|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-227 |
8.75e-96 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 282.72 E-value: 8.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQ 91
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLDLVASYAANPLDP-----HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEareriDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 167 GMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-213 |
2.97e-72 |
|
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: 220.73 E-value: 2.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQ 91
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLdlvasyaanpldphwlldtlglteaaratyrRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH 171
Cdd:cd03230 81 EPSLYENLTVRENL-------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489998165 172 ARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03230 130 SRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-308 |
3.99e-68 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 214.56 E-value: 3.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQGGGGYPA 98
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 ARAGEMLDLVASYAANPLD-----PHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHAR 173
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDeaeerAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 174 VLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKDQLRFTAPPRLDLSLLASALP-- 251
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVSMLIae 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 252 -----EGYQATELTPGEYLVEGPVDPQVLATVTAWCAQIDVLATDMRVEQRSLEDVFLDLTG 308
Cdd:TIGR01188 241 lgetgLGLLAVTVDSDRIKILVPDGDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKLTG 302
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-234 |
1.31e-64 |
|
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: 203.55 E-value: 1.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVML 90
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGGGGYPAARAGEMLDLVAsyAANPLDPHW-------LLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:COG4555 81 DERGLYDRLTVRENIRYFA--ELYGLFDEElkkrieeLIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 164 PTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKDQLR 234
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-224 |
3.38e-64 |
|
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: 201.58 E-value: 3.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSI--TAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVM 89
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQGGGGYPAARAGEMLDLVA-----SYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEP 164
Cdd:cd03263 81 PQFDALFDELTVREHLRFYArlkglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 165 TAGMDAHARVLVWELIDALRRdGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-310 |
6.90e-61 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 195.71 E-value: 6.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARlrARIGVML 90
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDPEDR--RRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGGGGYPAARAGEML-------DLVASYAANPLDpHWLlDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:COG4152 78 EERGLYPKMKVGEQLvylarlkGLSKAEAKRRAD-EWL-ERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 164 PTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKDQLRFTAPprldL 243
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEAD----G 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 244 SLLASALPEGYQATELTPGEYLV--EGPVDPQ-VLATVTawcAQIDVlaTDMRVEQRSLEDVFLDLTGRK 310
Cdd:COG4152 232 DAGWLRALPGVTVVEEDGDGAELklEDGADAQeLLRALL---ARGPV--REFEEVRPSLNEIFIEVVGEK 296
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-224 |
2.11e-59 |
|
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: 189.50 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQGGGGYPA 98
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 ARAGEMLDLVASYAANPLDP-----HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHAR 173
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAErreriDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489998165 174 VLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:cd03265 168 AHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-227 |
1.81e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.58 E-value: 1.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 7 TPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPitdnARLRARI 86
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP----RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGG---GGYPAaRAgemLDLVASYaanpLDPHW----------------LLDTLGLTEAARATYRRLSGGQQQRLA 147
Cdd:COG1121 78 GYVPQRAevdWDFPI-TV---RDVVLMG----RYGRRglfrrpsradreavdeALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 148 LACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVtVAAGTPAELMRS 227
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGPPEEVLTP 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-226 |
5.09e-52 |
|
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: 170.98 E-value: 5.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR-LRARIGVM 89
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLReLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQggggYPAA--------------------RAGEMLDLVasyaanpldpHWLLDTLGLTE-AARATYRrLSGGQQQRLAL 148
Cdd:COG1122 81 FQ----NPDDqlfaptveedvafgpenlglPREEIRERV----------EEALELVGLEHlADRPPHE-LSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 149 ACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMR 226
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-226 |
1.17e-51 |
|
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: 170.60 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 8 PEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD-NARLRARI 86
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD-ITGlPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 G-------------------VML--QGGGGYPAARAGEMLDLV-ASYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQ 144
Cdd:COG0411 80 GiartfqnprlfpeltvlenVLVaaHARLGRGLLAALLRLPRArREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 145 RLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAE 223
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
...
gi 489998165 224 LMR 226
Cdd:COG0411 240 VRA 242
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-219 |
5.32e-51 |
|
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: 167.46 E-value: 5.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARlrARIGVMLQ 91
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-KPLDIAAR--NRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLDLVAS-------YAANPLDpHWLlDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEP 164
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQlkglkkeEARRRID-EWL-ERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 165 TAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-313 |
5.54e-51 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 171.55 E-value: 5.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 8 PEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLdPITDNARL-RARI 86
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV-PVPARARLaRARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGGYPAARAGEMLDLVASY---------AANPLdphwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQ 157
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYfgmstreieAVIPS----LLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 158 LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS---------- 227
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEhigcqvieiy 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 228 -GAKDQLRFTAPPRLdlsllasalpegyQATELTpGEYLVEGPVDP-QVLATVTAWcaqidvlaTDMRVEQR--SLEDVF 303
Cdd:PRK13536 273 gGDPHELSSLVKPYA-------------RRIEVS-GETLFCYAPDPeQVRVQLRGR--------AGLRLLQRppNLEDVF 330
|
330
....*....|
gi 489998165 304 LDLTGRKLRQ 313
Cdd:PRK13536 331 LRLTGREMEK 340
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-219 |
7.01e-51 |
|
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: 167.01 E-value: 7.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPiTDNARLRARIGVMLQ 91
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLDLVASYAANP-LDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDA 170
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRkKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489998165 171 HARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-227 |
1.06e-50 |
|
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: 167.61 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIG---- 87
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 ---------------VML----QGGGGYPAARAGEMLDLVASYAanpldpHWLLDTLGLTEAARATYRRLSGGQQQRLAL 148
Cdd:cd03219 81 fqiprlfpeltvlenVMVaaqaRTGSGLLLARARREEREARERA------EELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 149 ACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-227 |
3.54e-49 |
|
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: 164.00 E-value: 3.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 7 TPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD----PITDNARL 82
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQGG-------------------GGYPAAragEMLDLVASYaanpldphwlLDTLGLTEAARATYRRLSGGQQ 143
Cdd:COG1127 81 RRRIGMLFQGGalfdsltvfenvafplrehTDLSEA---EIRELVLEK----------LELVGLPGAADKMPSELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 144 QRLALACALVGRPQLVFLDEPTAGMDAH-ARVLVwELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTP 221
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPItSAVID-ELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
....*.
gi 489998165 222 AELMRS 227
Cdd:COG1127 227 EELLAS 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-312 |
4.16e-49 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 165.75 E-value: 4.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 8 PEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARL-RARI 86
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHaRQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGGYPAARAGEMLDLVASY------AANPLDPHwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVF 160
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYfglsaaAARALVPP-LLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 161 LDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAK-DQLRFTAPP 239
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGcDVIEIYGPD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 240 RLDLSLLASALPEgyqATELTpGEYLVEGPVDPQ-VLATVTAwcaqidvlATDMRVEQR--SLEDVFLDLTGRKLR 312
Cdd:PRK13537 242 PVALRDELAPLAE---RTEIS-GETLFCYVRDPEpLHARLKG--------RAGLRYLHRpaNLEDVFLRLTGREMQ 305
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-224 |
9.95e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.04 E-value: 9.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD---NARlraRIGV 88
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-VTGlppEKR---NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGGG-----------GYP-----------AARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGGQQQRL 146
Cdd:COG3842 82 VFQDYAlfphltvaenvAFGlrmrgvpkaeiRARVAELLELV-----------------GLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARV-LVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREeMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-219 |
1.91e-47 |
|
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: 159.42 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKR-YGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVML-- 90
Cdd:cd03267 23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 --QGGGGYPAARAGEML----DLVASYAANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEP 164
Cdd:cd03267 103 ktQLWWDLPVIDSFYLLaaiyDLPPARFKKRLDE--LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 165 TAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-213 |
2.73e-47 |
|
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: 156.25 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 13 RLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDP-ITDNARLRARIGVMLQ 91
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 ggggypaaragemldlvasyaanpldphwlldtlglteaaratyrrLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH 171
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489998165 172 ARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-302 |
3.53e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 161.02 E-value: 3.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKR-YGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIG-VMLQ 91
Cdd:COG4586 24 LKGLFRReYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGvVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 ggggypaaR--------AGEMLDLVAS--------YAANpLDphWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGR 155
Cdd:COG4586 104 --------RsqlwwdlpAIDSFRLLKAiyripdaeYKKR-LD--ELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKD--- 231
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYkti 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 232 QLRFTAPPRldlsllASALPEGYQATELTPGEYLVEgpVDPQV-LATVTAWC-AQIDVlaTDMRVEQRSLEDV 302
Cdd:COG4586 253 VLELAEPVP------PLELPRGGEVIEREGNRVRLE--VDPREsLAEVLARLlARYPV--RDLTIEEPPIEEV 315
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-213 |
2.23e-45 |
|
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: 153.01 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 13 RLRGVCKRYGS--ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR-LRARIGVM 89
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQggggYP-----AARAGEmlDLVASYAANPLDPHW-------LLDTLGLTE-AARATYRrLSGGQQQRLALACALVGRP 156
Cdd:cd03225 81 FQ----NPddqffGPTVEE--EVAFGLENLGLPEEEieerveeALELVGLEGlRDRSPFT-LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 157 QLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
12-219 |
4.79e-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: 152.29 E-value: 4.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNARLRARIGVMLQ 91
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD-VTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLDLVASYAANPLDP-----HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEirarvRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489998165 167 GMDAHARV-LVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03259 160 ALDAKLREeLREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-219 |
7.62e-45 |
|
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: 152.14 E-value: 7.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIG 87
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQGGGGYPAARAGEMLDLVAS-YAANPLDPH----WLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLD 162
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGlYGLKGDELTarleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 163 EPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
11-225 |
9.32e-44 |
|
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: 150.19 E-value: 9.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITD-NARLRAR-IGV 88
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLASlSRRELARrIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGGGGYPAARAgemLDLVASYAAnpldPH----------------WLLDTLGLTEAARATYRRLSGGQQQRLALACAL 152
Cdd:COG1120 80 VPQEPPAPFGLTV---RELVALGRY----PHlglfgrpsaedreaveEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489998165 153 VGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-227 |
2.69e-43 |
|
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: 148.42 E-value: 2.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNA----RLRARIG 87
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQGGG-----------GYP-----AARAGEMLDLVASYaanpldphwlLDTLGLTEAARATYRRLSGGQQQRLALACA 151
Cdd:cd03261 81 MLFQSGAlfdsltvfenvAFPlrehtRLSEEEIREIVLEK----------LEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 152 LVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-213 |
3.12e-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: 146.56 E-value: 3.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDNAR-LRARIGV 88
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPpLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGGGgypaaragemldlvasyaanpLDPHwlldtlgLTEAARATYRrLSGGQQQRLALACALVGRPQLVFLDEPTAGM 168
Cdd:cd03229 81 VFQDFA---------------------LFPH-------LTVLENIALG-LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489998165 169 DAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03229 132 DPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-201 |
4.72e-42 |
|
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: 144.16 E-value: 4.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVML 90
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGGGGYPAARAGEMLDLVASY---AANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAG 167
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALyglRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....
gi 489998165 168 MDAHARVLVWELIDALRRDGVTVVLTTHHLKEAE 201
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-224 |
5.28e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.58 E-value: 5.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR----LRAR 85
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQGG-----------------GGYPAARAgeMLDLVasYAANPLDPHWLLDTLGLTEAA--RAtyRRLSGGQQQRL 146
Cdd:COG3638 82 IGMIFQQFnlvprlsvltnvlagrlGRTSTWRS--LLGLF--PPEDRERALEALERVGLADKAyqRA--DQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-210 |
2.03e-41 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 143.00 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGS----ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITdnaRLRARIG 87
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-EPVT---GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQGGGGYP----------------------AARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGGQQQR 145
Cdd:cd03293 77 YVFQQDALLPwltvldnvalglelqgvpkaeaRERAEELLELV-----------------GLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 146 LALACALVGRPQLVFLDEPTAGMDAHARVLVW-ELIDALRRDGVTVVLTTHHLKEAEELADRLVII 210
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-217 |
2.66e-41 |
|
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: 141.03 E-value: 2.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDNARLRARIGVM 89
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQggggypaaragemldlvasyaanpldphwlldtlglteaaratyrrLSGGQQQRLALACALVGRPQLVFLDEPTAGMD 169
Cdd:cd03216 81 YQ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489998165 170 AHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVA 217
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-219 |
3.34e-41 |
|
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: 142.29 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 20 RYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPitdnARLRARIGVMLQGGG---GY 96
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKRIGYVPQRRSidrDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 97 PAArageMLDLVASyaanPLDPHW----------------LLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVF 160
Cdd:cd03235 84 PIS----VRDVVLM----GLYGHKglfrrlskadkakvdeALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 161 LDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVtVAAG 219
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV-VASG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-225 |
3.35e-41 |
|
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: 142.57 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD-NARLRARIGVML 90
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD-ITGlPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 --QGGGGYPAARAGEMLdLVASYAANPLDPHWLLDTL-----GLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:cd03224 80 vpEGRRIFPELTVEENL-LLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 164 PTAGMdahARVLV---WELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:cd03224 159 PSEGL---APKIVeeiFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-227 |
9.02e-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: 148.51 E-value: 9.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 3 RAPDTPEVVLRLRGVCKRY-----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT 77
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 78 DNAR----LRARIGVMLQGgggyPAA------RAGEMLdlvasyaANPLDPH-------------WLLDTLGLTEAARAT 134
Cdd:COG1123 332 LSRRslreLRRRVQMVFQD----PYSslnprmTVGDII-------AEPLRLHgllsraerrervaELLERVGLPPDLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 135 Y-RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDH 212
Cdd:COG1123 401 YpHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYD 480
|
250
....*....|....*
gi 489998165 213 GVTVAAGTPAELMRS 227
Cdd:COG1123 481 GRIVEDGPTEEVFAN 495
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-227 |
2.86e-40 |
|
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: 140.50 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD---NARLRAR 85
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-ITGlppHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQGGGGYPaaragEM-----LDLVASYAANPLDPHWLLDT-------LGLTEAARATYrrLSGGQQQRLALACALV 153
Cdd:COG0410 80 IGYVPEGRRIFP-----SLtveenLLLGAYARRDRAEVRADLERvyelfprLKERRRQRAGT--LSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 154 GRPQLVFLDEPTAGMdahARVLV---WELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:COG0410 153 SRPKLLLLDEPSLGL---APLIVeeiFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-217 |
3.29e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.18 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGS----ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDN----A 80
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRAR-IGVMLQGGGGYPAARAGEMLDLVASYAANPLDP-----HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVG 154
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKErreraRELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489998165 155 RPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLkEAEELADRLVIIDHGVTVA 217
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-219 |
3.42e-40 |
|
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: 138.72 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 13 RLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRAR-IGVMLQ 91
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 ggggypaaragemldlvasyaanpldphwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH 171
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489998165 172 ARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03214 132 HQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-224 |
3.51e-40 |
|
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: 140.45 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARLRARIGVMLQ 91
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG-KDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYP----------------------AARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGGQQQRLALA 149
Cdd:cd03300 80 NYALFPhltvfeniafglrlkklpkaeiKERVAEALDLV-----------------QLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 150 CALVGRPQLVFLDEPTAGMDAHARV-LVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKdMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-213 |
3.65e-40 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 139.64 E-value: 3.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVhDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQ 91
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLDLVAS-YAANPLDPH----WLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWlKGIPSKEVKarvdEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489998165 167 GMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03264 160 GLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-213 |
6.22e-40 |
|
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: 139.16 E-value: 6.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGS----ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDN----ARLR 83
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 84 AR-IGVMLQGGGGYPAARAGEMLDLVASYAANPLDP-----HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQ 157
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKErreraEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 158 LVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLkEAEELADRLVIIDHG 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDG 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-240 |
6.32e-40 |
|
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: 140.13 E-value: 6.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSIT-AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPI-TDNARLRARIGVM 89
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQGGGGYP----------------------AARAGEMLDLVAsyaanpLDPHWLLDTlglteaaratY-RRLSGGQQQRL 146
Cdd:cd03295 81 IQQIGLFPhmtveenialvpkllkwpkekiRERADELLALVG------LDPAEFADR----------YpHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARV-LVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDqLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250
....*....|....*.
gi 489998165 226 RSGAKDQLR-FTAPPR 240
Cdd:cd03295 225 RSPANDFVAeFVGADR 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-227 |
6.60e-40 |
|
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: 139.60 E-value: 6.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVmlq 91
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 gggGYPAARAG---------------EMLDLVASYAANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRP 156
Cdd:cd03218 78 ---GYLPQEASifrkltveenilavlEIRGLSKKEREEKLEE--LLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 157 QLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
12-229 |
6.99e-40 |
|
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: 142.87 E-value: 6.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD------------- 78
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRD-ITRlppqkrdygivfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 79 ------NARLRARIGVMLQGGGGYPA---ARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGGQQQRLALA 149
Cdd:TIGR03265 84 syalfpNLTVADNIAYGLKNRGMGRAevaERVAELLDLV-----------------GLPGSERKYPGQLSGGQQQRVALA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 150 CALVGRPQLVFLDEPTAGMDAHARV-LVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:TIGR03265 147 RALATSPGLLLLDEPLSALDARVREhLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHP 226
|
.
gi 489998165 229 A 229
Cdd:TIGR03265 227 A 227
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
11-227 |
1.51e-39 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 138.95 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD-NARLRARIGVm 89
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQD-ITHlPMHERARLGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 lqgggGYPAARAGEMLDL-VA-------------SYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGR 155
Cdd:TIGR04406 79 -----GYLPQEASIFRKLtVEenimavleirkdlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVAN 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-227 |
2.95e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 141.05 E-value: 2.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITD-NARLRaRIGVML 90
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRER-RVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 Q------------------GGGGYP----AARAGEMLDLVasyaanpldphwlldtlGLTEAARatyRR---LSGGQQQR 145
Cdd:COG1118 82 QhyalfphmtvaeniafglRVRPPSkaeiRARVEELLELV-----------------QLEGLAD---RYpsqLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 146 LALACALVGRPQLVFLDEPTAGMDAHARVLVW-ELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRrWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
...
gi 489998165 225 MRS 227
Cdd:COG1118 222 YDR 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-227 |
5.18e-39 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 137.91 E-value: 5.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAG-SIEVLGLDPITDNAR-LRARI 86
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWeLRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GV----MLQGgggYPA-ARAgemLDLVAS--YAA----NPLDP------HWLLDTLGLTEAARATYRRLSGGQQQRLALA 149
Cdd:COG1119 81 GLvspaLQLR---FPRdETV---LDVVLSgfFDSiglyREPTDeqreraRELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 150 CALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDG-VTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-209 |
2.54e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.37 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 7 TPEVVLRLRGVCKRY----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITdnaRL 82
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-KPVT---GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQGGGGYP----------------------AARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSG 140
Cdd:COG1116 79 GPDRGVVFQEPALLPwltvldnvalglelrgvpkaerRERARELLELV-----------------GLAGFEDAYPHQLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 141 GQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVW-ELIDALRRDGVTVVLTTHHLKEAEELADRLVI 209
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQdELLRLWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-224 |
3.36e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 135.16 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITdnaRL----RARI 86
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED-IT---HLpmhkRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVmlqgggGYPAARAG---------------EMLDLVASYAANPLDphWLLDTLGLTEAARATYRRLSGGQQQRLALACA 151
Cdd:COG1137 79 GI------GYLPQEASifrkltvednilavlELRKLSKKEREERLE--ELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 152 LVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-214 |
1.49e-37 |
|
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: 132.76 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNARLRARIGVMLQ 91
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLDLVASYAANPLDP-----HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEidervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489998165 167 GMDAHARV-LVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGV 214
Cdd:cd03301 160 NLDAKLRVqMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-224 |
2.04e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 136.36 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIE-----VLGLDPitdnarlRAR- 85
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdVTDLPP-------KDRn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQggggypaaragemldlvaSYAanpLDPH--------------------------WLLDTLGLTEAARATYRRLS 139
Cdd:COG3839 77 IAMVFQ------------------SYA---LYPHmtvyeniafplklrkvpkaeidrrvrEAAELLGLEDLLDRKPKQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 140 GGQQQRLALACALVGRPQLVFLDEPTAGMDAHARV-LVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAA 218
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVeMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQV 215
|
....*.
