISMVH-QELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRL----LKKVYGVSDAQYKEhMEHVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL--- 188
Cdd:PRK10982 90 VMDNMWLgrypTKGMFVDQDKMYRD-TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtek 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488042473 189 DVLVKLKIREFLKEMNerykTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:PRK10982 169 EVNHLFTIIRKLKERG----CGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
43-242 |
1.06e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.86 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTP--TSGQITVNGMnPHKQrEEFVRTIGvvFGQRSQLWW-DIAVQES 119
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGF-PKKQ-ETFARISG--YCEQNDIHSpQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 120 F------RLLKKVygvSDAQYKEHMEHVIETLDIGPLLDKPV-----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PLN03140 974 LiysaflRLPKEV---SKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 189 D----VLVKLKIREFLKEmneryKTTILLTTH--DITDIEALCERVIMLDEGNIMYDGSL 242
Cdd:PLN03140 1051 DaraaAIVMRTVRNTVDT-----GRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSGPL 1105
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-252 |
1.88e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 31 LNRNYKIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQI--TVN---GMNPHKQREEFVRTIgVVFG 105
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENaniGYYAQDHAYDFENDL-TLFD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSQlwW------DIAVQESF-RLLkkvYGVSDAQykehmehvietldigplldKPVRKLSLGQRMRCELAAALIHNPPL 178
Cdd:PRK15064 404 WMSQ--WrqegddEQAVRGTLgRLL---FSQDDIK-------------------KSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042473 179 LFLDEPTIGLDVlvklkirEFLKEMN---ERYKTTILLTTHDITDIEALCERVI-MLDEGNIMYDGSLDN-LRTQwGVE 252
Cdd:PRK15064 460 LVMDEPTNHMDM-------ESIESLNmalEKYEGTLIFVSHDREFVSSLATRIIeITPDGVVDFSGTYEEyLRSQ-GIE 530
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-248 |
3.06e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 29 DLLNRNYKIVpavNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILT-PTSGQITVNGM-----NPhkqREEFVRTIGV 102
Cdd:PRK13549 269 DPVNPHIKRV---DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvkirNP---QQAIAQGIAM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 103 VFGQRSQ--LWWDIAVQESFRL--LKKVYGVS---DAQYKEHMEHVIETLDI-GPLLDKPVRKLSLGQRMRCELAAALIH 174
Cdd:PRK13549 343 VPEDRKRdgIVPVMGVGKNITLaaLDRFTGGSridDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488042473 175 NPPLLFLDEPTIGLDVLVKLKIrefLKEMNERYK--TTILLTTHDITDIEALCERVIMLDEGNIMYDGSLDNLrTQ 248
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEI---YKLINQLVQqgVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNL-TQ 494
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
51-252 |
3.16e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 51 GEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVN-----GMNPHKQReEFVRTIGVVFGQRSQLwwdiAVQESFRLLKK 125
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgiklGYFAQHQL-EFLRADESPLQHLARL----APQELEQKLRD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 126 VYGVSDAQykehmehvietldiGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDvlvkLKIREFLKEMNE 205
Cdd:PRK10636 413 YLGGFGFQ--------------GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEALI 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488042473 206 RYKTTILLTTHDITDIEALCERVIMLDEGNI-MYDGSLDNLRtQWGVE 252
Cdd:PRK10636 475 DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVePFDGDLEDYQ-QWLSD 521
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
41-236 |
4.09e-09 |
|
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: 54.85 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQItvnGMNPHK------QREEFvrTIGVVfgqRSQLW--W 112
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGEdllflpQRPYL--PLGTL---REQLIypW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DiavqesfrllkkvygvsdaqykehmehvietldigplldkpvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:cd03223 89 D------------------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488042473 193 KLKIREFLKEMneryKTTILLTTHDITdIEALCERVIMLD-EGNI 236
Cdd:cd03223 127 EDRLYQLLKEL----GITVISVGHRPS-LWKFHDRVLDLDgEGGW 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-234 |
4.40e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 1 MKSVIEVQGLRKEFtayssrPGLKgafrdllnrnykivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:PRK10762 1 MQALLQLKGIDKAF------PGVK---------------ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGMN-----PHKQRE--------------------------EFVRTIGVVFgqrsqlwWDIAVQESFRLLKKVyGV 129
Cdd:PRK10762 60 SILYLGKEvtfngPKSSQEagigiihqelnlipqltiaeniflgrEFVNRFGRID-------WKKMYAEADKLLARL-NL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 130 SdaqYKEHmehvietldigplldKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL-----DVLVKLkIREfLKEMN 204
Cdd:PRK10762 132 R---FSSD---------------KLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtetESLFRV-IRE-LKSQG 191
|
250 260 270
....*....|....*....|....*....|
gi 488042473 205 erykTTILLTTHDITDIEALCERVIMLDEG 234
Cdd:PRK10762 192 ----RGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
36-189 |
4.96e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 36 KIVPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNgmNPHKQRE---EFVRT-IGVVfgQRSQLW 111
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDinlKWWRSkIGVV--SQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 112 WDIAVQESFRL----LKKVYGVSDaQYKE------------------------------------HMEHVIETLD----- 146
Cdd:PTZ00265 472 FSNSIKNNIKYslysLKDLEALSN-YYNEdgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTIKdsevv 550
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 147 -----------IGPLLDK-------PVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:PTZ00265 551 dvskkvlihdfVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
39-276 |
9.22e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.64 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 39 PAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSQLWWDiAVQE 118
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLlkkvyGVSDAQyKEHMEHV---------IETLDIGPLLDKPVR--KLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK10789 408 NIAL-----GRPDAT-QQEIEHVarlasvhddILRLPQGYDTEVGERgvMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 188 LDVLVKLKIREFLKEMNEryKTTILLTTHDITdieALCE--RVIMLDEGNIMYDGSLDNLRTQWGVEKEIHfqfvapvSY 265
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGE--GRTVIISAHRLS---ALTEasEILVMQHGHIAQRGNHDQLAQQSGWYRDMY-------RY 549
|
250
....*....|.
gi 488042473 266 QELSMVMPDSH 276
Cdd:PRK10789 550 QQLEAALDDAP 560
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
38-218 |
2.26e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.87 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIG---VVFGQRSQLWWDI 114
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 115 AVQESFrllkkVYGvsDAQYKEHMEHVIETLDIGPLLD-----------KPVRKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:cd03290 94 TVEENI-----TFG--SPFNKQRYKAVTDACSLQPDIDllpfgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488042473 184 PTIGLDV-----LVKLKIREFLKEMneryKTTILLTTHDI 218
Cdd:cd03290 167 PFSALDIhlsdhLMQEGILKFLQDD----KRTLVLVTHKL 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-217 |
2.55e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 36 KIVPA----VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQ------ITVnGM---NPHKQREEFVRtiGV 102
Cdd:PRK11819 14 KVVPPkkqiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKV-GYlpqEPQLDPEKTVR--EN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 103 VfgqrsqlwwDIAVQESFRLLKKV------YGVSDAQYKEHME--------------HVIET-LDIG------PLLDKPV 155
Cdd:PRK11819 91 V---------EEGVAEVKAALDRFneiyaaYAEPDADFDALAAeqgelqeiidaadaWDLDSqLEIAmdalrcPPWDAKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042473 156 RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKemneRYKTTILLTTHD 217
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLH----DYPGTVVAVTHD 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
43-236 |
3.68e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITvngmnphkqREEFVRTigVVFGQRSQLWWDIAVQESFRL 122
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---------RSAKVRM--AVFSQHHVDGLDLSSNPLLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 123 LKKVYGVSDAQYKEHMEHVIETldiGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDvlvkLKIREFLKE 202
Cdd:PLN03073 596 MRCFPGVPEQKLRAHLGSFGVT---GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQ 668
|
170 180 190
....*....|....*....|....*....|....