gi 489998165 219 GTPAEL 224
Cdd:COG3839 216 GTPEEL 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-224 |
1.77e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.88 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG---LDPITDNARLRARIG 87
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedlTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 -----------------VMLqggG-----GYPAA----RAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGG 141
Cdd:COG1126 81 mvfqqfnlfphltvlenVTL---ApikvkKMSKAeaeeRAMELLERV-----------------GLADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 142 QQQRLALACALVGRPQLVFLDEPTAGMDAH--ARVLvwELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPElvGEVL--DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
....*
gi 489998165 220 TPAEL 224
Cdd:COG1126 219 PPEEF 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
2.21e-36 |
|
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: 128.27 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGS--ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNAR--LRARIG 87
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRDLDLesLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQggggypaaragemldlvasyaanplDPHWLLDTLglteaaratyrR---LSGGQQQRLALACALVGRPQLVFLDEP 164
Cdd:cd03228 80 YVPQ-------------------------DPFLFSGTI-----------ReniLSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489998165 165 TAGMDAHARVLVWELIDALrRDGVTVVLTTHHLkEAEELADRLVIIDHG 213
Cdd:cd03228 124 TSALDPETEALILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-213 |
7.51e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 7.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNA--RLRARIGvm 89
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG-KPLSAMPppEWRRQVA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 lqggggYPAARA-------GEMLDLVASYAANPLDPH---WLLDTLGLTEAA-RATYRRLSGGQQQRLALACALVGRPQL 158
Cdd:COG4619 78 ------YVPQEPalwggtvRDNLPFPFQLRERKFDREralELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-224 |
9.33e-36 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 129.34 E-value: 9.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIeVLGLDPIT-------------- 77
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-LLRGQHIEglpghqiarmgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 78 --DNARLRARIGVM---------------LQGGGGYPAARAGEMLDLvaSYAAnpldpHWLlDTLGLTEAARATYRRLSG 140
Cdd:PRK11300 85 tfQHVRLFREMTVIenllvaqhqqlktglFSGLLKTPAFRRAESEAL--DRAA-----TWL-ERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 141 GQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
....*
gi 489998165 220 TPAEL 224
Cdd:PRK11300 237 TPEEI 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-224 |
2.45e-35 |
|
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: 128.07 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSIT-AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD----PITDNARLRARI 86
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGGYPAARAGE-----MLDLVASYAA--NPLDPH------WLLDTLGLTEAARATYRRLSGGQQQRLALACALV 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnvlsgRLGRRSTWRSlfGLFPKEekqralAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 154 GRPQLVFLDEPTAGMD-AHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:cd03256 161 QQPKLILADEPVASLDpASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-224 |
3.18e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.83 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 8 PEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDNARLRAR 85
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQggggypaaragEmLDLVA--SYAAN------PLDPHW------------LLDTLGLTEAARATYRRLSGGQQQR 145
Cdd:COG1129 81 IAIIHQ-----------E-LNLVPnlSVAENiflgrePRRGGLidwramrrrareLLARLGLDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 146 LALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-231 |
3.63e-35 |
|
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: 127.61 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGS----ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNAR--LRAR 85
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG-RPVTRRRRkaFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQ----------------------GGGGYPAARAGEMLDLVasyaanpldphwlldtlGLTEAARatYRR---LSG 140
Cdd:COG1124 81 VQMVFQdpyaslhprhtvdrilaeplriHGLPDREERIAELLEQV-----------------GLPPSFL--DRYphqLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 141 GQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
250
....*....|..
gi 489998165 220 TPAELmRSGAKD 231
Cdd:COG1124 222 TVADL-LAGPKH 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-228 |
4.59e-35 |
|
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: 133.34 E-value: 4.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 4 APDTPEVVLRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT-DNAR 81
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 LRARIGVMLQG------------GGGYP---------AARAGEMLDLVASYAANpldphwlLDTLgLTEAARatyrRLSG 140
Cdd:COG4988 409 WRRQIAWVPQNpylfagtirenlRLGRPdasdeeleaALEAAGLDEFVAALPDG-------LDTP-LGEGGR----GLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 141 GQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRdGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGT 220
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGT 554
|
....*...
gi 489998165 221 PAELMRSG 228
Cdd:COG4988 555 HEELLAKN 562
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-224 |
5.08e-35 |
|
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: 126.53 E-value: 5.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFV-----RPDAGSIEVLG---LDPITDNARLR 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 84 ARIGVMLQggggYPAARAGEMLDLVAsYAANP--------LDP--HWLLDTLGLTEAA--RATYRRLSGGQQQRLALACA 151
Cdd:cd03260 81 RRVGMVFQ----KPNPFPGSIYDNVA-YGLRLhgiklkeeLDErvEEALRKAALWDEVkdRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 152 LVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
12-224 |
5.63e-35 |
|
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: 127.07 E-value: 5.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRaRIGVMLQ 91
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GgggYPAARAGEMLDLVA------------SYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLV 159
Cdd:cd03296 82 H---YALFRHMTVFDNVAfglrvkprserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 160 FLDEPTAGMDAHARVlvwELIDALRR----DGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:cd03296 159 LLDEPFGALDAKVRK---ELRRWLRRlhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-223 |
2.72e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.39 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDN--ARLRAR 85
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdLSRLKRReiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQGGG------------------GYP----AARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGGQQ 143
Cdd:COG2884 81 IGVVFQDFRllpdrtvyenvalplrvtGKSrkeiRRRVREVLDLV-----------------GLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 144 QRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAE 223
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-227 |
5.15e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.02 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRY--GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDA---GSIEVLGLDPITDNARLR 83
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 84 AR-IGVMLQGgggyPAA-----RAGEMLDLV-----ASYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACAL 152
Cdd:COG1123 82 GRrIGMVFQD----PMTqlnpvTVGDQIAEAlenlgLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 153 VGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-224 |
6.71e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 125.26 E-value: 6.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 25 TAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNA----RLRARIGVMLQggggYP--- 97
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklkDLRKKVGLVFQ----FPehq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 98 ------------------------AARAGEMLDLVAsyaanpLDPHWLLdtlglteaaRATYRrLSGGQQQRLALACALV 153
Cdd:TIGR04521 95 lfeetvykdiafgpknlglseeeaEERVKEALELVG------LDEEYLE---------RSPFE-LSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 154 GRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-213 |
6.94e-34 |
|
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: 123.77 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARL---- 82
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQGGGGY--PAARAGEMLdLVASYAANPLDPHW--------LLDTLGLTEAARATY-RRLSGGQQQRLALACA 151
Cdd:cd03257 81 RKEIQMVFQDPMSSlnPRMTIGEQI-AEPLRIHGKLSKKEarkeavllLLVGVGLPEEVLNRYpHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 152 LVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-225 |
2.17e-33 |
|
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: 129.57 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYG--SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpIT--DNARLRARIG 87
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID-LRqiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQGG------------GGYP---------AARAGEMLDLVAsyaANPLDphwlLDTLgLTEAARatyrRLSGGQQQRL 146
Cdd:COG2274 553 VVLQDVflfsgtirenitLGDPdatdeeiieAARLAGLHDFIE---ALPMG----YDTV-VGEGGS----NLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRdGVTVVLTTHHLkEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-231 |
2.69e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 124.05 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 13 RLRGVCKRYGSIT-AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI-----EVLGLDPItdnaRLRARI 86
Cdd:COG1125 3 EFENVTKRYPDGTvAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRIlidgeDIRDLDPV----ELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGG------------------GYP----AARAGEMLDLVAsyaanpLDPhwlldtlglteaarATYRR-----LS 139
Cdd:COG1125 79 GYVIQQIGlfphmtvaeniatvprllGWDkeriRARVDELLELVG------LDP--------------EEYRDrypheLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 140 GGQQQRLALACALVGRPQLVFLDEPTAGMDAHAR-VLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAA 218
Cdd:COG1125 139 GGQQQRVGVARALAADPPILLMDEPFGALDPITReQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQY 218
|
250
....*....|...
gi 489998165 219 GTPAELMRSGAKD 231
Cdd:COG1125 219 DTPEEILANPAND 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
12-224 |
2.70e-33 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 125.23 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVeMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQ 91
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARA--------GEMLDLVASYAANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:NF000106 93 VR*GRRESFSgrenlymiGR*LDLSRKDARARADE--LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 164 PTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-223 |
3.55e-33 |
|
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: 121.77 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 5 PDTPEVVLRLRGVCKRY----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITD 78
Cdd:COG4181 2 SSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 79 NARLRAR---IGVMLQ--------------------GGGGYPAARAGEMLDLVasyaanpldphwlldtlGLTEAARATY 135
Cdd:COG4181 82 DARARLRarhVGFVFQsfqllptltalenvmlplelAGRRDARARARALLERV-----------------GLGHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 136 RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHhlkeAEELA---DRLVIID 211
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTH----DPALAarcDRVLRLR 220
|
250
....*....|..
gi 489998165 212 HGVTVAAGTPAE 223
Cdd:COG4181 221 AGRLVEDTAATA 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-226 |
9.64e-33 |
|
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: 126.80 E-value: 9.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 4 APDTPEVVLRLRGVCKRY--GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT-DNA 80
Cdd:COG4987 326 APAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRARIGVMLQ---------------GGGGYPAARAGEMLDLVAsyaanpLDPhWL------LDTLgLTEAARatyrRLS 139
Cdd:COG4987 406 DLRRRIAVVPQrphlfdttlrenlrlARPDATDEELWAALERVG------LGD-WLaalpdgLDTW-LGEGGR----RLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 140 GGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGvTVVLTTHHLKEAeELADRLVIIDHGVTVAAG 219
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRLAGL-ERMDRILVLEDGRIVEQG 551
|
....*..
gi 489998165 220 TPAELMR 226
Cdd:COG4987 552 THEELLA 558
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-234 |
1.24e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGL---DPITDNARLRARIGVML 90
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGGGGYPAARAGE--MLDLV----ASYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEP 164
Cdd:PRK09493 84 QQFYLFPHLTALEnvMFGPLrvrgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 165 TAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKDQLR 234
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-216 |
2.64e-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: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 13 RLRGVCKRYG-SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGldPITDNARLRARIGVMLQ 91
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG--KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYP-AARAGEMLDLVA-SYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMD 169
Cdd:cd03226 79 DVDYQLfTDSVREELLLGLkELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489998165 170 AHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTV 216
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-223 |
4.30e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 119.36 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITaVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNARLRARIGVMLQ 91
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKD-ITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLD--LVASYAANPLDPHWLLDT---LGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:cd03299 79 NYALFPHMTVYKNIAygLKKRKVDKKEIERKVLEIaemLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 167 GMDAHAR-VLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAE 223
Cdd:cd03299 159 ALDVRTKeKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-224 |
6.65e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 121.34 E-value: 6.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpIT--DNARLRA- 84
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVD-LTalSERELRAa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 --RIGVMLQGGG------------------GYP----AARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSG 140
Cdd:COG1135 81 rrKIGMIFQHFNllssrtvaenvalpleiaGVPkaeiRKRVAELLELV-----------------GLSDKADAYPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 141 GQQQRLALACALVGRPQLVFLDEPTAGMDAH--ARVLvwELIDALRRD-GVTVVLTTHhlkEAE---ELADRLVIIDHGV 214
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPEttRSIL--DLLKDINRElGLTIVLITH---EMDvvrRICDRVAVLENGR 218
|
250
....*....|
gi 489998165 215 TVAAGTPAEL 224
Cdd:COG1135 219 IVEQGPVLDV 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-226 |
7.00e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.11 E-value: 7.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 10 VVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITD-NARLRARI-G 87
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-RPLADwSPAELARRrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQ--------------GGGGYP-AARAGEMLDLVASYaanpldphwlLDTLGLTEAARATYRRLSGGQQQRLALACAL 152
Cdd:PRK13548 80 VLPQhsslsfpftveevvAMGRAPhGLSRAEDDALVAAA----------LAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 153 V------GRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
.
gi 489998165 226 R 226
Cdd:PRK13548 230 T 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-224 |
1.76e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.10 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 1 MNRAPDTPEV--------VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG 72
Cdd:PRK11607 1 MNDAIPRPQAktrkaltpLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 73 LDpITDNARLRARIGVMLQGGGGYP----------------------AARAGEMLDLVasyaanpldpHwlldtlgLTEA 130
Cdd:PRK11607 81 VD-LSHVPPYQRPINMMFQSYALFPhmtveqniafglkqdklpkaeiASRVNEMLGLV----------H-------MQEF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 131 ARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHAR-VLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVI 209
Cdd:PRK11607 143 AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAI 222
|
250
....*....|....*
gi 489998165 210 IDHGVTVAAGTPAEL 224
Cdd:PRK11607 223 MNRGKFVQIGEPEEI 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-231 |
2.54e-31 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 123.70 E-value: 2.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVhDAEVMA-LLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNARLRA---RI 86
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDI-PAGCMVgLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD-MADARHRRAvcpRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGG--YPAARAGEMLDLVAS-YAANPLDPHW----LLDTLGLTE-AARATyRRLSGGQQQRLALACALVGRPQL 158
Cdd:NF033858 79 AYMPQGLGKnlYPTLSVFENLDFFGRlFGQDAAERRRrideLLRATGLAPfADRPA-GKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALR--RDGVTVVLTTHHLKEAEELaDRLVIIDHGVTVAAGTPAELM-RSGAKD 231
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRaeRPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLaRTGADT 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-221 |
3.81e-31 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 123.59 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQGGGGYPAARAGEML 105
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 106 DLVA-----SYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELI 180
Cdd:TIGR01257 1025 LFYAqlkgrSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489998165 181 daLR-RDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTP 221
Cdd:TIGR01257 1105 --LKyRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-224 |
1.87e-30 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 115.09 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGS-ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNAR-----LRA 84
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTD-ITKLRGkklrkLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGVMLQGGGGYPAARAGEMLdLVASYAANPLDPHWL--------------LDTLGLTEAA--RATYrrLSGGQQQRLAL 148
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENV-LHGRLGYKPTWRSLLgrfseedkeralsaLERVGLADKAyqRADQ--LSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 149 ACALVGRPQLVFLDEPTAGMDAHARVLVwelIDALRR----DGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQV---MDYLKRinkeDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-214 |
2.34e-30 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 114.16 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDN----ARLRARIG 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK-LTDDkkniNELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQGGGGYPAARAGE--MLDLV-------ASYAANPLDphwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQL 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLEniTLAPIkvkgmskAEAEERALE---LLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGV 214
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-166 |
6.52e-30 |
|
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: 110.82 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR-LRARIGVMLQGGGGYPAARAGEML 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 106 DLVASYAANPLDP-----HWLLDTLGLTEAA----RATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:pfam00005 81 RLGLLLKGLSKREkdaraEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-223 |
8.56e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 8.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 7 TPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDNARLRA 84
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIG-----------------VML---QGGGGYP---AARAgEMLDLVASYAAnPLDPHwlldtlglteaarATYRRLSGG 141
Cdd:COG3845 81 GIGmvhqhfmlvpnltvaenIVLglePTKGGRLdrkAARA-RIRELSERYGL-DVDPD-------------AKVEDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 142 QQQRLALACALVGRPQLVFLDEPTAgmdaharVL----VWELIDALRR---DGVTVVLTTHHLKEAEELADRLVIIDHGV 214
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTA-------VLtpqeADELFEILRRlaaEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
....*....
gi 489998165 215 TVAAGTPAE 223
Cdd:COG3845 219 VVGTVDTAE 227
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-213 |
9.23e-30 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 112.34 E-value: 9.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD--PITDN--ARLRAR 85
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvnRLRGRqlPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQGGGGYPAARAGE--MLDLVASYAANPLDPHW---LLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVF 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYEnvALPLEVRGKKEREIQRRvgaALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489998165 161 LDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-223 |
1.24e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.81 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 1 MNRAPDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNA 80
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-ITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRARIGVMLQggggypaaragemldlvaSYAanpLDPHW-----------------------LLDTLG---LTEAARAT 134
Cdd:PRK09452 83 AENRHVNTVFQ------------------SYA---LFPHMtvfenvafglrmqktpaaeitprVMEALRmvqLEEFAQRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 135 YRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
250
....*....|
gi 489998165 214 VTVAAGTPAE 223
Cdd:PRK09452 222 RIEQDGTPRE 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-230 |
1.31e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.96 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRY--GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLdPITDNA--RLRA 84
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-VLSEETvwDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGVMLQG-------------------GGGYPAAragEMLDLVasyaanpldpHWLLDTLGLTEAARATYRRLSGGQQQR 145
Cdd:PRK13635 82 QVGMVFQNpdnqfvgatvqddvafgleNIGVPRE---EMVERV----------DQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 146 LALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
....*.
gi 489998165 225 MRSGAK 230
Cdd:PRK13635 228 FKSGHM 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-227 |
1.77e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.90 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD----PITDNARLRArig 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaawSPWELARRRA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQGG--------------GGYP-AARAGEMLDLVASYAAnpldphwLLDTLGLteAARAtYRRLSGGQQQRLALACAL 152
Cdd:COG4559 79 VLPQHSslafpftveevvalGRAPhGSSAAQDRQIVREALA-------LVGLAHL--AGRS-YQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 153 V-------GRPQLVFLDEPTAGMD-AHA-RVLvwELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAE 223
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDlAHQhAVL--RLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
....
gi 489998165 224 LMRS 227
Cdd:COG4559 227 VLTD 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-219 |
2.86e-29 |
|
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: 111.23 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITAvsNLDLDVhDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDNARL---RARIGVMLQGG 93
Cdd:cd03297 8 KRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvLFDSRKKINLppqQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 94 G-------------GYPAARAGEMLDLVASyaanpldphwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVF 160
Cdd:cd03297 85 AlfphlnvrenlafGLKRKRNREDRISVDE----------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 161 LDEPTAGMDAHAR-VLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03297 155 LDEPFSALDRALRlQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-224 |
3.85e-29 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 117.81 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYG--SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGV 88
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGGGGYPAARAGEMLDLVASYAANPLD-----PHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEeiekvANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 164 PTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-224 |
9.67e-29 |
|
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: 110.36 E-value: 9.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGS----ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD--NARLRA 84
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTD-LTLlsGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 ---RIGVMLQ-----------GGGGYP-----------AARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLS 139
Cdd:cd03258 80 arrRIGMIFQhfnllssrtvfENVALPleiagvpkaeiEERVLELLELV-----------------GLEDKADAYPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 140 GGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAA 218
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
....*.