gi 488042473 203 MNERYKTTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:PLN03073 669 GLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-234 |
3.82e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 4 VIEVQGLRKEFtayssrPGLKgafrdllnrnykivpAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILtPT---SG 80
Cdd:NF040905 1 ILEMRGITKTF------PGVK---------------ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 81 QITVNGmnphkQREEFvRTI------GVVF-----------------------GQRSQLWWDIAVQESFRLLKKVygvsd 131
Cdd:NF040905 59 EILFDG-----EVCRF-KDIrdsealGIVIihqelalipylsiaeniflgnerAKRGVIDWNETNRRARELLAKV----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 132 aqykehmehvieTLDIGPllDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL-----DVLVKLkirefLKEMNER 206
Cdd:NF040905 128 ------------GLDESP--DTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneedsAALLDL-----LLELKAQ 188
|
250 260
....*....|....*....|....*...
gi 488042473 207 YKTTILLtTHDITDIEALCERVIMLDEG 234
Cdd:NF040905 189 GITSIII-SHKLNEIRRVADSITVLRDG 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-216 |
9.45e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.54 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGIL-----TPTSGQITVNGMN---PHKQREEFVRTIGVVFgQRSQLWW 112
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiysPDVDPIEVRREVGMVF-QYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAVQESFRLLKKVYGVSDAQyKEHMEHVIETLDIGPLLDKPVRKL-------SLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLVKSK-KELDERVEWALKKAALWDEVKDRLndypsnlSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190
....*....|....*....|....*....|.
gi 488042473 186 IGLDVLVKLKIREFLKEMNERYktTILLTTH 216
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
43-248 |
1.29e-07 |
|
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: 53.38 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTpTSGQITVNGMN-----PHKQREEF---VRTIGVVFGQ-RSQL--- 110
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSwnsvtLQTWRKAFgviPQKVFIFSGTfRKNLdpy 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 --WWDiavQESFRLLKKVyGVSDA--QYKEHMEHVIEtlDIGPLldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:TIGR01271 1316 eqWSD---EEIWKVAEEV-GLKSVieQFPDKLDFVLV--DGGYV-------LSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488042473 187 GLDVLVKLKIREFLKEMNEryKTTILLTTHditDIEAL--CERVIMLDEGNIMYDGSLDNLRTQ 248
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQSFS--NCTVILSEH---RVEALleCQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
54-189 |
1.79e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 54 VGYI-GENGAGKSTTIKMLTGILTPTSGQITVNGMNPHKQREEFVRTIGVVFGQRSqlwwDIAVQESFRLLKKVYGVSDA 132
Cdd:PRK13541 28 ITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKL----EMTVFENLKFWSEIYNSAET 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488042473 133 QYKehmehVIETLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:PRK13541 104 LYA-----AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
43-262 |
7.65e-07 |
|
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: 49.85 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTpTSGQITVNGMNPHK-QREEFVRTIGVV-----------------F 104
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGVIpqkvfifsgtfrknldpY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 105 GQRS-QLWWDIAVQESFRLLKKvygvsdaQYKEHMEHVIEtlDIGPLldkpvrkLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:cd03289 101 GKWSdEEIWKVAEEVGLKSVIE-------QFPGQLDFVLV--DGGCV-------LSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 184 PTIGLDVLVKLKIREFLKEMNEryKTTILLTTHditDIEAL--CERVIMLDEGNIMYDGSLDNLRTqwgvEKEIHFQFVA 261
Cdd:cd03289 165 PSAHLDPITYQVIRKTLKQAFA--DCTVILSEH---RIEAMleCQRFLVIEENKVRQYDSIQKLLN----EKSHFKQAIS 235
|
.
gi 488042473 262 P 262
Cdd:cd03289 236 P 236
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
57-217 |
2.09e-06 |
|
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: 47.60 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 57 IGENGAGKSTTI---KM-LTGILTPTSgqiTVNGMNPHKQREEFVRT-IGVVFGQRSQLwwDIAVQESFRLLKKVYGVSD 131
Cdd:cd03240 28 VGQNGAGKTTIIealKYaLTGELPPNS---KGGAHDPKLIREGEVRAqVKLAFENANGK--KYTITRSLAILENVIFCHQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 132 AQYKEhmehvietldigPLLDKPVRkLSLGQRM------RCELAAALIHNPPLLFLDEPTIGLDV-LVKLKIREFLKEMN 204
Cdd:cd03240 103 GESNW------------PLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERK 169
|
170
....*....|...
gi 488042473 205 ERYKTTILLTTHD 217
Cdd:cd03240 170 SQKNFQLIVITHD 182
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
33-225 |
5.47e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 47.69 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 33 RNYKivpAVNDVSFTIKQGEMVgYIGENGAGKSTTIKMLTGILTPTSG-QITVNGMNPHKQREEFVRTIGVVFGQR-SQL 110
Cdd:COG3593 9 KNFR---SIKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSrKFDEEDFYLGDDPDLPEIEIELTFGSLlSRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 WWDIAVQESFRLLKKVYGVSDAQYKEHMEHVIETL-------------DIGPLLDK------------------PVRKLS 159
Cdd:COG3593 85 LRLLLKEEDKEELEEALEELNEELKEALKALNELLseylkelldgldlELELSLDEledllkslslriedgkelPLDRLG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488042473 160 LGQR------MRCELA-AALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERyKTTILLTTH-----DITDIEALC 225
Cdd:COG3593 165 SGFQrlillaLLSALAeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEK-PNQVIITTHsphllSEVPLENIR 241
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
43-245 |
1.88e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 43 DVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPT---SGQITVNGMnphkQREEFV-RTIGVVFGQRSQLWWDIAVQE 118
Cdd:PLN03140 183 DASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGY----RLNEFVpRKTSAYISQNDVHVGVMTVKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 119 SFRLLKKVYGV-------SDAQYKEH------------------MEHV-----------IETLDIGP---LLDKPVRKLS 159
Cdd:PLN03140 259 TLDFSARCQGVgtrydllSELARREKdagifpeaevdlfmkataMEGVksslitdytlkILGLDICKdtiVGDEMIRGIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 160 LGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLT-------THDITDiealceRVIMLD 232
Cdd:PLN03140 339 GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSllqpapeTFDLFD------DIILLS 412
|
250
....*....|...
gi 488042473 233 EGNIMYDGSLDNL 245
Cdd:PLN03140 413 EGQIVYQGPRDHI 425
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
38-222 |
3.28e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 38 VPAVNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITV------NGMNPHKQRE-------------EFVR 98
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfknehtNDMTNEQDYQgdeeqnvgmknvnEFSL 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 99 TIGVVFGQRSQLW------------------------WDIAVQESFRLLKKVY-----GVSDAQYKE--------HMEHV 141
Cdd:PTZ00265 1261 TKEGGSGEDSTVFknsgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIYenikfGKEDATREDvkrackfaAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 142 IETL------DIGPLldkpVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKTTILLTT 215
Cdd:PTZ00265 1341 IESLpnkydtNVGPY----GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIA 1416
|
....*..
gi 488042473 216 HDITDIE 222
Cdd:PTZ00265 1417 HRIASIK 1423
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-221 |
6.84e-05 |
|
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: 42.36 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 50 QGEMVGYIGENGAGKSTTIKMLTGILTPTSGQ-ITVNGMNPHKQREEFVRTIGVVFGQRSqlwwdiavqesfrllkkvyg 128
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGGKKAS-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 129 vsdaqykehmehvietldigplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV-----LVKLKIREFLKEM 203
Cdd:smart00382 61 -----------------------------GSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLLLL 111
|
170
....*....|....*...
gi 488042473 204 NERYKTTILLTTHDITDI 221
Cdd:smart00382 112 KSEKNLTVILTTNDEKDL 129
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
41-204 |
8.22e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.35 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVngmnPHKQREEFV-----RTIGVVfgqRSQLWWDIA 115
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK----PAKGKLFYVpqrpyMTLGTL---RDQIIYPDS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 116 VQESFRllkkvYGVSDAQykehMEHVIETLDIGPLLDKPV---------RKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:TIGR00954 541 SEDMKR-----RGLSDKD----LEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170
....*....|....*...
gi 488042473 187 GLDVLVKLKIREFLKEMN 204
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREFG 629
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
113-222 |
8.97e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.53 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 DIAVQESFRLLKKVYGVSDAQYKEHMEHVIETLDiGPLldkPVRKLSLGQRmRCELAAALIH----NPPLLFLDEPTIGL 188
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGG-GEL---PAFELSDGTK-RLLALLAALLsalpKGGLLLIDEPESGL 270
|
90 100 110
....*....|....*....|....*....|....