gi 489998165 219 GTPAEL 224
Cdd:cd03258 223 GTVEEV 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-227 |
2.26e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.22 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 3 RAPDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPitDNA 80
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDA--GDI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRARIGVMLQGGGGY------------------PAARAGEMLDLvasyaanpldphwLLDTLGLTEAARATYRRLSGGQ 142
Cdd:NF033858 336 ATRRRVGYMSQAFSLYgeltvrqnlelharlfhlPAAEIAARVAE-------------MLERFDLADVADALPDSLPLGI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 143 QQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWE-LIDALRRDGVTVVLTTHHLKEAeELADRLVIIDHGVTVAAGTP 221
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRlLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTP 481
|
....*.
gi 489998165 222 AELMRS 227
Cdd:NF033858 482 AALVAA 487
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-233 |
2.42e-28 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 109.15 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD---NARLRARIGV 88
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGED-ITKlppHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGGGGYPAARAGEMLDLVAsyAANPLDPHWLLDTL-GLTEAARATYRR----LSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGL--AALPRRSRKIPDEIyELFPVLKEMLGRrggdLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 164 PTAGMDAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKDQL 233
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYL 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-224 |
4.76e-28 |
|
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: 110.66 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 42 LLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRArIGVMLQGGGGYP----------------------AA 99
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH-INMVFQSYALFPhmtveenvafglkmrkvpraeiKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 100 RAGEMLDLVAsyaanpldphwlldtlgLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVW-E 178
Cdd:TIGR01187 80 RVLEALRLVQ-----------------LEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489998165 179 LIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:TIGR01187 143 LKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-213 |
5.04e-28 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 106.75 E-value: 5.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYgsitAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGV 88
Cdd:cd03215 2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 mlqgggGY-PAARAGEMLDLVASYAANpldphwlldtLGLTeaaratyRRLSGGQQQRLALACALVGRPQLVFLDEPTAG 167
Cdd:cd03215 78 ------AYvPEDRKREGLVLDLSVAEN----------IALS-------SLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489998165 168 MDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-224 |
1.26e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.91 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLglDPITDNAR-----------L 82
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARslsqqkglirqL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQGGGGYPAARAGE-------MLDLVASYAANPLDPHwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGR 155
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLEniiegpvIVKGEPKEEATARARE-LLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-228 |
1.62e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.18 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD--NARLRARIGV 88
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD-IRDltLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQ---------------GGGGYP------AARAGEMLDLVASyaanpldphwL---LDTLgLTEAARatyrRLSGGQQQ 144
Cdd:COG1132 419 VPQdtflfsgtireniryGRPDATdeeveeAAKAAQAHEFIEA----------LpdgYDTV-VGERGV----NLSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 145 RLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRdGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAEL 224
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEEL 561
|
....
gi 489998165 225 MRSG 228
Cdd:COG1132 562 LARG 565
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
17-227 |
1.78e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 109.81 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 17 VCKRYGSITAvsNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARL------RARIGVML 90
Cdd:COG4148 7 FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGiflpphRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGGGGYPAARAGEMLDLV---ASYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAG 167
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGrkrAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 168 MDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:COG4148 164 LDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-235 |
9.82e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.48 E-value: 9.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 16 GVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGldpiTDNARLRAR---IGVMLQG 92
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLHARdrkVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 93 gggYPAARAGEMLDLVA------------SYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVF 160
Cdd:PRK10851 83 ---YALFRHMTVFDNIAfgltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 161 LDEPTAGMDAHARVlvwELIDALRR----DGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKdqlRF 235
Cdd:PRK10851 160 LDEPFGALDAQVRK---ELRRWLRQlheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT---RF 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-210 |
1.04e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.85 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 20 RYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPI---------TDNARLRARIGVML 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVayvpqrsevPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 -----QGGGGYPAARAGEMLDlvasyAAnpldphwlLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPT 165
Cdd:NF040873 81 grwarRGLWRRLTRDDRAAVD-----DA--------LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489998165 166 AGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAeELADRLVII 210
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-234 |
2.10e-26 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 105.03 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 3 RAPDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT-DNAR 81
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 LRA----RIGVMLQGGGGYP----------------------AARAGEMLDLVasyaanpldphwlldtlGLTEAARATY 135
Cdd:cd03294 96 LRElrrkKISMVFQSFALLPhrtvlenvafglevqgvpraerEERAAEALELV-----------------GLEGWEHKYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 136 RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGV 214
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
250 260
....*....|....*....|
gi 489998165 215 TVAAGTPAELMRSGAKDQLR 234
Cdd:cd03294 239 LVQVGTPEEILTNPANDYVR 258
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-238 |
2.24e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.32 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGL-----DPITDNA--RLRA 84
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsQKPSEKAirLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGVMLQGGGGYPAARAGE--------MLDLVASYAANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRP 156
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEnlieapckVLGLSKEQAREKAMK--LLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 157 QLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGtpaelmrsgakDQLRFT 236
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-----------DASHFT 229
|
..
gi 489998165 237 AP 238
Cdd:COG4161 230 QP 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-225 |
3.75e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.82 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI----EVLGLDPItdNARLRARI 86
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddEDISLLPL--HARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGGYPAARAGEML--------DLVASYAANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQL 158
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLmavlqirdDLSAEQREDRANE--LMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-226 |
3.80e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.96 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNARLRARIGVMLQ 91
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED-VTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGE-------MLDLVASYAANPLDphwllDTLGLTEAARATYR---RLSGGQQQRLALACALVGRPQLVFL 161
Cdd:PRK11432 86 SYALFPHMSLGEnvgyglkMLGVPKEERKQRVK-----EALELVDLAGFEDRyvdQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 162 DEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMR 226
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-213 |
2.62e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 101.68 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 1 MNRAPDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGsiEVLG----LDPI 76
Cdd:PRK11247 2 MNTARLNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAgtapLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 77 TDNARLrarigvMLQGGGGYPAARageMLDLVASyaanPLDPHW------LLDTLGLTEAARATYRRLSGGQQQRLALAC 150
Cdd:PRK11247 80 REDTRL------MFQDARLLPWKK---VIDNVGL----GLKGQWrdaalqALAAVGLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489998165 151 ALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-234 |
3.97e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.60 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAvsNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNArlrarigvmlq 91
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-LTALP----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 ggggyPAARAGEML----DLVA--SYAAN---PLDP------------HWLLDTLGLTEAARATYRRLSGGQQQRLALAC 150
Cdd:COG3840 68 -----PAERPVSMLfqenNLFPhlTVAQNiglGLRPglkltaeqraqvEQALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 151 ALV-GRPqLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:COG3840 143 CLVrKRP-ILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
....*.
gi 489998165 229 AKDQLR 234
Cdd:COG3840 222 PPPALA 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-225 |
4.49e-25 |
|
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: 105.33 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY--GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpIT--DNARLRARIG 87
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVD-IRqiDPADLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQggggYPAARAGEMLDLVASYAANPLDPHWL--LDTLGLTEAAR---ATY--------RRLSGGQQQRLALACALVG 154
Cdd:TIGR03375 543 YVPQ----DPRLFYGTLRDNIALGAPYADDEEILraAELAGVTEFVRrhpDGLdmqigergRSLSGGQRQAVALARALLR 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 155 RPQLVFLDEPTAGMDAHARVlvwELIDALRR--DGVTVVLTTHHLkEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSEE---RFKDRLKRwlAGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-228 |
4.83e-25 |
|
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: 100.38 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGS--ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDN--ARLRARIG 87
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD-VRDYtlASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQG------------GGGYPAARAGEMLDlvASYAANPLD-----PHWLLDTLGlteaARATyrRLSGGQQQRLALAC 150
Cdd:cd03251 80 LVSQDvflfndtvaeniAYGRPGATREEVEE--AARAANAHEfimelPEGYDTVIG----ERGV--KLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 151 ALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLtTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVI-AHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-234 |
6.52e-25 |
|
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: 104.80 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 3 RAPDTPEVVLRLRGVCKRYG--SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIeVLGLDPITDN- 79
Cdd:TIGR02203 322 RAIERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-LLDGHDLADYt 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 80 -ARLRARIG-----VMLQGGGGYPAARAGEMLDLV------ASYAANPLDphwLLDTL--GLTEAARATYRRLSGGQQQR 145
Cdd:TIGR02203 401 lASLRRQVAlvsqdVVLFNDTIANNIAYGRTEQADraeierALAAAYAQD---FVDKLplGLDTPIGENGVLLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 146 LALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLtTHHLKEAEElADRLVIIDHGVTVAAGTPAELM 225
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-AHRLSTIEK-ADRIVVMDDGRIVERGTHNELL 555
|
250
....*....|
gi 489998165 226 -RSGAKDQLR 234
Cdd:TIGR02203 556 aRNGLYAQLH 565
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-209 |
6.63e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYG----SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITD--------- 78
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-VPVTGpgadrgvvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 79 ---------NARLRARIGVMLQG-GGGYPAARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGGQQQRLAL 148
Cdd:COG4525 83 qkdallpwlNVLDNVAFGLRLRGvPKAERRARAEELLALV-----------------GLADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 149 ACALVGRPQLVFLDEPTAGMDAHARVLVWELI-DALRRDGVTVVLTTHHLKEAEELADRLVI 209
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLlDVWQRTGKGVFLITHSVEEALFLATRLVV 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-213 |
7.44e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 99.40 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD--PITDNA--RLRARIGV 88
Cdd:cd03292 3 FINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsDLRGRAipYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGGGGYPAARAGE--MLDLVASYAANPLDPH---WLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:cd03292 83 VFQDFRLLPDRNVYEnvAFALEVTGVPPREIRKrvpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489998165 164 PTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-224 |
1.43e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.16 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 23 SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpiTDNAR----LRARIGVMLQGGGGYPA 98
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEEnlwdIRNKAGMVFQNPDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 ARAGEmlDLVASYAAN-PLDPHWL-------LDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDA 170
Cdd:PRK13633 100 ATIVE--EDVAFGPENlGIPPEEIrervdesLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 171 HARVLVWELIDAL-RRDGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13633 178 SGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-226 |
1.48e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.58 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVlGLDPITDNAR------LRARIGVMLQggggYPAA 99
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKqkeikpVRKKVGVVFQ----FPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 100 RAGE--MLDLVA----SYAANPLDPHWL----LDTLGLT-EAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGM 168
Cdd:PRK13643 96 QLFEetVLKDVAfgpqNFGIPKEKAEKIaaekLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 169 DAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMR 226
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-238 |
1.84e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.34 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 1 MNRAPDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTtvemcegFVR---------PDA---GSI 68
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKST-------LLRclnrmndliPGArveGEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 69 EVLG---LDPITDNARLRARIGvM---------------------LQGgggypAARAGEMLDLVASYaanpldphwlldt 124
Cdd:COG1117 74 LLDGediYDPDVDVVELRRRVG-MvfqkpnpfpksiydnvayglrLHG-----IKSKSELDEIVEES------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 125 lgLTEAA-----------RATyrRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLT 193
Cdd:COG1117 135 --LRKAAlwdevkdrlkkSAL--GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489998165 194 THHLKEAEELADRLVIIDHGVTVAAGTPAELmrsgakdqlrFTAP 238
Cdd:COG1117 210 THNMQQAARVSDYTAFFYLGELVEFGPTEQI----------FTNP 244
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-210 |
2.77e-24 |
|
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: 102.75 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 4 APDTPEVVLRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPItDNA 80
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpLADA-DAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRARIGVMLQggggYPAARAGEMLDLVAsYAANPLDPHWLLDTLGLTEAARATY--------------RRLSGGQQQRL 146
Cdd:TIGR02857 393 SWRDQIAWVPQ----HPFLFAGTIAENIR-LARPDASDAEIREALERAGLDEFVAalpqgldtpigeggAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRdGVTVVLTTHHLKEAeELADRLVII 210
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-223 |
3.45e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.23 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY----------------------GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI 68
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 69 EV-----------LGLDP-IT--DNARLRARIgvMlqgggGYPAARAGEMLDLVASYAanpldphwlldtlGLTEAARAT 134
Cdd:COG1134 84 EVngrvsallelgAGFHPeLTgrENIYLNGRL--L-----GLSRKEIDEKFDEIVEFA-------------ELGDFIDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 135 YRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH--ARVLvwELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDH 212
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqKKCL--ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
250
....*....|.
gi 489998165 213 GVTVAAGTPAE 223
Cdd:COG1134 222 GRLVMDGDPEE 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-220 |
3.47e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTT---TVEMCEGfvrPDAGSIEVLGL-----DPITDNA--R 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGNhfdfsKTPSDKAirE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 LRARIGVMLQGGGGYPAARAGE--------MLDLVASYAANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALV 153
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHLTVQQnlieapcrVLGLSKDQALARAEK--LLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 154 GRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGT 220
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
11-224 |
3.92e-24 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 98.14 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTT----------TVEMC--EGFVRPDAGSIevlgLDPITD 78
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTllrslnrmndLVPGVriEGKVLFDGQDI----YDKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 79 NARLRARIGVMLQGGGGYPAARageMLDLVASYAANPLDPHWLLDTL---GLTEAA---------RATYRRLSGGQQQRL 146
Cdd:TIGR00972 77 VVELRRRVGMVFQKPNPFPMSI---YDNIAYGPRLHGIKDKKELDEIveeSLKKAAlwdevkdrlHDSALGLSGGQQQRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQI 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-219 |
4.05e-24 |
|
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: 97.66 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 24 ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpIT--DNARLRARIGVMLQGGG------- 94
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD-IRqlDPADLRRNIGYVPQDVTlfygtlr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 95 -----GYPAARAGEMLDLVASYAANPL---DPHWLldTLGLTEAARAtyrrLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:cd03245 96 dnitlGAPLADDERILRAAELAGVTDFvnkHPNGL--DLQIGERGRG----LSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489998165 167 GMDAHARVLVWELIDALRRDgVTVVLTTHHLKeAEELADRLVIIDHGVTVAAG 219
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGD-KTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-219 |
4.51e-24 |
|
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: 97.60 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEV-----------LGLDP-IT-- 77
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvssllglgGGFNPeLTgr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 78 DNARLRARIGvmlqgggGYPAARAGEMLDLVASYAanpldphwlldtlGLTEAARATYRRLSGGQQQRLALACALVGRPQ 157
Cdd:cd03220 103 ENIYLNGRLL-------GLSRKEIDEKIDEIIEFS-------------ELGDFIDLPVKTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 158 LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-227 |
4.90e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.52 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 6 DTPEVVLRLRGVCKRYGSIT--AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR-L 82
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQG------GGGYPAARA----------GEMLDLVASYAanpldphwllDTLGLTEAARATYRRLSGGQQQRL 146
Cdd:PRK13632 82 RKKIGIIFQNpdnqfiGATVEDDIAfglenkkvppKKMKDIIDDLA----------KKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGV-TVVLTTHHLKEAeELADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
..
gi 489998165 226 RS 227
Cdd:PRK13632 231 NN 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-209 |
8.73e-24 |
|
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: 98.97 E-value: 8.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRP---DAGSIEVLGLDpIT--DNAR 81
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGED-LLklSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 LRA---------------------RIG------VMLQGGGGYPAA--RAGEMLDLVasyaanpldphwlldtlGLTEAAR 132
Cdd:COG0444 80 LRKirgreiqmifqdpmtslnpvmTVGdqiaepLRIHGGLSKAEAreRAIELLERV-----------------GLPDPER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 133 AtYRR----LSGGQQQRLALACALVGRPQLVFLDEPTAGMDA--HARVLvwELIDALRRD-GVTVVLTTHHLKEAEELAD 205
Cdd:COG0444 143 R-LDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVtiQAQIL--NLLKDLQRElGLAILFITHDLGVVAEIAD 219
|
....
gi 489998165 206 RLVI 209
Cdd:COG0444 220 RVAV 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
25-219 |
9.07e-24 |
|
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: 95.46 E-value: 9.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 25 TAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQggggypaaragem 104
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 105 ldlvasyaanplDPHW----LLDTLGlteaaratyRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELI 180
Cdd:cd03247 83 ------------RPYLfdttLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489998165 181 -DALRrdGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAG 219
Cdd:cd03247 142 fEVLK--DKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-229 |
9.35e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 99.42 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITAvsNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARL-----RARIGVMLQGG 93
Cdd:TIGR02142 7 KRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 94 GGYPAARAGEMLDLVASYAANPL---DPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDa 170
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSErriSFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 171 haRVLVWELIDALRR----DGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGA 229
Cdd:TIGR02142 164 --DPRKYEILPYLERlhaeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-214 |
1.13e-23 |
|
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: 94.98 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITA--VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT-DNARLRARIGV 88
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQggggypaaragEMLDLVASYAANPLdphwlldtlglteaaratyrrlSGGQQQRLALACALVGRPQLVFLDEPTAGM 168
Cdd:cd03246 81 LPQ-----------DDELFSGSIAENIL----------------------SGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489998165 169 DAHARVLVWELIDALRRDGVTVVLTTHHlKEAEELADRLVIIDHGV 214
Cdd:cd03246 128 DVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGR 172
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-239 |
1.27e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPIT-DNAR-LRARIG 87
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG-EPITkENIReVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQGGGGYPAARAGEM--------LDLVASYAANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLV 159
Cdd:PRK13652 82 LVFQNPDDQIFSPTVEQdiafgpinLGLDEETVAHRVSS--ALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 160 FLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL-MRSGAKDQLRFTA 237
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARVHLDL 239
|
..
gi 489998165 238 PP 239
Cdd:PRK13652 240 PS 241
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-238 |
1.28e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSIT-AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNARL---RARI 86
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLqgiRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGGYPAARAGEMlDLV---ASYAANPLDPHWLLDtLGLTEAARATYRR-----LSGGQQQRLALACALVGRPQL 158
Cdd:PRK13644 80 GIVFQNPETQFVGRTVEE-DLAfgpENLCLPPIEIRKRVD-RALAEIGLEKYRHrspktLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSGAKDQLRFTAP 238
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPP 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-213 |
1.32e-23 |
|
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: 96.35 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRY-----GSIT--AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR 81
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 LRARigVMLqggggypAARAGEM---------------LDLVAsyaaNPL-----DPHW-------LLDTLGLTE----A 130
Cdd:COG4778 82 ASPR--EIL-------ALRRRTIgyvsqflrviprvsaLDVVA----EPLlergvDREEararareLLARLNLPErlwdL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 131 ARATYrrlSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVII 210
Cdd:COG4778 149 PPATF---SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
...
gi 489998165 211 DHG 213
Cdd:COG4778 226 TPF 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-225 |
1.35e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 21 YGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRAR-IGVMLQGgggYPAA 99
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARrLALLPQH---HLTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 100 RAGEMLDLVAsYAANPLDPHW-------------LLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:PRK11231 89 EGITVRELVA-YGRSPWLSLWgrlsaednarvnqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 167 GMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-226 |
1.51e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.81 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARL---RARIGVMLQggggYPAARAG 102
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdiRKKVGLVFQ----YPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 103 EmlDLVASyaanplDPHWLLDTLGLTEaaRATYRR----------------------LSGGQQQRLALACALVGRPQLVF 160
Cdd:PRK13637 98 E--ETIEK------DIAFGPINLGLSE--EEIENRvkramnivgldyedykdkspfeLSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 161 LDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMR 226
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-225 |
2.00e-23 |
|
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: 96.07 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 13 RLRGVCKRYGS---ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR-LRARIGV 88
Cdd:cd03249 2 EFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGgggyPAARAGEMLDLV--------------ASYAANPLD-----PHWLlDTL-GlteaARATyrRLSGGQQQRLAL 148
Cdd:cd03249 82 VSQE----PVLFDGTIAENIrygkpdatdeeveeAAKKANIHDfimslPDGY-DTLvG----ERGS--QLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 149 ACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRdGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELM 225
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-224 |
2.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPIT-DNARL---RARIGVMLQGgggyP---- 97
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKyDKKSLlevRKTVGIVFQN----Pddql 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 98 -AARAGEmldlvaSYAANPLDphwlldtLGL---------TEAARAT----YRR-----LSGGQQQRLALACALVGRPQL 158
Cdd:PRK13639 92 fAPTVEE------DVAFGPLN-------LGLskeevekrvKEALKAVgmegFENkpphhLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
2.87e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.95 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 1 MNRAPdTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI-----EVLGLDP 75
Cdd:COG4674 1 MSLDT-MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVlfggtDLTGLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 76 itdNARLRARIG-----------------VMLQGGGGYP------AARAGEMLDLVASyaanpldphwLLDTLGLTEAAR 132
Cdd:COG4674 80 ---HEIARLGIGrkfqkptvfeeltvfenLELALKGDRGvfaslfARLTAEERDRIEE----------VLETIGLTDKAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 133 ATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGvTVVLTTHHLKEAEELADRlviidh 212
Cdd:COG4674 147 RLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH-SVVVVEHDMEFVRQIARK------ 219
|
....
gi 489998165 213 gVTV 216
Cdd:COG4674 220 -VTV 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-228 |
3.84e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 95.37 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD--NARLRARIGVMLQGGG--------- 94
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID-IRDisRKSLRSMIGVVLQDTFlfsgtimen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 95 ---GYPAARAGEMLdlVASYAANPldpHWLLDTL--GLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMD 169
Cdd:cd03254 97 irlGRPNATDEEVI--EAAKEAGA---HDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 170 AHARVLVWELIDALRrDGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:cd03254 172 TETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-226 |
6.78e-23 |
|
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: 98.72 E-value: 6.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRY-----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITD----- 78
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 79 -NARLRAR--IGVMLQGGGGYP---------AARAGEMLDLVASYAANpldphWLLDTLGLTE-AARATYRR----LSGG 141
Cdd:TIGR03269 357 pDGRGRAKryIGILHQEYDLYPhrtvldnltEAIGLELPDELARMKAV-----ITLKMVGFDEeKAEEILDKypdeLSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 142 QQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGT 220
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 489998165 221 PAELMR 226
Cdd:TIGR03269 512 PEEIVE 517
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-227 |
7.91e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 7.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 13 RLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD----PITDNAR----LR- 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvattPSRELAKrlaiLRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 84 -----ARIGVM-LQGGGGYPAARA---GEMLDLVASYaanpldphwlLDTLGLTEAARATYRRLSGGQQQRLALACALVG 154
Cdd:COG4604 83 enhinSRLTVReLVAFGRFPYSKGrltAEDREIIDEA----------IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 155 RPQLVFLDEPTAGMD-AHARvlvwELIDALRR----DGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:COG4604 153 DTDYVLLDEPLNNLDmKHSV----QMMKLLRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITP 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-213 |
8.11e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 8.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLdPITDNARLRariGVMLQ 91
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVEGPGAER---GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYP----------------------AARAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGGQQQRLALA 149
Cdd:PRK11248 78 NEGLLPwrnvqdnvafglqlagvekmqrLEIAHQMLKKV-----------------GLEGAEKRYIWQLSGGQRQRVGIA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 150 CALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-230 |
1.02e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEvLGLDPITDNAR------LRARIGVMLQggggYPA- 98
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVITAGKKnkklkpLRKKVGIVFQ----FPEh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 --------------------------ARAGEMLDLVasyaanpldphwlldtlGLTEA--ARATYRrLSGGQQQRLALAC 150
Cdd:PRK13634 97 qlfeetvekdicfgpmnfgvseedakQKAREMIELV-----------------GLPEEllARSPFE-LSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 151 ALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGA 229
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
.
gi 489998165 230 K 230
Cdd:PRK13634 239 E 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-226 |
1.36e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR-LRARIGVMLQG------------ 92
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGLVFQDpddqvfsstvwd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 93 -----------GGGYPAARAGEMLDLVASYAANPLDPHwlldtlglteaaratyrRLSGGQQQRLALACALVGRPQLVFL 161
Cdd:PRK13647 100 dvafgpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------------HLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 162 DEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMR 226
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
38-219 |
2.57e-22 |
|
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: 92.23 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 38 EVMALLGPNGAGKTTTVEMCEGFVRP--DAGSIEVLGLdPITDNArLRARIGVMLQggggypaaragemlDLVasyaanp 115
Cdd:cd03213 36 ELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGR-PLDKRS-FRKIIGYVPQ--------------DDI------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 116 ldphwLLDTLGLTEAAR--ATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLT 193
Cdd:cd03213 93 -----LHPTLTVRETLMfaAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICS 167
|
170 180
....*....|....*....|....*..
gi 489998165 194 THHLK-EAEELADRLVIIDHGVTVAAG 219
Cdd:cd03213 168 IHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
12-219 |
2.68e-22 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 92.56 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGsiTAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRArIGVMLQ 91
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGGYPAARAGEMLDL--VASYAANPLDP---HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:cd03298 78 ENNLFAHLTVEQNVGLglSPGLKLTAEDRqaiEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489998165 167 GMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-224 |
4.03e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.71 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR----LRARIGVMLQG-GGGYPAAR 100
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKtvwdIREKVGIVFQNpDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 101 AGemlDLVASYAANPLDP--------HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHA 172
Cdd:PRK13640 102 VG---DDVAFGLENRAVPrpemikivRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489998165 173 RVLVWELIDALRRD-GVTVVLTTHHLKEAeELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13640 179 KEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
14-210 |
5.62e-22 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 91.52 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR-----LRARIGV 88
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkaskfRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGGGGYPAARAGEMLDLVASYAANPLDPH-----WLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKrekkkEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489998165 164 PTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLkEAEELADRLVII 210
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-219 |
5.99e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.68 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 4 APDTPevVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD-PITDNARL 82
Cdd:PRK11701 1 MMDQP--LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 -RARIGVMLQGGGGYPAARAGEMLDLVASYAANPLDP-----------------HWL----LDTLGLTEAARAtyrrLSG 140
Cdd:PRK11701 79 sEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERlmavgarhygdiratagDWLerveIDAARIDDLPTT----FSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 141 GQQQRLALACALVGRPQLVFLDEPTAGMD--AHARVLvwELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVA 217
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQARLL--DLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
..
gi 489998165 218 AG 219
Cdd:PRK11701 233 SG 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-230 |
7.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.92 E-value: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNAR------LRARIGVMLQggggYPAA 99
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDIT-ITHKTKdkyirpVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 100 RAGE---------------M-LDLVASYAanpldpHWLLDTLGLT-EAARATYRRLSGGQQQRLALACALVGRPQLVFLD 162
Cdd:PRK13646 97 QLFEdtvereiifgpknfkMnLDEVKNYA------HRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 163 EPTAGMDAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAK 230
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-224 |
8.43e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.97 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDNA---RLRARIGVMLQggggYPAARAGE 103
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKnlkKLRKKVSLVFQ----FPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 104 MLDL-----------VASYAANPLDPHWLlDTLGLTEA-ARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH 171
Cdd:PRK13641 101 NTVLkdvefgpknfgFSEDEAKEKALKWL-KKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489998165 172 ARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-213 |
1.48e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.99 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARLRArigVMLQGGGGYPAARAGEMLDLv 108
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-KQITEPGPDRM---VVFQNYSLLPWLTVRENIAL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 109 ASYAANP----------LDPHwlLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHAR-VLVW 177
Cdd:TIGR01184 78 AVDRVLPdlskserraiVEEH--IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRgNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 489998165 178 ELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
10-229 |
2.24e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 10 VVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD--NAR-LRARI 86
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD-ITDwqTAKiMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGGYPAARAGEMLDLVASYAANPLDPHWLLDTLGLTeaARATYRR------LSGGQQQRLALACALVGRPQLVF 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELF--PRLHERRiqragtMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 161 LDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGA 229
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-228 |
3.04e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPI--TDNARLRARIGVM 89
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-DDVeaLSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQGGGGYPAARAGEMLDLVASYAANPLDPHWLLDTLGLTEAARAT---------YRRLSGGQQQRLALACALVGRPQLVF 160
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTgvaqfadrpVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 161 LDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-237 |
3.25e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.87 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 22 GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNAR--LRARIGVMLQGGG----- 94
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD-IRTVTRasLRRNIAVVFQDAGlfnrs 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 95 -------GYPAARAGEMLDlvASYAANPLDpHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAG 167
Cdd:PRK13657 425 iednirvGRPDATDEEMRA--AAERAQAHD-FIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 168 MDAHARVLVWELIDALRRDGVTVVLtTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSGAkdqlRFTA 237
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFII-AHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGG----RFAA 565
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
9-205 |
3.75e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTV-------EMCEGFvRPDaGSIEVLG---LDPITD 78
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF-RVE-GKVTFHGknlYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 79 NARLRARIGVMLQGGGGYPAArageMLDLVAsYAANPLDPHWLLDTL---GLTEAA---------RATYRRLSGGQQQRL 146
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPFPKS----IYDNIA-YGARINGYKGDMDELverSLRQAAlwdevkdklKQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELAD 205
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-225 |
4.35e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRG--VCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNA--RLRA 84
Cdd:PRK10253 3 ESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG-EHIQHYAskEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGVMLQGgggypAARAGEML--DLVAS--YAANPLDPHW----------LLDTLGLTEAARATYRRLSGGQQQRLALAC 150
Cdd:PRK10253 82 RIGLLAQN-----ATTPGDITvqELVARgrYPHQPLFTRWrkedeeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 151 ALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-213 |
5.60e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.07 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGS---IEVLGlDPITDNARL--- 82
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLG-RTVQREGRLard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 ----RARIGVMLQGGGGYPAARAGEMLdLVASYAANPLdphW-----------------LLDTLGLTEAARATYRRLSGG 141
Cdd:PRK09984 81 irksRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPF---WrtcfswftreqkqralqALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 142 QQQRLALACALVGRPQLVFLDEPTAGMDAH-ARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPEsARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-234 |
6.54e-21 |
|
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: 89.86 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY---------GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG-----LDPi 76
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqLDR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 77 TDNARLRARIGVMLQGGGGYPAARA------GEMLDLVASY--AANPLDPHWLLDTLGL-TEAARATYRRLSGGQQQRLA 147
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMtvrqiiGEPLRHLTSLdeSEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 148 LACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL-- 224
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLls 240
|
250
....*....|
gi 489998165 225 MRSGAKDQLR 234
Cdd:TIGR02769 241 FKHPAGRNLQ 250
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
27-238 |
8.43e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.79 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNA-RLRARIGVMLQGGGGYPAARAGEml 105
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQNPDNQFVGATVE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 106 DLVASYAANPLDPHWL--------LDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVW 177
Cdd:PRK13650 101 DDVAFGLENKGIPHEEmkervneaLELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 178 ELIDALRRD-GVTVVLTTHHLKEAeELADRLVIIDHGVTVAAGTPAEL-MRSGAKDQLRFTAP 238
Cdd:PRK13650 181 KTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELfSRGNDLLQLGLDIP 242
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-228 |
8.55e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 89.08 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRYG--SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD-PITDNARLRARIGVML 90
Cdd:cd03252 3 FEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGG--------GGYPAARAGEMLDLVAsYAANPLDPHWLLDTL--GLTEAARATYRRLSGGQQQRLALACALVGRPQLVF 160
Cdd:cd03252 83 QENvlfnrsirDNIALADPGMSMERVI-EAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 161 LDEPTAGMDAHA-RVLVWELIDALrrDGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:cd03252 162 FDEATSALDYESeHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-224 |
8.73e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 8.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMcegfvrpdagsieVLGLDPITDnarlrariGVMLQGG 93
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRM-------------IAGLEDITS--------GDLFIGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 94 GGY----PAARAGEMLdlVASYAanpLDPHW-LLDT----LGLTEAARATYRR---------------------LSGGQQ 143
Cdd:PRK11000 65 KRMndvpPAERGVGMV--FQSYA---LYPHLsVAENmsfgLKLAGAKKEEINQrvnqvaevlqlahlldrkpkaLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 144 QRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPA 222
Cdd:PRK11000 140 QRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPL 219
|
..
gi 489998165 223 EL 224
Cdd:PRK11000 220 EL 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-213 |
8.79e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.48 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 5 PDTPEV--VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFV--RPDAGSIEVLGlDPITDNA 80
Cdd:COG2401 22 DLSERVaiVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD-NQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRARIGvmlqggggypaaRAGEMLDLVAsyaanpldphwLLDTLGLTEAA--RATYRRLSGGQQQRLALACALVGRPQL 158
Cdd:COG2401 101 SLIDAIG------------RKGDFKDAVE-----------LLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 159 VFLDEPTAGMDAH-ARVLVWELIDALRRDGVTVVLTTHHLKEAEELA-DRLVIIDHG 213
Cdd:COG2401 158 LVIDEFCSHLDRQtAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-203 |
1.43e-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: 87.41 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEvLGLDPITDNARLRARigVMLQ 91
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR-WNGTPLAEQRDEPHE--NILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GG---GGYPAARAGEMLD-LVASYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAG 167
Cdd:TIGR01189 78 LGhlpGLKPELSALENLHfWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 489998165 168 MDAHARVLVWELIDALRRDGVTVVLTTHH---LKEAEEL 203
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLTTHQdlgLVEAREL 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-224 |
2.32e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.67 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 7 TPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD-PITDNARL--- 82
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENiPAMSRSRLytv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQGGGGYPaaragemlDL-VASYAANPLDPH-------------WLLDTLGLTEAARATYRRLSGGQQQRLAL 148
Cdd:PRK11831 83 RKRMSMLFQSGALFT--------DMnVFDNVAYPLREHtqlpapllhstvmMKLEAVGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 149 ACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-238 |
3.65e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 87.93 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 5 PDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI----EVLGLDPITDNA 80
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIrvggEEIRLKPDRDGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 ----------RLRARIGVMLQGGG-------------------GYPAARAGEMLDLvasyaanpldphwLLDTLGLTEAA 131
Cdd:COG4598 82 lvpadrrqlqRIRTRLGMVFQSFNlwshmtvlenvieapvhvlGRPKAEAIERAEA-------------LLAKVGLADKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 132 RATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHarvLVWE---LIDALRRDGVTVVLTTHHLKEAEELADRLV 208
Cdd:COG4598 149 DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE---LVGEvlkVMRDLAEEGRTMLVVTHEMGFARDVSSHVV 225
|
250 260 270
....*....|....*....|....*....|.
gi 489998165 209 IIDHGVTVAAGTPAELMRSGAKDQLR-FTAP 238
Cdd:COG4598 226 FLHQGRIEEQGPPAEVFGNPKSERLRqFLSS 256
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-224 |
5.48e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNAR------LRARIGVMLQggggYPAA 99
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTL-ITSTSKnkdikqIRKKVGLVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 100 RAGE--MLDLVA----SYAANPLDPHWL-LDTLGLTEAARATYRR----LSGGQQQRLALACALVGRPQLVFLDEPTAGM 168
Cdd:PRK13649 97 QLFEetVLKDVAfgpqNFGVSQEEAEALaREKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 169 DAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
14-228 |
5.68e-20 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 90.40 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRYG--SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT-DNARLRARIGVML 90
Cdd:TIGR03797 454 VDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGlDVQAVRRQLGVVL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGG------------GGYP-----AARAGEMLDLVASYAANPLDPHWLLDTLGLTeaaratyrrLSGGQQQRLALACALV 153
Cdd:TIGR03797 534 QNGrlmsgsifeniaGGAPltldeAWEAARMAGLAEDIRAMPMGMHTVISEGGGT---------LSGGQRQRLLIARALV 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 154 GRPQLVFLDEPTAGMDAHARVLVWELIDALRrdgVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIVSESLERLK---VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-221 |
6.53e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.09 E-value: 6.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIE------------VLGLD---P 75
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrngklrigyvpqKLYLDttlP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 76 ITDNARLRARigvmlqggggyPAARAGEMLDLVASYAANPLdphwlldtlglteaARATYRRLSGGQQQRLALACALVGR 155
Cdd:PRK09544 84 LTVNRFLRLR-----------PGTKKEDILPALKRVQAGHL--------------IDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVtVAAGTP 221
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHI-CCSGTP 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-213 |
9.46e-20 |
|
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: 85.99 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 4 APDTPEVVLRLRGVCKRYGSITAV---SNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPIT--D 78
Cdd:cd03248 4 APDHLKGIVKFQNVTFAYPTRPDTlvlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG-KPISqyE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 79 NARLRARIGVMLQggggYPAARAGEMLDLVA-----------SYAANPLDPHWLLDTL--GLTEAARATYRRLSGGQQQR 145
Cdd:cd03248 83 HKYLHSKVSLVGQ----EPVLFARSLQDNIAyglqscsfecvKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 146 LALACALVGRPQLVFLDEPTAGMDAHARVLVWELI-DALRRDgvTVVLTTHHLKEAEElADRLVIIDHG 213
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALyDWPERR--TVLVIAHRLSTVER-ADQILVLDGG 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
26-195 |
1.02e-19 |
|
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: 84.78 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPI----TDNARLRARIGVMLQGG-------- 93
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG-EPLdysrKGLLERRQRVGLVFQDPddqlfaad 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 94 ------------GGYPA---ARAGEMLDLVasyaanpldphwllDTLGLTEaaRATYRrLSGGQQQRLALACALVGRPQL 158
Cdd:TIGR01166 86 vdqdvafgplnlGLSEAeveRRVREALTAV--------------GASGLRE--RPTHC-LSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTH 195
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-223 |
1.54e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.55 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 13 RLRGVCKRY----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpIT--DNARLRA-- 84
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQD-LTalSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 -RIGVMLQG------------------GGGYPAA----RAGEMLDLVasyaanpldphwlldtlGLTEAARATYRRLSGG 141
Cdd:PRK11153 82 rQIGMIFQHfnllssrtvfdnvalpleLAGTPKAeikaRVTELLELV-----------------GLSDKADRYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 142 QQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGT 220
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
...
gi 489998165 221 PAE 223
Cdd:PRK11153 225 VSE 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-239 |
1.73e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.63 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY----GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDN----ARLR 83
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 84 -ARIGVMLQGGGGYPAARAGEMLDLVASYAANP-----LDPHWLLDTLGLTEaaRATYR--RLSGGQQQRLALACALVGR 155
Cdd:PRK10535 85 rEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLErkqrlLRAQELLQRLGLED--RVEYQpsQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEElADRLVIIDHGVTVaAGTPAELMRSGAKDQLRF 235
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV-RNPPAQEKVNVAGGTEPV 240
|
....