gi 488042473 189 DVLVKLKIREFLKEmNERYKTTILLTTHDITDIE 222
Cdd:pfam13304 271 HPKLLRRLLELLKE-LSRNGAQLILTTHSPLLLD 303
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
41-236 |
9.29e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKsTTIKML-------TGIltptSGQITVNGmnphkqREEFVRT--------IGVVFG 105
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGR-TELAMSvfgrsygRNI----SGTVFKDG------KEVDVSTvsdaidagLAYVTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 106 QRSQ----LWWDIAVQESFRLLKKV--YGVSDaqykEHMEHVI-----ETLDI-GPLLDKPVRKLSLGQRMRCELAAALI 173
Cdd:NF040905 345 DRKGyglnLIDDIKRNITLANLGKVsrRGVID----ENEEIKVaeeyrKKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042473 174 HNPPLLFLDEPTIGLDVLVKLKIREFLKEMNERYKtTILLTTHDITDIEALCERVIMLDEGNI 236
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
33-217 |
3.80e-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: 40.42 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 33 RNYKIVPAVNDVSFTikQGEMVGYIGENGAGKSTTIkmltgiltptsgqitvngmnphkqreefvRTIGVVFGQRSQLww 112
Cdd:cd03227 5 GRFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTIL-----------------------------DAIGLALGGAQSA-- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 113 diavqesfrlLKKVYGVSDAQYK--EHMEHVIEtldigplldkpVRKLSLGQRMRCELAAALIH---NP-PLLFLDEPTI 186
Cdd:cd03227 52 ----------TRRRSGVKAGCIVaaVSAELIFT-----------RLQLSGGEKELSALALILALaslKPrPLYILDEIDR 110
|
170 180 190
....*....|....*....|....*....|.
gi 488042473 187 GLDVLVKLKIREFLKEMNERyKTTILLTTHD 217
Cdd:cd03227 111 GLDPRDGQALAEAILEHLVK-GAQVIVITHL 140
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-86 |
7.39e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 7.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042473 27 FRDLLNRNYKIVPAV-NDVSFTIKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGQITVNG 86
Cdd:PTZ00243 1311 FEGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG 1371
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
41-216 |
9.75e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.01 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 41 VNDVSFTIKQGEMVGYIGENGAGKSTTIKMLTG--ILTPTSGQITVNGMNPHKQREEfvrtigvvfgQRSQLWWDIAVQ- 117
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPE----------ERAHLGIFLAFQy 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 118 ---------ESFRLL-----KKVYGVSDAQYKEHMEHVIETLDIGPL----LDKPVRK-LSLGQRMRCELAAALIHNPPL 178
Cdd:CHL00131 93 pieipgvsnADFLRLaynskRKFQGLPELDPLEFLEIINEKLKLVGMdpsfLSRNVNEgFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488042473 179 LFLDEPTIGLDVLVkLKI--REFLKEMNEryKTTILLTTH 216
Cdd:CHL00131 173 AILDETDSGLDIDA-LKIiaEGINKLMTS--ENSIILITH 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
153-239 |
1.03e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 153 KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIREFLKemneRYKTTILLTTHD-------ITDIEALC 225
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSHAreflntvVTDILHLH 415
|
90
....*....|....
gi 488042473 226 ERVIMLDEGNimYD 239
Cdd:PLN03073 416 GQKLVTYKGD--YD 427
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
35-222 |
4.95e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 37.30 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 35 YKIVPA----VNDVSFTIKQGEMVGYIGENGAGKSTTIkmLTGIltPTSGQITVNgmnphKQREEFVRTIGVVFGQRSql 110
Cdd:cd03238 1 LTVSGAnvhnLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGL--YASGKARLI-----SFLPKFSRNKLIFIDQLQ-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042473 111 wwdiavqesfRLLKkvygvsdaqykehmehvietLDIGPL-LDKPVRKLSLGQRMRCELAAALIHNPP--LLFLDEPTIG 187
Cdd:cd03238 70 ----------FLID--------------------VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190
....*....|....*....|....*....|....*
gi 488042473 188 LDVLVKLKIREFLKEMNERyKTTILLTTHDITDIE 222
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLS 153
|
|
| |