gi 489998165 236 TAPP 239
Cdd:PRK10535 241 VNTA 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-213 |
1.81e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.91 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY--GSI---TAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITdnaRL---- 82
Cdd:COG1101 2 LELKNLSKTFnpGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-VT---KLpeyk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RAR-IGVMLQGgggyPAA-RAGEM-----LDLvasyAANPLDPHWLldTLGLTEAARATYRR------------------ 137
Cdd:COG1101 78 RAKyIGRVFQD----PMMgTAPSMtieenLAL----AYRRGKRRGL--RRGLTKKRRELFREllatlglglenrldtkvg 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 138 -LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:COG1101 148 lLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-224 |
1.84e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 8 PEVVLRLRGVCKRYGSIT-AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIeVLGLDPITDNAR----L 82
Cdd:PRK13636 2 EDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKglmkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQ-------GGGGYPAARAGEM-LDLVASYAANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVG 154
Cdd:PRK13636 81 RESVGMVFQdpdnqlfSASVYQDVSFGAVnLKLPEDEVRKRVDN--ALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 155 RPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-226 |
3.15e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 24 ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR---------------------- 81
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekekvleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 ---LRARIGVMLQGGG-------------------GYPAA----RAGEMLDLVAsyaanpLDPHWLldtlglteaARATY 135
Cdd:PRK13651 100 ikeIRRRVGVVFQFAEyqlfeqtiekdiifgpvsmGVSKEeakkRAAKYIELVG------LDESYL---------QRSPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 136 RrLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVT 215
Cdd:PRK13651 165 E-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
250
....*....|.
gi 489998165 216 VAAGTPAELMR 226
Cdd:PRK13651 244 IKDGDTYDILS 254
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-225 |
3.48e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.86 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPIT--DNARLRARIGVMLQ-----GGG-----GY 96
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-VPLVqyDHHYLHRQVALVGQepvlfSGSvreniAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 97 PAARAGEMLDLVASYAANPLDPHWLLDTLGLTEAARaTYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLV 176
Cdd:TIGR00958 578 GLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE-KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489998165 177 WELidaLRRDGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELM 225
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLM 701
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-203 |
3.62e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 18 CKRyGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARigvmlqggggY- 96
Cdd:PRK13539 10 CVR-GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH----------Yl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 97 -------PAARAGEMLDLVAS-YAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALV-GRPqLVFLDEPTAG 167
Cdd:PRK13539 79 ghrnamkPALTVAENLEFWAAfLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRP-IWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 489998165 168 MDAHARVLVWELIDALRRDGVTVVLTTHH---LKEAEEL 203
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATHIplgLPGAREL 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-226 |
4.55e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.38 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 3 RAPDTPEVVLRLRGVCKRygsiTAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDNA 80
Cdd:COG1129 248 RAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRARIGvmlqggggY-PAARAGE--MLDL-------VASYAAnpLDPHWLLDTLGLTEAARATYRR------------- 137
Cdd:COG1129 324 AIRAGIA--------YvPEDRKGEglVLDLsirenitLASLDR--LSRGGLLDRRRERALAEEYIKRlriktpspeqpvg 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 138 -LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTV 216
Cdd:COG1129 394 nLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
250
....*....|....*
gi 489998165 217 A-----AGTPAELMR 226
Cdd:COG1129 474 GeldreEATEEAIMA 488
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-219 |
5.20e-19 |
|
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: 84.50 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI----------EVLGLDPITDNA 80
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaelELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRARIGVMLQGG------GGYPAARAGE-MLDLVASYAAN--PLDPHWL----LDTLGLTEAARAtyrrLSGGQQQRLA 147
Cdd:TIGR02323 83 LMRTEWGFVHQNPrdglrmRVSAGANIGErLMAIGARHYGNirATAQDWLeeveIDPTRIDDLPRA----FSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 148 LACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-211 |
7.05e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGS----ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPIT-----DN 79
Cdd:PRK10584 4 ENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVG-QPLHqmdeeAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 80 ARLRAR-IGVMLQGGGGYPAARAGEMLDLVA-----SYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALV 153
Cdd:PRK10584 83 AKLRAKhVGFVFQSFMLIPTLNALENVELPAllrgeSSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 154 GRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIID 211
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-232 |
7.16e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 7.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 2 NRAPDTP-EVVLRLRGVC-KRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDN 79
Cdd:COG3845 247 EKAPAEPgEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 80 ARLRARIGVmlqgggGY-PAARAGE--MLDL-VA------SYAANPLDPHWLLDTLGLTEAAR--------------ATY 135
Cdd:COG3845 327 PRERRRLGV------AYiPEDRLGRglVPDMsVAenlilgRYRRPPFSRGGFLDRKAIRAFAEelieefdvrtpgpdTPA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 136 RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVT 215
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
250 260
....*....|....*....|....
gi 489998165 216 VAAGTPAE-------LMRSGAKDQ 232
Cdd:COG3845 481 VGEVPAAEatreeigLLMAGVKEE 504
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-226 |
7.85e-19 |
|
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: 82.57 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGF--VRPDAGSIEVLGLDpITD---NARLRARIGVMLQggggYPAARAG- 102
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGED-ITDlppEERARLGIFLAFQ----YPPEIPGv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 103 EMLDLVasyaanpldphwlldtlglteaaRATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDA 182
Cdd:cd03217 93 KNADFL-----------------------RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489998165 183 LRRDGVTVVLTTHHLKEAEEL-ADRLVIIDHGVTVAAGtPAELMR 226
Cdd:cd03217 150 LREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELAL 193
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
27-220 |
1.02e-18 |
|
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: 86.25 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT-DNARLRARIGVMLQGGGGYPA------A 99
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFGKHIGYLPQDVELFPGtvaeniA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 100 RAGEMLDLVASYAANPL-DPHWLLDTL--GLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLV 176
Cdd:TIGR01842 414 RFGENADPEKIIEAAKLaGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQAL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489998165 177 WELIDALRRDGVTVVLTTHHLKeAEELADRLVIIDHGVTVAAGT 220
Cdd:TIGR01842 494 ANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGE 536
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-219 |
1.30e-18 |
|
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: 82.70 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDA---GSIEVLGLDPitDNARLRARIGVMLQGGGGYPAARAGE 103
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 104 MLdlvaSYAAN-------------PLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDA 170
Cdd:cd03234 101 TL----TYTAIlrlprkssdairkKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489998165 171 HARVLVWELIDALRRDGVTVVLTTHHLK-EAEELADRLVIIDHGVTVAAG 219
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRsDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-238 |
1.36e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 20 RYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNAR----LRARIGVMLQGGgg 95
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRgllaLRQQVATVFQDP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 96 ypaaragemlDLVASYAANPLDPHWLLDTLGLTEAARAtyRR--------------------LSGGQQQRLALACALVGR 155
Cdd:PRK13638 87 ----------EQQIFYTDIDSDIAFSLRNLGVPEAEIT--RRvdealtlvdaqhfrhqpiqcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM-RSGAKDQLR 234
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFaCTEAMEQAG 234
|
....
gi 489998165 235 FTAP 238
Cdd:PRK13638 235 LTQP 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-237 |
1.60e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG-----LDPiTDNARLraRI 86
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkLDH-KLAAQL--GI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGGYPAARAGEMLDL------------VASYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVG 154
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIgrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 155 RPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL-------MRS 227
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVsnddivrLMV 242
|
250
....*....|
gi 489998165 228 GAKDQLRFTA 237
Cdd:PRK09700 243 GRELQNRFNA 252
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-195 |
3.20e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEV-----LGL----DPITDNARLRA 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkglrIGYlpqePPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 rigVMLQGGGGYPAARAgEMLDLVASYAANPLDPH--------------W--------LLDTLGLTEAAR-ATYRRLSGG 141
Cdd:COG0488 81 ---TVLDGDAELRALEA-ELEELEAKLAEPDEDLErlaelqeefealggWeaearaeeILSGLGFPEEDLdRPVSELSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489998165 142 QQQRLALACALVGRPQLVFLDEPTAGMDAHArvLVWeLIDALRRDGVTVVLTTH 195
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLES--IEW-LEEFLKNYPGTVLVVSH 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-225 |
3.68e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD-----------PITDNARL---RA 84
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlKVADKNQLrllRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGVMLQGGGGYPAARAGE--------MLDLVASYAANPLDPHwlLDTLGLTEAARATY-RRLSGGQQQRLALACALVGR 155
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLEnvmeapiqVLGLSKQEARERAVKY--LAKVGIDERAQGKYpVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-213 |
3.91e-18 |
|
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: 81.06 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 31 DLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDNARLRARIGVMLQGGGGYP--AARAGEMLDLV 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS-HTGLAPYQRPVSMLFQENNLFAhlTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 109 ASYAANPLDPHWLLD---TLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-R 184
Cdd:TIGR01277 97 PGLKLNAEQQEKVVDaaqQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLcS 176
|
170 180
....*....|....*....|....*....
gi 489998165 185 RDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-213 |
4.94e-18 |
|
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: 79.03 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGldpitdnarlRARIGVMLQ 91
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 ggggypaaragemldlvasyaanpldphwlldtlglteaaratyrrLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH 171
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489998165 172 ARVLvweLIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03221 105 SIEA---LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-220 |
5.21e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 8 PEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIevlgldpitdnarlraRIG 87
Cdd:COG0488 312 GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------------KLG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQggggypaaragemldlVASYAANP--LDPHW-LLDTL-----GLTEAARATY---------------RRLSGGQQQ 144
Cdd:COG0488 376 ETVK----------------IGYFDQHQeeLDPDKtVLDELrdgapGGTEQEVRGYlgrflfsgddafkpvGVLSGGEKA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 145 RLALACALVGRPQLVFLDEPTAGMDAHARVLvweLIDALRR-DGvTVVLTTH--HLkeAEELADRLVII-DHGVTVAAGT 220
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEA---LEEALDDfPG-TVLLVSHdrYF--LDRVATRILEFeDGGVREYPGG 513
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-227 |
5.21e-18 |
|
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: 84.41 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpIT--DNARLRARIGVMLQGGGGYPA------ 98
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD-LSqwDREELGRHIGYLPQDVELFDGtiaeni 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 ARAGEmldlvasyaANPLDphwlldtlgLTEAARAT------------Y--------RRLSGGQQQRLALACALVGRPQL 158
Cdd:COG4618 427 ARFGD---------ADPEK---------VVAAAKLAgvhemilrlpdgYdtrigeggARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKeAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-224 |
6.29e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.08 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGF--VRPDAGSI--------------------- 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 69 -----------EVLGL----DPITdnARLRARIGVMLQ-------------------GGGGYPAARAGEMldlvasyAAN 114
Cdd:TIGR03269 81 pcpvcggtlepEEVDFwnlsDKLR--RRIRKRIAIMLQrtfalygddtvldnvlealEEIGYEGKEAVGR-------AVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 115 pldphwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWE-LIDALRRDGVTVVLT 193
Cdd:TIGR03269 152 ------LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLT 225
|
250 260 270
....*....|....*....|....*....|.
gi 489998165 194 THHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:TIGR03269 226 SHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-226 |
9.79e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVrPDAGSIEVLGLD----PITDNARLRArigvML-QGGGGYPAARA 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlsdwSAAELARHRA----YLsQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 102 GEMLDL----VASYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALV-------GRPQLVFLDEPTAGMDA 170
Cdd:COG4138 87 FQYLALhqpaGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 171 HARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMR 226
Cdd:COG4138 167 AQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-224 |
1.32e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 24 ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEV----LGLDP-------------ITDNARLRARI 86
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKnnhelitnpyskkIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQggggYPAARA-----------GEMLDLVASYAANPLDPHWLlDTLGLTEA--ARATYRrLSGGQQQRLALACALV 153
Cdd:PRK13631 119 SMVFQ----FPEYQLfkdtiekdimfGPVALGVKKSEAKKLAKFYL-NKMGLDDSylERSPFG-LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 154 GRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-197 |
1.32e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 83.18 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT-DNARLRARI 86
Cdd:TIGR02868 332 KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQGGGGYpAARAGEMLdLVASYAANPLDPHWLLDTLGLTEAARATY-----------RRLSGGQQQRLALACALVGR 155
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENL-RLARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489998165 156 PQLVFLDEPTAGMDAH-ARVLVWELIDALrrDGVTVVLTTHHL 197
Cdd:TIGR02868 490 APILLLDEPTEHLDAEtADELLEDLLAAL--SGRTVVLITHHL 530
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-227 |
3.55e-17 |
|
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: 81.65 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 4 APDTPEVVLRLRGVCKRY-----------GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVrPDAGSIEVLG 72
Cdd:COG4172 268 VPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 73 --LDPITDNA--RLRARIGVMLQGGGG-------------------YPAARAGEMLDLVASyaanpldphwLLDTLGLTE 129
Cdd:COG4172 347 qdLDGLSRRAlrPLRRRMQVVFQDPFGslsprmtvgqiiaeglrvhGPGLSAAERRARVAE----------ALEEVGLDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 130 AARATY-RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRL 207
Cdd:COG4172 417 AARHRYpHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRV 496
|
250 260
....*....|....*....|
gi 489998165 208 VIIDHGVTVAAGTPAELMRS 227
Cdd:COG4172 497 MVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-224 |
4.32e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.19 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVR--PDA---GSIEVLGLDPIT-DNARLRA 84
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKmDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGVMLQGGGGYP-------AARAGEMLDLVASYAANPLDPHWLLDTLGLTEAAR----ATYRRLSGGQQQRLALACALV 153
Cdd:PRK14247 83 RVQMVFQIPNPIPnlsifenVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKdrldAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 154 GRPQLVFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-229 |
5.09e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 78.99 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 33 DVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD----PITDNARLRARIGVML----QGGGGYPAARagem 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvsykPQYIKADYEGTVRDLLssitKDFYTHPYFK---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 105 ldlvaSYAANPLDPHWLLDTLgLTEaaratyrrLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIdalR 184
Cdd:cd03237 97 -----TEIAKPLQIEQILDRE-VPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI---R 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489998165 185 R----DGVTVVLTTHHLKEAEELADRLVIIDH--GVTVAAGTPaELMRSGA 229
Cdd:cd03237 160 RfaenNEKTAFVVEHDIIMIDYLADRLIVFEGepSVNGVANPP-QSLRSGM 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
41-228 |
7.29e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.64 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 41 ALLGPNGAGKTTTVEMCEGFVRPDAGSIeVLGLDPITDN--ARLRARIGVMLQGgggyPAAR-AGEMLDL-VASYAANPL 116
Cdd:PRK13648 39 SIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDnfEKLRKHIGIVFQN----PDNQfVGSIVKYdVAFGLENHA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 117 DPH--------WLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-G 187
Cdd:PRK13648 114 VPYdemhrrvsEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhN 193
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489998165 188 VTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:PRK13648 194 ITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-225 |
8.46e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.09 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 31 DLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNarlrarigvmlqggggyPAARAGEMLdlvas 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----------------PSRRPVSML----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 111 YAANPLDPHW---------LLDTLGLTEAARATYRR-----------------LSGGQQQRLALACALVGRPQLVFLDEP 164
Cdd:PRK10771 77 FQENNLFSHLtvaqniglgLNPGLKLNAAQREKLHAiarqmgiedllarlpgqLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 165 TAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-213 |
9.65e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 9.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR----LRAR 85
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQ-----------GGGGYPAARAGEMLDLVASYAANPldphwlLDTLGLTEAARATYRRLSGGQQQRLALACALVG 154
Cdd:PRK10908 81 IGMIFQdhhllmdrtvyDNVAIPLIIAGASGDDIRRRVSAA------LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 155 RPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-219 |
1.00e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 21 YGSITAVSNLDLDVHDAEVMALLGPNGAGKTTtveMCEGFVR-----PDA---GSIEVLGLD---PITDNARLRARIGVM 89
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKST---LLRTFNRllelnEEArveGEVRLFGRNiysPDVDPIEVRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQGGGGYP-------AARAGEMLDLVASYAANPLDPHWLLDTLGLTEAARATYR----RLSGGQQQRLALACALVGRPQL 158
Cdd:PRK14267 91 FQYPNPFPhltiydnVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 159 VFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-228 |
1.50e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.89 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVrPDAGSIEVLG-----LDP--------------------ITDNARLr 83
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreLDPeswrkhlswvgqnpqlphgtLRDNVLL- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 84 arigvmlqgggGYPAARAGEMLDLVA-SYAANPLDPHwlldTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLD 162
Cdd:PRK11174 446 -----------GNPDASDEQLQQALEnAWVSEFLPLL----PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 163 EPTAGMDAHARVLVWELIDALRRdGVTVVLTTHHLkeaEELA--DRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQL---EDLAqwDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-206 |
2.08e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.12 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCE--GFVRPD---AGSIEVLGLD---PITDNA 80
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNiysPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 RLRARIGVMLQGGGGYPAA--------------RAGEMLDLVASyaaNPLDPHWLLDTLG--LTEAARAtyrrLSGGQQQ 144
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSiyenvvyglrlkgiKDKQVLDEAVE---KSLKGASIWDEVKdrLHDSALG----LSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 145 RLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELADR 206
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDR 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-234 |
2.27e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.92 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 17 VCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD--PITDnARLR----ARIGVML 90
Cdd:PRK10070 34 ILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiaKISD-AELRevrrKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGGGGYPAARAGEMLDLVASYAANPLDPHW--LLDTL---GLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPT 165
Cdd:PRK10070 113 QSFALMPHMTVLDNTAFGMELAGINAEERRekALDALrqvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 166 AGMDAHARVLVW-ELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRSGAKDQLR 234
Cdd:PRK10070 193 SALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-224 |
2.66e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEV------LGLDPITDNARLRARIGVMLQggggYPAA 99
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQ----FPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 100 RAGEMlDLVASYAANPLD------------PHwLLDTLGLTE--AARATYRrLSGGQQQRLALACALVGRPQLVFLDEPT 165
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNlgenkqeaykkvPE-LLKLVQLPEdyVKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 166 AGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
12-213 |
2.77e-16 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 76.30 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSIT----AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI-----EVLGLDPITDNARL 82
Cdd:NF038007 2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLtlagkEVTNLSYSQKIILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQGGGGYPAARAGEMLDLVASYAANPLDP-----HWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQ 157
Cdd:NF038007 82 RELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKEriervNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 158 LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHlKEAEELADRLVIIDHG 213
Cdd:NF038007 162 LLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-224 |
3.45e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.96 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY-GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMcegfvrpdagsieVLGLDPITDnarlrariGVML 90
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRM-------------VAGLERITS--------GEIW 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGG----GGYPAARAGEMLdlVASYAanpLDPH--------WLLDTLGL---------TEAARATY---------RRLSG 140
Cdd:PRK11650 63 IGGrvvnELEPADRDIAMV--FQNYA---LYPHmsvrenmaYGLKIRGMpkaeieervAEAARILEleplldrkpRELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 141 GQQQRLALACALVGRPQlVFL-DEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAA 218
Cdd:PRK11650 138 GQRQRVAMGRAIVREPA-VFLfDEPLSNLDAKLRVQMRLEIQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQI 216
|
....*.
gi 489998165 219 GTPAEL 224
Cdd:PRK11650 217 GTPVEV 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
29-228 |
3.60e-16 |
|
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: 76.11 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD--PITDNArLRARIGVMLQ--------------- 91
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirEVTLDS-LRRAIGVVPQdtvlfndtigyniry 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 GGGG------YPAARAGEMLDLVAS----YaanpldphwllDTL----GLteaaratyrRLSGGQQQRLALACALVGRPQ 157
Cdd:cd03253 98 GRPDatdeevIEAAKAAQIHDKIMRfpdgY-----------DTIvgerGL---------KLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 158 LVFLDEPTAGMDAHARVLVWELIDALRRdGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-205 |
3.71e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMC------EGFVRPDaGSIEVLG---LDPITDNARL 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRVE-GRVEFFNqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQGGGGYPAArageMLDLVAsYAANPLDPHWLLDTLGLTEAA--------------RATYRRLSGGQQQRLAL 148
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMS----VYDNVA-YGVKIVGWRPKLEIDDIVESAlkdadlwdeikhkiHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 149 ACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEELAD 205
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-234 |
5.42e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 16 GVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARLRAR-----IGVML 90
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG-EPLAKLNRAQRKafrrdIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGGGGY--PAARAGEMLD------LVASYAANPLDPHWLLDTLGLT-EAARATYRRLSGGQQQRLALACALVGRPQLVFL 161
Cdd:PRK10419 96 QDSISAvnPRKTVREIIReplrhlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 162 DEPTAGMDAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEELADRLVIIDHG--VTVAAGTPAELMRSGAKDQLR 234
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQqQFGTACLFITHDLRLVERFCQRVMVMDNGqiVETQPVGDKLTFSSPAGRVLQ 251
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-227 |
5.98e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.24 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHDAEVMALLGPNGAGKTTT-------VEMCEGFVRPDaGSIEVLGLDPI-TDNARLRARIGVMLQGGGGYPA 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLlkvlnrlIEIYDSKIKVD-GKVLYFGKDIFqIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 ARagemldlVASYAANPLDPHWLLDTLGLTEAARATYRR-----------------LSGGQQQRLALACALVGRPQLVFL 161
Cdd:PRK14246 105 LS-------IYDNIAYPLKSHGIKEKREIKKIVEECLRKvglwkevydrlnspasqLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 162 DEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
9-227 |
6.68e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.98 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCK--RYGS-------ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPIT-- 77
Cdd:PRK15112 2 ETLLEVRNLSKtfRYRTgwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-HPLHfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 78 DNARLRARIGVMLQGGGGY--PAARAGEMLDLvasyaanPLDPHWLLDTLGLTEAARATYRR--------------LSGG 141
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPSTSlnPRQRISQILDF-------PLRLNTDLEPEQREKQIIETLRQvgllpdhasyyphmLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 142 QQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGT 220
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
....*..
gi 489998165 221 PAELMRS 227
Cdd:PRK15112 234 TADVLAS 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-224 |
7.17e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 1 MNRAPDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG-----LDP 75
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 76 ----------------ITDNARLRARIGVMLQGgggyPAARAGEMLDLVASYAANpLDPHWLLDTLGLTEaaratyrrls 139
Cdd:PRK15439 81 akahqlgiylvpqeplLFPNLSVKENILFGLPK----RQASMQKMKQLLAALGCQ-LDLDSSAGSLEVAD---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 140 ggqQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:PRK15439 146 ---RQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
....*
gi 489998165 220 TPAEL 224
Cdd:PRK15439 223 KTADL 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-227 |
1.16e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 39 VMALLGPNGAGKTTTVEMCEGFVRPDAG---SIEVL----GLDPITDNARLRARIGVMLQGGGGYPAARageMLDLVASY 111
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrySGDVLlggrSIFNYRDVLEFRRRVGMLFQRPNPFPMSI---MDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 112 AANPLDP--------HWLLDTLGLTEAARATYR----RLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWEL 179
Cdd:PRK14271 126 RAHKLVPrkefrgvaQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489998165 180 IDALrRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:PRK14271 206 IRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-233 |
1.56e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 1 MNRAPDTPEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIeVLGLDPITD-N 79
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESwS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 80 ARLRAR-IGVMLQGgggYPAARAGEMLDLVA--SY----------AANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRL 146
Cdd:PRK10575 80 SKAFARkVAYLPQQ---LPAAEGMTVRELVAigRYpwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
....*...
gi 489998165 226 RSGAKDQL 233
Cdd:PRK10575 237 RGETLEQI 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-211 |
1.73e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.47 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRY--GSITA--VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPITDNAR--L 82
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSSAAKaeL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RAR-IGVMLQG-------------------GGGYPA---ARAGEMLDLVasyaanpldphwlldtlGLteAARATYR--R 137
Cdd:PRK11629 85 RNQkLGFIYQFhhllpdftalenvamplliGKKKPAeinSRALEMLAAV-----------------GL--EHRANHRpsE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIID 211
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-213 |
3.36e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 28 SNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIevlgldpITDNARLRAR-IGVMLQGGGGY-PAARAGEML 105
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-------MLNGKEINALsTAQRLARGLVYlPEDRQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 106 DLVASYAANPL-----DPHWLLDT-------------LGLT-EAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:PRK15439 353 YLDAPLAWNVCalthnRRGFWIKParenavleryrraLNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489998165 167 GMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-213 |
4.08e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDN---ARLRAR 85
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG-KEVTFNgpkSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQggggypaarageMLDLVA--SYAAN------PLDP----HW---------LLDTLGLTEAARATYRRLSGGQQQ 144
Cdd:PRK10762 81 IGIIHQ------------ELNLIPqlTIAENiflgreFVNRfgriDWkkmyaeadkLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 145 RLALACALVGRPQLVFLDEPT-AGMDAHARVLvWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTdALTDTETESL-FRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-225 |
4.14e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGfVRPDA---GSIEVLGLDPITDNAR--LRAR 85
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRdtERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQGGGGYPAARAGEMLDL---------VASYAANPLDPHWLLDTLGLTEAARA-TYRRLSGGQQQRLALACALVGR 155
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLgneitlpggRMAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAgTPAELM 225
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTM 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-225 |
4.84e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGfVRPDA---GSI----EVLGLDPITDNAR 81
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIifegEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 lrARIGVMLQGGGGYPAARAGEMLDL--------VASYAANPLDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALV 153
Cdd:PRK13549 82 --AGIAIIHQELALVKELSVLENIFLgneitpggIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 154 GRPQLVFLDEPTAGM-DAHARVLVwELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAgTPAELM 225
Cdd:PRK13549 160 KQARLLILDEPTASLtESETAVLL-DIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGM 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-216 |
6.24e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGfVRPdAGSIE--------------------- 69
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYP-HGSYEgeilfdgevcrfkdirdseal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 70 -------VLGLDP---ITDNARL---RARIGVMlqgggGYPAA--RAGEMLDLVasyaanpldphwlldtlGLTEAARAT 134
Cdd:NF040905 79 giviihqELALIPylsIAENIFLgneRAKRGVI-----DWNETnrRARELLAKV-----------------GLDESPDTL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 135 YRRLSGGQQQRLALACALVGRPQLVFLDEPTAGM-DAHARVLVwELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:NF040905 137 VTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALL-DLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
...
gi 489998165 214 VTV 216
Cdd:NF040905 216 RTI 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-238 |
6.91e-15 |
|
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: 74.72 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 7 TPEVVLRLRGVCKRYGS----ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVE-----MCEGFVRPDaGSI-----EVLG 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALsilrlLPDPAAHPS-GSIlfdgqDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 73 LDPitdnARLRA----RIG-----------------------VMLQGGGGYPAA--RAGEMLDLVasyaanpldphwlld 123
Cdd:COG4172 81 LSE----RELRRirgnRIAmifqepmtslnplhtigkqiaevLRLHRGLSGAAAraRALELLERV--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 124 tlGLTEAAR--ATY-RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH--ARVLvwELIDALRRD-GVTVVLTTHHL 197
Cdd:COG4172 142 --GIPDPERrlDAYpHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTvqAQIL--DLLKDLQRElGMALLLITHDL 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489998165 198 KEAEELADRLVIIDHGVTVAAGTPAELmrsgakdqlrFTAP 238
Cdd:COG4172 218 GVVRRFADRVAVMRQGEIVEQGPTAEL----------FAAP 248
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
29-226 |
7.12e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 72.68 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGfvRPD----AGSIEVLGLDPITDNARLRARIGVMLqgGGGYPAARAG-E 103
Cdd:TIGR01978 18 GVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDERARAGLFL--AFQYPEEIPGvS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 104 MLDLV-----ASYAANPLDPHWLLDTLGLTEAARATY--------RRL----SGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:TIGR01978 94 NLEFLrsalnARRSARGEEPLDLLDFEKLLKEKLALLdmdeeflnRSVnegfSGGEKKRNEILQMALLEPKLAILDEIDS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 167 GMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELA-DRLVIIDHGVTVAAGTPaELMR 226
Cdd:TIGR01978 174 GLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDV-ELAK 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-195 |
8.48e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 71.74 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDA---GSIEVLGLDpITDNARLRARIGV 88
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRR-LTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQ----------GGG---GYPAARAGEMLDLVASYAanpldphwlLDTLGLTEAARATYRRLSGGQQQRLALACALVGR 155
Cdd:COG4136 81 LFQddllfphlsvGENlafALPPTIGRAQRRARVEQA---------LEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELI-DALRRDGVTVVLTTH 195
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTH 192
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-224 |
8.58e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 1 MNRAPDTPEVVLRLrgvcKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNA 80
Cdd:PRK13642 1 MNKILEVENLVFKY----EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 81 -RLRARIGVMLQG-------------------GGGYPAAragEMLDLV--ASYAANPLDphwlldtLGLTEAARatyrrL 138
Cdd:PRK13642 77 wNLRRKIGMVFQNpdnqfvgatveddvafgmeNQGIPRE---EMIKRVdeALLAVNMLD-------FKTREPAR-----L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 139 SGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEElADRLVIIDHGVTVA 217
Cdd:PRK13642 142 SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
....*..
gi 489998165 218 AGTPAEL 224
Cdd:PRK13642 221 EAAPSEL 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
1.29e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 2 NRAPDTPEVVLRLRGVCKRY--GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLdPITD- 78
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ-PIADy 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 79 -NARLRARIGVMLQggggypaaR----AGEMLD--LVASYAANPLDPHWLLDTLGL-----TEAARATY-----RRLSGG 141
Cdd:PRK11160 408 sEAALRQAISVVSQ--------RvhlfSATLRDnlLLAAPNASDEALIEVLQQVGLeklleDDKGLNAWlgeggRQLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 142 QQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGvTVVLTTHHLKEAEELaDRLVIIDHGVTVAAGTP 221
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTH 557
|
....
gi 489998165 222 AELM 225
Cdd:PRK11160 558 QELL 561
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-196 |
1.30e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 28 SNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPItdnARLRARIGVML----QGGGGYPAARAGE 103
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-EPI---RRQRDEYHQDLlylgHQPGIKTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 104 MLDLVASyAANPLDP--HW-LLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELI 180
Cdd:PRK13538 94 NLRFYQR-LHGPGDDeaLWeALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*.
gi 489998165 181 DALRRDGVTVVLTTHH 196
Cdd:PRK13538 173 AQHAEQGGMVILTTHQ 188
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-236 |
2.80e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 25 TAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLdPITDNAR--LRARIGVMLQGGGGYPA---- 98
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-PTRQALQknLVAYVPQSEEVDWSFPVlved 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 ----ARAGEMLDLvasYAANPLDPHWLLDTLGLTEAARATYRR---LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH 171
Cdd:PRK15056 100 vvmmGRYGHMGWL---RRAKKRDRQIVTAALARVDMVEFRHRQigeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 172 ARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHgvTVAAGTPAELMRSGAKDQLRFT 236
Cdd:PRK15056 177 TEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG--TVLASGPTETTFTAENLELAFS 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-217 |
3.11e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNAR--LRARIGVM 89
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaaLAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQG--------------GGGYPaARAGeMLD---LVASYAAnpldphwLLDTLGLTEAARATYRRLSGGQQQRLALACAL 152
Cdd:PRK11288 85 YQElhlvpemtvaenlyLGQLP-HKGG-IVNrrlLNYEARE-------QLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 153 VGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVA 217
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
29-228 |
3.72e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.87 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTvemceGFV-------RPDAGSIEVLGLDpITDnarL----RARIGVML--Qgggg 95
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTL-----AKVlmghpkyEVTSGSILLDGED-ILE---LspdeRARAGIFLafQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 96 YPAARAG---EMLdLVASYAANPLDPhwlLDTLGLTEAARATYRRL---------------SGGQQQRLALACALVGRPQ 157
Cdd:COG0396 85 YPVEIPGvsvSNF-LRTALNARRGEE---LSAREFLKLLKEKMKELgldedfldryvnegfSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 158 LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHH---LKEAEelADRLVIIDHGVTVAAGTPA---ELMRSG 228
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSGGKElalELEEEG 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-206 |
4.05e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 71.69 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 7 TPEVVLRLRGVCKRY-----------GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI-----EV 70
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIlfdgqDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 71 LGLDPiTDNARLRARIGVMLQ-------------------------GGGGYPAARAGEMLDLVasyaanpldphwlldtl 125
Cdd:COG4608 83 TGLSG-RELRPLRRRMQMVFQdpyaslnprmtvgdiiaeplrihglASKAERRERVAELLELV----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 126 GLteaARATYRR----LSGGQQQRLALACALVGRPQLVFLDEPTAGMDA--HARVLvwELIDALRRD-GVTVVLTTHHLK 198
Cdd:COG4608 145 GL---RPEHADRypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiQAQVL--NLLEDLQDElGLTYLFISHDLS 219
|
....*...
gi 489998165 199 EAEELADR 206
Cdd:COG4608 220 VVRHISDR 227
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
41-213 |
4.40e-14 |
|
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: 69.58 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 41 ALLGPNGAGKTTTVEMCEGfvRPDAGSIE---VLGLDPITDNarLRARIGVMLQggggypaaragemldlvasyaanpLD 117
Cdd:cd03232 37 ALMGESGAGKTTLLDVLAG--RKTAGVITgeiLINGRPLDKN--FQRSTGYVEQ------------------------QD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 118 PHwlLDTLGLTEAAR--ATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTH 195
Cdd:cd03232 89 VH--SPNLTVREALRfsALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
170
....*....|....*....
gi 489998165 196 H-LKEAEELADRLVIIDHG 213
Cdd:cd03232 167 QpSASIFEKFDRLLLLKRG 185
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
138-213 |
5.86e-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: 69.42 E-value: 5.86e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH-ARVLVWELIDALRRDGVTVVLTTHHLkEAEELADRLVIIDHG 213
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-226 |
5.90e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 30 LDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVrPDAGSIEVLGLD----PITDNARLRArigVMLQGGGGYPAARAGEML 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPleawSAAELARHRA---YLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 106 DLVASYAANPLDPHWLLD----TLGLTEAARATYRRLSGGQQQRLALACAL-----VGRP--QLVFLDEPTAGMDAHARV 174
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNevaeALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489998165 175 LVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMR 226
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
38-224 |
6.53e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.00 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 38 EVMALLGPNGAGKTTTVEMCEGFVRPD---AGSIEVLGLdPItDNARLRARIGVMLQGGGGYPAARAGE------MLDLV 108
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM-PI-DAKEMRAISAYVQQDDLFIPTLTVREhlmfqaHLRMP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 109 ASYAANP--LDPHWLLDTLGLTEAAR------ATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELI 180
Cdd:TIGR00955 130 RRVTKKEkrERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489998165 181 DALRRDGVTVVLTTHH-LKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:TIGR00955 210 KGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
12-221 |
1.61e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 68.21 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGS--ITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT-DNARLRARIGV 88
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGgggyPAARAGEMldlvasyaANPLDPHWLLDTLGLTEAARATY--RRLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:cd03369 87 IPQD----PTLFSGTI--------RSNLDPFDEYSDEEIYGALRVSEggLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 167 GMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEELaDRLVIIDHGVTVAAGTP 221
Cdd:cd03369 155 SIDYATDALIQKTIREEFTN-STILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-214 |
1.80e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSIT-AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNAR--LRARIGV 88
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG-KPVTAEQPedYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 M---------LQGGGGYPAARAgemldLVASyaanpldphWlLDTLGLT-----EAARATYRRLSGGQQQRLALACALVG 154
Cdd:PRK10522 402 VftdfhlfdqLLGPEGKPANPA-----LVEK---------W-LERLKMAhklelEDGRISNLKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 155 RPQLVFLDEPTAGMDAH-ARVLVWELIDALRRDGVTVVLTTH--HLKeaeELADRLVIIDHGV 214
Cdd:PRK10522 467 ERDILLLDEWAADQDPHfRREFYQVLLPLLQEMGKTIFAISHddHYF---IHADRLLEMRNGQ 526
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-207 |
2.15e-13 |
|
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: 67.90 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 18 CKRyGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIevlgLDPITDNARLRARIGVMLQGGGGYP 97
Cdd:cd03231 8 CER-DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV----LLNGGPLDFQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 98 A--ARAGEMLDLVASYAANPLDPHW-LLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARV 174
Cdd:cd03231 83 GikTTLSVLENLRFWHADHSDEQVEeALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....
gi 489998165 175 LVWELIDALRRDGVTVVLTTHH-LKEAEELADRL 207
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQdLGLSEAGAREL 196
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-208 |
2.81e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.57 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 30 LDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARLRaRIGVMLQGGGGYPAARAGEMLD-LV 108
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-KTATRGDRSR-FMAYLGHLPGLKADLSTLENLHfLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 109 ASYAANPLD-PHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDG 187
Cdd:PRK13543 108 GLHGRRAKQmPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
170 180
....*....|....*....|.
gi 489998165 188 VTVVLTTHHLKEAEELADRLV 208
Cdd:PRK13543 188 GAALVTTHGAYAAPPVRTRML 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
137-213 |
6.18e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.08 E-value: 6.18e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 137 RLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-233 |
6.21e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITDN--ARLRARIGVMLQG----------- 92
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD-LRDYtlASLRNQVALVSQNvhlfndtiann 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 93 -----GGGYP------AARAGEMLDLVasyaaNPLDPHwlLDTL-GLTEAAratyrrLSGGQQQRLALACALVGRPQLVF 160
Cdd:PRK11176 437 iayarTEQYSreqieeAARMAYAMDFI-----NKMDNG--LDTViGENGVL------LSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489998165 161 LDEPTAGMDAHARVLVWELIDALRRDGvTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELM-RSGAKDQL 233
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLaQNGVYAQL 575
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
12-221 |
2.25e-12 |
|
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: 65.21 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY--GSITAVSNLDLDVHDAEVMALLGPNGAGKTT-------TVEMCEGFVRPDAGSIEVLGLDpitdnaRL 82
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllalfrLVELSSGSILIDGVDISKIGLH------DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQ-----GG---------GGYPAARAGEMLDLVAsyaanpLDPHW--LLDTLGLTEAARATyrRLSGGQQQRL 146
Cdd:cd03244 77 RSRISIIPQdpvlfSGtirsnldpfGEYSDEELWQALERVG------LKEFVesLPGGLDTVVEEGGE--NLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTP 221
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKD-CTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-228 |
8.00e-12 |
|
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: 65.58 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITavsnLDLD---VHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEV----------LGLD-PITDNARLRA 84
Cdd:COG1245 349 KSYGGFS----LEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEdlkisykpqyISPDyDGTVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGVMLQGgggypaaragemldlvaSYA----ANPLDPHWLLDTLgLTEaaratyrrLSGGQQQRLALACALVGRPQLVF 160
Cdd:COG1245 425 ANTDDFGS-----------------SYYkteiIKPLGLEKLLDKN-VKD--------LSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 161 LDEPTAGMDAHARVLVWELIdalRR----DGVTVVLTTHHLKEAEELADRLVIID-----HGVtvaAGTPAElMRSG 228
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAI---RRfaenRGKTAMVVDHDIYLIDYISDRLMVFEgepgvHGH---ASGPMD-MREG 548
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-220 |
1.18e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.36 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 22 GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPD---AGS-----IEVLGLdPITDNARLRA-RIGVMLQG 92
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSatfngREILNL-PEKELNKLRAeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 93 --GGGYPAARAGE------MLDLVASYAANPLDPHWLLDTLGLTEAaRATYR----RLSGGQQQRLALACALVGRPQLVF 160
Cdd:PRK09473 106 pmTSLNPYMRVGEqlmevlMLHKGMSKAEAFEESVRMLDAVKMPEA-RKRMKmyphEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 161 LDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGT 220
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-213 |
1.22e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 4 APDTPEVVLRlRGVCKrYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEG------------FVRpDAGSIEV- 70
Cdd:PRK10938 255 PANEPRIVLN-NGVVS-YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlFGR-RRGSGETi 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 71 -------------LGLD-PITDNARlrariGVMLQGgggypaarageMLDLVASYAANP-----LDPHWLlDTLGLTEA- 130
Cdd:PRK10938 332 wdikkhigyvsssLHLDyRVSTSVR-----NVILSG-----------FFDSIGIYQAVSdrqqkLAQQWL-DILGIDKRt 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 131 ARATYRRLSGGQQqRLAL-ACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVL-TTHHLKEAEE-LADRL 207
Cdd:PRK10938 395 ADAPFHSLSWGQQ-RLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAEDAPAcITHRL 473
|
....*.
gi 489998165 208 VIIDHG 213
Cdd:PRK10938 474 EFVPDG 479
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-222 |
1.59e-11 |
|
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: 63.15 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 36 DAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEvlglDPITDNARLRARIGVMLQG------GGGYPAARAGEMLDLVA 109
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD----DPPDWDEILDEFRGSELQNyftkllEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 110 SYAA-------------NPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLV 176
Cdd:cd03236 101 KAVKgkvgellkkkderGKLDE--LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489998165 177 WELIDALRRDGVTVVLTTHHLKEAEELADRlviidhgVTVAAGTPA 222
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEHDLAVLDYLSDY-------IHCLYGEPG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
137-213 |
1.71e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 1.71e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 137 RLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
19-211 |
1.94e-11 |
|
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: 61.82 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITAVSNLDlDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEvlgldpitdnarlrarigvmlqggggypa 98
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE----------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 aragemLDLVasyaanpldphwlldtlglTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWE 178
Cdd:cd03222 58 ------WDGI-------------------TPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR 112
|
170 180 190
....*....|....*....|....*....|....
gi 489998165 179 LIDALRRDGV-TVVLTTHHLKEAEELADRLVIID 211
Cdd:cd03222 113 AIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-225 |
2.21e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 28 SNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNARLRARIGV-MLQGGggyPAARAGEMLD 106
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG-RPLSSLSHSVLRQGVaMVQQD---PVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 107 LVASYAANPLDPHW-LLDTLGLTEAARA----TYRR-------LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARV 174
Cdd:PRK10790 434 NVTLGRDISEEQVWqALETVQLAELARSlpdgLYTPlgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489998165 175 LVWELIDALRRDgVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELM 225
Cdd:PRK10790 514 AIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
136-196 |
2.67e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.06 E-value: 2.67e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 136 RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAlRRDGVTVVLTTHH 196
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR 543
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-216 |
4.01e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 25 TAVSNLDLDVHDAEVMALLGPNGAGKTTT------------VEMCEGFVRPDAGSIevlgLDpiTDNARLRA----RIGV 88
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTalsilrllpsppVVYPSGDIRFHGESL----LH--ASEQTLRGvrgnKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQG-----------------------GGGYPAARaGEMLDLvasyaanpldphwlLDTLGLTEAAR--ATY-RRLSGGQ 142
Cdd:PRK15134 97 IFQEpmvslnplhtlekqlyevlslhrGMRREAAR-GEILNC--------------LDRVGIRQAAKrlTDYpHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 143 QQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTV 216
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-228 |
4.75e-11 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 63.61 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 21 YGSiTAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDPItDNARLRARIGVMLQGgggyPA 98
Cdd:TIGR01193 485 YGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfsLKDI-DRHTLRQFINYLPQE----PY 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 ARAGEMLDLVASYAANPLDPHWLLDTLGLTE----------------AARATyrRLSGGQQQRLALACALVGRPQLVFLD 162
Cdd:TIGR01193 559 IFSGSILENLLLGAKENVSQDEIWAACEIAEikddienmplgyqtelSEEGS--SISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 163 EPTAGMDAharVLVWELIDALRR-DGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:TIGR01193 637 ESTSNLDT---ITEKKIVNNLLNlQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDRN 699
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-224 |
6.76e-11 |
|
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: 62.89 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSIT-----AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGlDPITDNAR--LRA 84
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG-QPVTADNReaYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGV----------MLQGGGGYPAARAGEmldlvasyaanpldphwLLDTLGLT-----EAARATYRRLSGGQQQRLALA 149
Cdd:COG4615 407 LFSAvfsdfhlfdrLLGLDGEADPARARE-----------------LLERLELDhkvsvEDGRFSTTDLSQGQRKRLALL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 150 CALV-GRPQLVFlDEPTAGMDAHAR-VLVWELIDALRRDGVTVVLTTH-----HlkeaeeLADRLVIIDHGVTVAAGTPA 222
Cdd:COG4615 470 VALLeDRPILVF-DEWAADQDPEFRrVFYTELLPELKARGKTVIAISHddryfD------LADRVLKMDYGKLVELTGPA 542
|
..
gi 489998165 223 EL 224
Cdd:COG4615 543 AL 544
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-226 |
6.95e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.25 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKrYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTT----VEMCEGFVRPDAGSIEVLGlDPITDNArLRAR- 85
Cdd:PRK10418 4 QIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDG-KPVAPCA-LRGRk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 86 IGVMLQGgggyP----------AARAGEMLDLVASYAANPLDPHwLLDTLGLTEAARATYR---RLSGGQQQRLALACAL 152
Cdd:PRK10418 81 IATIMQN----PrsafnplhtmHTHARETCLALGKPADDATLTA-ALEAVGLENAARVLKLypfEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 153 VGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMR 226
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
27-196 |
1.22e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHD-------------AEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQGG 93
Cdd:PRK13540 4 VIELDFDYHDqpllqqisfhlpaGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 94 GGYP--AARAGEMLDLVASYAANPLDP--------HWLLDTLGLteaaratyrrLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:PRK13540 84 GINPylTLRENCLYDIHFSPGAVGITElcrlfsleHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 489998165 164 PTAGMDAHARVLVWELIDALRRDGVTVVLTTHH 196
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-207 |
1.27e-10 |
|
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: 58.92 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 38 EVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQGGGGypaaragemldlvasyaanpld 117
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS---------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 118 phwlldtlglteaaratyrrLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDA------LRRDGVTVV 191
Cdd:smart00382 61 --------------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllKSEKNLTVI 120
|
170
....*....|....*.
gi 489998165 192 LTTHHLKEAEELADRL 207
Cdd:smart00382 121 LTTNDEKDLGPALLRR 136
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
138-213 |
1.47e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 1.47e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-228 |
1.76e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 27 VSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDA-------GSIEVLGLDPITDNARLRARIGVmlqgGGGYPAA 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirGSVAYVPQVSWIFNATVRENILF----GSDFESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 100 RAGEMLDLVAsyAANPLDphwLLDTLGLTEAARATYRrLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWE- 178
Cdd:PLN03232 709 RYWRAIDVTA--LQHDLD---LLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDs 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489998165 179 -LIDALRrdGVTVVLTTHHLkEAEELADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:PLN03232 783 cMKDELK--GKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKSG 830
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-228 |
1.88e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITavsnLDLD---VHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEvlgldpitdnarLRARIGVMLQGGGG 95
Cdd:PRK13409 348 KKLGDFS----LEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------------PELKISYKPQYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 96 YPAARAGEML-----DLVASY----AANPLDPHWLLDTLgLTEaaratyrrLSGGQQQRLALACALVGRPQLVFLDEPTA 166
Cdd:PRK13409 412 DYDGTVEDLLrsitdDLGSSYykseIIKPLQLERLLDKN-VKD--------LSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 167 GMDAHARVLVWELIdalRR----DGVTVVLTTHHLKEAEELADRLVIID-----HGVtvaAGTPAElMRSG 228
Cdd:PRK13409 483 HLDVEQRLAVAKAI---RRiaeeREATALVVDHDIYMIDYISDRLMVFEgepgkHGH---ASGPMD-MREG 546
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-232 |
1.90e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 3 RAPDTPEVVLRLRGVcKRYGSITAVSnldLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARL 82
Cdd:PRK11288 249 RPRPLGEVRLRLDGL-KGPGLREPIS---FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLqggggYPAARAGEMLDLVASYAANP--------------LDPHWLLDTLGL--------TEAARATYRRLSG 140
Cdd:PRK11288 325 AIRAGIML-----CPEDRKAEGIIPVHSVADNInisarrhhlragclINNRWEAENADRfirslnikTPSREQLIMNLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 141 GQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVaagt 220
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA---- 475
|
250
....*....|..
gi 489998165 221 pAELMRSGAKDQ 232
Cdd:PRK11288 476 -GELAREQATER 486
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
12-212 |
1.91e-10 |
|
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: 59.54 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVckryGSITAVSNLDLDvhdAEVMALLGPNGAGKTTTVEMCE----GFVRPdaGSIEVLGLDPITDNARLRARIG 87
Cdd:cd03240 4 LSIRNI----RSFHERSEIEFF---SPLTLIVGQNGAGKTTIIEALKyaltGELPP--NSKGGAHDPKLIREGEVRAQVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 VMLQGGGG--YPAARAGEMLDLVASYAANPLDphWLL-DTLGlteaaratyrRLSGGQQQ------RLALACALVGRPQL 158
Cdd:cd03240 75 LAFENANGkkYTITRSLAILENVIFCHQGESN--WPLlDMRG----------RCSGGEKVlasliiRLALAETFGSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 159 VFLDEPTAGMDA-HARVLVWELIDALRRDGV-TVVLTTHHlkeaEELADRlviIDH 212
Cdd:cd03240 143 LALDEPTTNLDEeNIEESLAEIIEERKSQKNfQLIVITHD----EELVDA---ADH 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-219 |
2.02e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIeVLGLDPITDNARL------RARIGVMLQGGGGYP----- 97
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRVLFDAEKGiclppeKRRIGYVFQDARLFPhykvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 98 --------AARAGEMLDLVASYAANPLdphwlLDTLGLTeaaratyrrLSGGQQQRLALACALVGRPQLVFLDEPTAGMD 169
Cdd:PRK11144 95 gnlrygmaKSMVAQFDKIVALLGIEPL-----LDRYPGS---------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 170 A-HARvlvwELIDALRRDGVTV----VLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:PRK11144 161 LpRKR----ELLPYLERLAREInipiLYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-217 |
2.66e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 14 LRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGV----- 88
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGIsmvhq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 ----MLQGG-------GGYPaaRAGEMLDLVASYAanplDPHWLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQ 157
Cdd:PRK10982 81 elnlVLQRSvmdnmwlGRYP--TKGMFVDQDKMYR----DTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 158 LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHGVTVA 217
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
135-212 |
2.93e-10 |
|
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: 57.93 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 135 YRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMD--AHARVLvweliDALRRDGVTVVLTTHHlKEAEELADRLVIIDH 212
Cdd:cd03223 89 DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDeeSEDRLY-----QLLKELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
38-196 |
3.89e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 38 EVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNARLRaRIGVMLQGGGGYPAARAGEMLDLVA-------- 109
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILK-RTGFVTQDDILYPHLTVRETLVFCSllrlpksl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 110 SYAANPLDPHWLLDTLGLTEAARATY-----RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALR 184
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170
....*....|..
gi 489998165 185 RDGVTVVLTTHH 196
Cdd:PLN03211 254 QKGKTIVTSMHQ 265
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-193 |
9.24e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 3 RAPDT-PEVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIevlGLDPitdnar 81
Cdd:PRK10636 303 RAPESlPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAK------ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 lrariGVMLqgggGYPAA------RAGEM-LDLVASYAANPLDPHwLLDTLG--------LTEAARatyrRLSGGQQQRL 146
Cdd:PRK10636 374 -----GIKL----GYFAQhqleflRADESpLQHLARLAPQELEQK-LRDYLGgfgfqgdkVTEETR----RFSGGEKARL 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489998165 147 ALACALVGRPQLVFLDEPTAGMDAHAR-VLVWELIDAlrrDGVTVVLT 193
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRqALTEALIDF---EGALVVVS 484
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-226 |
1.77e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.53 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 17 VCKRYGSItaVSNLDLDVHDAEVMALLGPNGAGKTTTV-----EMCEGfVRPDAGSI--------EVLGLDPITDNARLR 83
Cdd:PRK13547 9 VARRHRAI--LRDLSLRIEPGRVTALLGRNGAGKSTLLkalagDLTGG-GAPRGARVtgdvtlngEPLAAIDAPRLARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 84 ArigVMLQGG--------------GGYPAARAGEMLDL----VASYAanpldphwlLDTLGLTEAARATYRRLSGGQQQR 145
Cdd:PRK13547 86 A---VLPQAAqpafafsareivllGRYPHARRAGALTHrdgeIAWQA---------LALAGATALVGRDVTTLSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 146 LALACAL---------VGRPQLVFLDEPTAGMD-AHARVLVwELIDALRRDGVTVVLT-THHLKEAEELADRLVIIDHGV 214
Cdd:PRK13547 154 VQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLL-DTVRRLARDWNLGVLAiVHDPNLAARHADRIAMLADGA 232
|
250
....*....|..
gi 489998165 215 TVAAGTPAELMR 226
Cdd:PRK13547 233 IVAHGAPADVLT 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-219 |
3.40e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 15 RGVCKR-YGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDaGSIEVLGlDPITDNAR-----LRARIGV 88
Cdd:PRK15134 289 KGILKRtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDG-QPLHNLNRrqllpVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 89 MLQGgggyPAARAGEMLDlVASYAANPLDPHW--------------LLDTLGLTEAARATY-RRLSGGQQQRLALACALV 153
Cdd:PRK15134 367 VFQD----PNSSLNPRLN-VLQIIEEGLRVHQptlsaaqreqqviaVMEEVGLDPETRHRYpAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489998165 154 GRPQLVFLDEPTAGMDAHARVLVWELIDALR-RDGVTVVLTTHHLKEAEELADRLVIIDHGVTVAAG 219
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-219 |
3.43e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGVCKRYG-----------SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG--LDP 75
Cdd:PRK10261 311 EPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 76 ITDNA--RLRARIGVMLQGgggyPAARagemLD---LVASYAANPLDPH-------------WLLDTLGLT-EAARATYR 136
Cdd:PRK10261 391 LSPGKlqALRRDIQFIFQD----PYAS----LDprqTVGDSIMEPLRVHgllpgkaaaarvaWLLERVGLLpEHAWRYPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 137 RLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVT 215
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
....
gi 489998165 216 VAAG 219
Cdd:PRK10261 543 VEIG 546
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
137-227 |
4.43e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.67 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 137 RLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAL-RRDGVTVVLTTHHLKEAEELADRLVIIDHGVT 215
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
90
....*....|..
gi 489998165 216 VAAGTPAELMRS 227
Cdd:PRK11022 233 VETGKAHDIFRA 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-230 |
6.91e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 3 RAPD---TP-EVVLRLRGV-CKRYGSITAVSnldLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPIT 77
Cdd:PRK10982 238 RFPDkenKPgEVILEVRNLtSLRQPSIRDVS---FDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 78 DNARLRARIGVML-----QGGGGYpaaragEMLDL--------VASYAaNPL----------DPHWLLDTLGL-TEAARA 133
Cdd:PRK10982 315 HNANEAINHGFALvteerRSTGIY------AYLDIgfnslisnIRNYK-NKVglldnsrmksDTQWVIDSMRVkTPGHRT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 134 TYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
250 260
....*....|....*....|..
gi 489998165 214 -----VTVAAGTPAELMRSGAK 230
Cdd:PRK10982 468 lvagiVDTKTTTQNEILRLASL 489
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-224 |
7.05e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.25 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 23 SITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD--PITDNARLRAR--IGVMLQGgggyPA 98
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllGMKDDEWRAVRsdIQMIFQD----PL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 99 ARAGEMLDlVASYAANPLDPHW--------------LLDTLGLTEAARATY-RRLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:PRK15079 109 ASLNPRMT-IGEIIAEPLRTYHpklsrqevkdrvkaMMLKVGLLPNLINRYpHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 164 PTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-227 |
7.51e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 22 GSITAVSNLDLDVHDAEVMALLGPNGAGKTTT-------VEMCEGFVRPDA-----GSIEVLGLDPITDNARLRAR---I 86
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTalalmrlLEQAGGLVQCDKmllrrRSRQVIELSEQSAAQMRHVRgadM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQG--GGGYPAARAGEM------LDLVASYAANPLDPHWLLDTLGLTEAARATYR---RLSGGQQQRLALACALVGR 155
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQiaesirLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 156 PQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAELMRS 227
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-228 |
8.99e-09 |
|
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: 56.37 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDpITD--NARLRARIGVMLQG------------GG 94
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD-IRDvtQASLRAAIGIVPQDtvlfndtiayniAY 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 95 GYP---------AARAGEMLDLVAS----YaanpldphwllDTL----GLteaaratyrRLSGGQQQRLALACALVGRPQ 157
Cdd:COG5265 455 GRPdaseeeveaAARAAQIHDFIESlpdgY-----------DTRvgerGL---------KLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 158 LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLtthhlkeAEEL-----ADRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRTTLVI-------AHRLstivdADEILVLEAGRIVERGTHAELLAQG 583
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-231 |
1.10e-08 |
|
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: 56.49 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRY--GSITAVSNLDLDVHDAEVMALLGPNGAGKTTTV-------EMCEGFVRPDAGSIEVLGLDpitdnaRL 82
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTlglfrinESAEGEIIIDGLNIAKIGLH------DL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 83 RARIGVMLQGgggyPAARAGEM---LDLVASYAANplDPHWLLDTL-----------GLTEAARATYRRLSGGQQQRLAL 148
Cdd:TIGR00957 1359 RFKITIIPQD----PVLFSGSLrmnLDPFSQYSDE--EVWWALELAhlktfvsalpdKLDHECAEGGENLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 149 ACALVGRPQLVFLDEPTAGMDAHARVLVWELIDAlRRDGVTVVLTTHHLKEAEELAdRLVIIDHGVTVAAGTPAELMR-- 226
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQqr 1510
|
....*....
gi 489998165 227 ----SGAKD 231
Cdd:TIGR00957 1511 gifySMAKD 1519
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-195 |
1.27e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 11 VLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLDPITDNA-RLRARIGVM 89
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 90 LQGgggyPAARAGEMLD-LVASYA---ANPlDPHWLLDTLGLTEAARATYRR----LSGGQQQRLALACALVGRPQLVFL 161
Cdd:PRK10247 87 AQT----PTLFGDTVYDnLIFPWQirnQQP-DPAIFLDDLERFALPDTILTKniaeLSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 489998165 162 DEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTH 195
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREqNIAVLWVTH 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-210 |
1.34e-08 |
|
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: 55.95 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 38 EVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVlglDPITD-------------------NARLRA--------RIGVML 90
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKPNLGDYDE---EPSWDevlkrfrgtelqdyfkklaNGEIKVahkpqyvdLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 91 QGGGGYPAARAGE--MLDLVAsyaanpldphwllDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGM 168
Cdd:COG1245 177 KGTVRELLEKVDErgKLDELA-------------EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489998165 169 DAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVII 210
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-224 |
1.71e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 15 RGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTT---TVEMCEgfvRPDAGSI-----EVLGLDPITDnARLRARI 86
Cdd:PRK11308 19 RGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTlarLLTMIE---TPTGGELyyqgqDLLKADPEAQ-KLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 87 GVMLQG--GGGYPAARAGEMLdlvasyaANPLDPHWLLDTLGLTEAARATYRRL--------------SGGQQQRLALAC 150
Cdd:PRK11308 95 QIVFQNpyGSLNPRKKVGQIL-------EEPLLINTSLSAAERREKALAMMAKVglrpehydryphmfSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 151 ALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-227 |
2.66e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 12 LRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEvlgldpITDNarlrARIGVMLQ 91
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------WSEN----ANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 92 gggGYPAARAGEM--LDLVASYAANPLDPHWLLDTLGL----TEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPT 165
Cdd:PRK15064 390 ---DHAYDFENDLtlFDWMSQWRQEGDDEQAVRGTLGRllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 166 AGMDAharvlvwELIDAL-----RRDGvTVVLTTHHLKEAEELADRLV-IIDHGVTVAAGTPAELMRS 227
Cdd:PRK15064 467 NHMDM-------ESIESLnmaleKYEG-TLIFVSHDREFVSSLATRIIeITPDGVVDFSGTYEEYLRS 526
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
137-210 |
3.25e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.98 E-value: 3.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 137 RLSGGQQQRLALACAL----VGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTThHLKEAEELADRLVII 210
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIT-HLPELAELADKLIHI 153
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-70 |
3.88e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 3.88e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 9 EVVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEV 70
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
138-195 |
4.71e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 4.71e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTH 195
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-210 |
5.13e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 39 VMALLGPNGAGKTTTVEMCEGFVRPDAGSIEvlglDPITDNARLRARIGVMLQG------GGGYPAARAGEMLDLVASY- 111
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSGELIPNLGDYE----EEPSWDEVLKRFRGTELQNyfkklyNGEIKVVHKPQYVDLIPKVf 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 112 ------------AANPLDPhwLLDTLGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWEL 179
Cdd:PRK13409 177 kgkvrellkkvdERGKLDE--VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARL 254
|
170 180 190
....*....|....*....|....*....|.
gi 489998165 180 IDALRRdGVTVVLTTHHLKEAEELADRLVII 210
Cdd:PRK13409 255 IRELAE-GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
138-227 |
6.60e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.27 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRD-GVTVVLTTHHLKEAEELADRLVIIDHGVTV 216
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90
....*....|.
gi 489998165 217 AAGTPAELMRS 227
Cdd:PRK15093 239 ETAPSKELVTT 249
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
138-198 |
9.84e-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: 51.56 E-value: 9.84e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAH-ARVLVWE-LIDALRRDGVTVVLTTHHLK 198
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEgILKFLQDDKRTLVLVTHKLQ 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
136-225 |
1.06e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 136 RRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDH--- 212
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdr 1436
|
90
....*....|....*
gi 489998165 213 -GVTVAA-GTPAELM 225
Cdd:PTZ00265 1437 tGSFVQAhGTHEELL 1451
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
122-227 |
2.05e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.32 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 122 LDTLGLTEAARAtyrrLSGGQQQRLALA----CALVGrpQLVFLDEPTAGM---DAHarvlvwELIDALR--RD-GVTVV 191
Cdd:TIGR00630 477 LDYLSLSRAAGT----LSGGEAQRIRLAtqigSGLTG--VLYVLDEPSIGLhqrDNR------RLINTLKrlRDlGNTLI 544
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489998165 192 LTTHHlKEAEELADRLVII-----DH-GVTVAAGTPAELMRS 227
Cdd:TIGR00630 545 VVEHD-EDTIRAADYVIDIgpgagEHgGEVVASGTPEEILAN 585
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
138-213 |
2.39e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 2.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-213 |
4.23e-07 |
|
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: 49.24 E-value: 4.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 138 LSGGQQQRLALACALVGRPQ--LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEElADRLVIIDHG 213
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-228 |
4.43e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 28 SNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVL----GLDPITD---NARLRARIGVmlqgGGGYPAAR 100
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIrgtvAYVPQVSwifNATVRDNILF----GSPFDPER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 101 AGEMLDLVAsyAANPLDphwLLDTLGLTE-AARATyrRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWE- 178
Cdd:PLN03130 710 YERAIDVTA--LQHDLD---LLPGGDLTEiGERGV--NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDk 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489998165 179 -LIDALRrdGVTVVLTTHHLKEAEELaDRLVIIDHGVTVAAGTPAELMRSG 228
Cdd:PLN03130 783 cIKDELR--GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNG 830
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
134-195 |
8.78e-07 |
|
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: 49.70 E-value: 8.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 134 TYRRLSGGQQQRLALACALVGRPQ---LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTH 195
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
138-227 |
1.08e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWE--LIDALRrdGVTVVLTTHHLkEAEELADRLVIIDHGVT 215
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALA--GKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
90
....*....|..
gi 489998165 216 VAAGTPAELMRS 227
Cdd:PTZ00243 860 EFSGSSADFMRT 871
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-211 |
2.23e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 20 RYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI------------------EVLGLDPITDNAR 81
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlawvnqetpalPQPALEYVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 82 ----LRARIGVMLQGGGGYPAARAGEMLDLVASYAANPLDPHwLLDTLGLT-EAARATYRRLSGGQQQRLALACALVGRP 156
Cdd:PRK10636 90 eyrqLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAAS-LLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489998165 157 QLVFLDEPTAGMDAHArvLVWeLIDALRRDGVTVVLTTHHLKEAEELADRLVIID 211
Cdd:PRK10636 169 DLLLLDEPTNHLDLDA--VIW-LEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-213 |
2.34e-06 |
|
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: 47.26 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 19 KRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTT----TVEMCEGFVRPDaGSIEVLGLDPITDNARLRARIGVMLQGGG 94
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 95 GYPAARAGEMLDLVASYAANpldphwlldtlglteaarATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAhARV 174
Cdd:cd03233 94 HFPTLTVRETLDFALRCKGN------------------EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS-STA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489998165 175 LVW-----ELIDALRrdGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:cd03233 155 LEIlkcirTMADVLK--TTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
138-195 |
2.85e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 2.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 138 LSGGQQQRLALACALVGRPQ-LVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTH 195
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-215 |
3.30e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 10 VVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSI------EVL-------GLDP- 75
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklEVAyfdqhraELDPe 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 76 --ITDNARlRARIGVMLQGgggypaaRAGEMLdlvaSYaanpldphwLLDTLGLTEAARATYRRLSGGQQQRLALACALV 153
Cdd:PRK11147 398 ktVMDNLA-EGKQEVMVNG-------RPRHVL----GY---------LQDFLFHPKRAMTPVKALSGGERNRLLLARLFL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 154 GRPQLVFLDEPTAGMDAHARVLVWELIDALrrDGvTVVLTTHhlkeaeelaDRlVIIDHGVT 215
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSY--QG-TVLLVSH---------DR-QFVDNTVT 505
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-197 |
4.84e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 30 LDLDVHdaevMALLGPNGAGKTTTVEMCEGFVRPDAGSI--------------EVLGLDpITDNARLrarigVMLQGGGG 95
Cdd:PLN03073 532 IDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLD-LSSNPLL-----YMMRCFPG 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 96 YPAARagemldlvasyaanpLDPHwlLDTLGLTE--AARATYRrLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHAr 173
Cdd:PLN03073 602 VPEQK---------------LRAH--LGSFGVTGnlALQPMYT-LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA- 662
|
170 180
....*....|....*....|....*.
gi 489998165 174 vlVWELID--ALRRDGVTVVLTTHHL 197
Cdd:PLN03073 663 --VEALIQglVLFQGGVLMVSHDEHL 686
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-197 |
4.98e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 4.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 138 LSGGQQQRLALACAL---VGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHL 197
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-196 |
5.03e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 30 LDLDVHDAEVMALLGPNGAGKTTTVEMCEGfvRPD----AGSIEVLGLDPITDNARLRARIGVMLqgGGGYPAARAG--- 102
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevtGGTVEFKGKDLLELSPEDRAGEGIFM--AFQYPVEIPGvsn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 103 -----EMLDLVASY-AANPLD----PHWLLDTLGLTEA-----ARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAG 167
Cdd:PRK09580 96 qfflqTALNAVRSYrGQEPLDrfdfQDLMEEKIALLKMpedllTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180
....*....|....*....|....*....
gi 489998165 168 MDAHARVLVWELIDALRRDGVTVVLTTHH 196
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-227 |
6.94e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 138 LSGGQQQRLALACA----LVGrpQLVFLDEPTAGMdaH----ARvlvweLIDALR--RD-GVTVVLTTHHlKEAEELADR 206
Cdd:COG0178 486 LSGGEAQRIRLATQigsgLVG--VLYVLDEPSIGL--HqrdnDR-----LIETLKrlRDlGNTVIVVEHD-EDTIRAADY 555
|
90 100 110
....*....|....*....|....*....|
gi 489998165 207 lvIID-------HG--VtVAAGTPAELMRS 227
Cdd:COG0178 556 --IIDigpgageHGgeV-VAQGTPEEILKN 582
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-221 |
7.50e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 138 LSGGQQQRLALACALVGR---PQLVFLDEPTAGMDAHArvlVWELIDALRR---DGVTVVLTTHHLkEAEELADRlvIID 211
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHD---VKKLLEVLQRlvdKGNTVVVIEHNL-DVIKCADW--IID 243
|
90
....*....|....*...
gi 489998165 212 --------HGVTVAAGTP 221
Cdd:cd03271 244 lgpeggdgGGQVVASGTP 261
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-226 |
7.60e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 137 RLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDHG--- 213
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGrit 483
|
90
....*....|....*
gi 489998165 214 --VTVAAGTPAELMR 226
Cdd:NF040905 484 geLPREEASQERIMR 498
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-224 |
7.88e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 138 LSGGQQQRLALACALVGR---PQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHL---KEAEeladrlVIID 211
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLdviKTAD------YIID 903
|
90 100
....*....|....*....|.
gi 489998165 212 --------HGVTVAAGTPAEL 224
Cdd:TIGR00630 904 lgpeggdgGGTVVASGTPEEV 924
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-197 |
9.30e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 9.30e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 137 RLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALR--RDGVTVVLtTHHL 197
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII-AHRL 640
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-225 |
9.32e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 30 LDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD----PITDnarLRARIGVMLQGgggyPAARAGeml 105
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfGLMD---LRKVLGIIPQA----PVLFSG--- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 106 dlVASYAANPLDPH-----W-------LLDT-----LGLTEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGM 168
Cdd:PLN03130 1328 --TVRFNLDPFNEHndadlWeslerahLKDVirrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 169 DAHARVLVWELIdalRRD--GVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELM 225
Cdd:PLN03130 1406 DVRTDALIQKTI---REEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-70 |
1.27e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 1.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 10 VVLRLRGVCKRYGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEV 70
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
136-233 |
1.36e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 136 RR---LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHLKEAEELADRLVIIDH 212
Cdd:PRK10938 131 RRfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
90 100
....*....|....*....|.
gi 489998165 213 GVTVAAGTPAELMRSGAKDQL 233
Cdd:PRK10938 211 CTLAETGEREEILQQALVAQL 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-169 |
1.47e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIeVLGLDPITdnARL-----RARIGVMLQggggYPAARAGE 103
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLIV--ARLqqdppRNVEGTVYD----FVAEGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 104 MLDLVASY-------AANP--------------LDPH--WLLDT--------LGLTEAARATyrRLSGGQQQRLALACAL 152
Cdd:PRK11147 94 QAEYLKRYhdishlvETDPseknlnelaklqeqLDHHnlWQLENrinevlaqLGLDPDAALS--SLSGGWLRKAALGRAL 171
|
170
....*....|....*..
gi 489998165 153 VGRPQLVFLDEPTAGMD 169
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLD 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-225 |
2.12e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 9 EVVLRLRGvckryGSITAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLD----PITDnarLRA 84
Cdd:PLN03232 1239 DVHLRYRP-----GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfGLTD---LRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 85 RIGVMLQGgggyPAARAGEMldlvaSYAANPLDPH-----W-------LLDTL-----GLTEAARATYRRLSGGQQQRLA 147
Cdd:PLN03232 1311 VLSIIPQS----PVLFSGTV-----RFNIDPFSEHndadlWealerahIKDVIdrnpfGLDAEVSEGGENFSVGQRQLLS 1381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 148 LACALVGRPQLVFLDEPTAGMDAHARVLVWELIDALRRDgVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAELM 225
Cdd:PLN03232 1382 LARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
122-213 |
4.94e-05 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 122 LDTLGLTEAARAtyrrLSGGQQQRLALA----CALVGrpQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTHHl 197
Cdd:cd03270 126 LGYLTLSRSAPT----LSGGEAQRIRLAtqigSGLTG--VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD- 198
|
90
....*....|....*.
gi 489998165 198 KEAEELADRlvIIDHG 213
Cdd:cd03270 199 EDTIRAADH--VIDIG 212
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
122-227 |
8.19e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 122 LDTLGLTEAARaTyrrLSGGQQQRLALA----CALVGrpQLVFLDEPTAGMdaH----ARvlvweLIDALR--RD-GVTV 190
Cdd:PRK00349 478 LDYLTLSRSAG-T---LSGGEAQRIRLAtqigSGLTG--VLYVLDEPSIGL--HqrdnDR-----LIETLKhlRDlGNTL 544
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489998165 191 VLTTHHlKEAEELADRLVII-----DHG--VtVAAGTPAELMRS 227
Cdd:PRK00349 545 IVVEHD-EDTIRAADYIVDIgpgagVHGgeV-VASGTPEEIMKN 586
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-227 |
9.61e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 121 LLDTLGLT----EAARATyrrLSGGQQQRLALACALVGRPQLV--FLDEPTAGM---DAHARVLVwelIDALRRDGVTVV 191
Cdd:PRK00635 459 ILIDLGLPyltpERALAT---LSGGEQERTALAKHLGAELIGItyILDEPSIGLhpqDTHKLINV---IKKLRDQGNTVL 532
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489998165 192 LTTHHlKEAEELADRLVIIDHGV------TVAAGTPAELMRS 227
Cdd:PRK00635 533 LVEHD-EQMISLADRIIDIGPGAgifggeVLFNGSPREFLAK 573
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-213 |
1.01e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 38 EVMALLGPNGAGKTT----TVEMCEGFVRPDAGSIEVLGLDPITDNARLRARIGVMLQGGGGYPAARAGEMLDLVA---- 109
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAArckt 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 110 -----------SYAANPLDphWLLDTLGL-----TEAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAhAR 173
Cdd:TIGR00956 168 pqnrpdgvsreEYAKHIAD--VYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS-AT 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489998165 174 VLvwELIDALRR-----DGVTVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:TIGR00956 245 AL--EFIRALKTsanilDTTPLVAIYQCSQDAYELFDKVIVLYEG 287
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-224 |
1.20e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.55 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 25 TAVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLGLdPITDnARL---RARIGVMLQG--------- 92
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI-PLTK-LQLdswRSRLAVVSQTpflfsdtva 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 93 ---GGGYPAARAGEMLDlvASYAANPLDphwllDTLGL-----TEAA-RATYrrLSGGQQQRLALACALVGRPQLVFLDE 163
Cdd:PRK10789 407 nniALGRPDATQQEIEH--VARLASVHD-----DILRLpqgydTEVGeRGVM--LSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489998165 164 PTAGMDAHARvlvWELIDALR--RDGVTVVLTTHHLKEAEElADRLVIIDHGVTVAAGTPAEL 224
Cdd:PRK10789 478 ALSAVDGRTE---HQILHNLRqwGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQL 536
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-226 |
2.21e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 138 LSGGQQQRLALACALVGRPQ---LVFLDEPTAGMDAH--ARVLvwELIDALRRDGVTVVLTTHHL---KeaeeLADRlvI 209
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHdiRKLL--EVLHRLVDKGNTVVVIEHNLdviK----TADW--I 898
|
90 100
....*....|....*....|....*.
gi 489998165 210 IDHG---------VtVAAGTPAELMR 226
Cdd:COG0178 899 IDLGpeggdgggeI-VAEGTPEEVAK 923
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
138-195 |
2.30e-04 |
|
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: 42.61 E-value: 2.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHArvLVWeLIDALRRDGVTVVLTTH 195
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES--VAW-LERHLQEYPGTVVAVTH 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
138-229 |
2.87e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 42.63 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHARVLVWEliDALRRDGV----TVVLTTHHLKEAEELADRLVIIDHG 213
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE--HVIGPEGVlknkTRILVTHGISYLPQVDVIIVMSGGK 838
|
90
....*....|....*.
gi 489998165 214 VTVAAGTPAELMRSGA 229
Cdd:TIGR00957 839 ISEMGSYQELLQRDGA 854
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
105-172 |
3.17e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 3.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 105 LDLVASYAANPLDPHwLLDTLGLT-EAARATYRRLSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHA 172
Cdd:PLN03073 312 LELIDAYTAEARAAS-ILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-86 |
2.18e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489998165 26 AVSNLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG-LDPITDNARLRARI 86
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISAGLSGQL 100
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
128-182 |
3.71e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.06 E-value: 3.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489998165 128 TEAARATYRR---LSGGQQQRL---ALACALV----------GRPQLVFLDEPTAGMDAHARVLVWELIDA 182
Cdd:pfam13558 20 DGSEVETYRRsggLSGGEKQLLaylPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-224 |
4.50e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 38.74 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 29 NLDLDVHDAEVMALLGPNGAGKTTTVEMCEGFVRPDAGSIEVLG----------LDPIT-----------DNARLRARIG 87
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrisfspqtswIMPGTikdniifglsyDEYRYTSVIK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 88 vmlqggggypAARAGEMLDLVASYAANPLDPHwlldtlGLTeaaratyrrLSGGQQQRLALACALVGRPQLVFLDEPTAG 167
Cdd:TIGR01271 524 ----------ACQLEEDIALFPEKDKTVLGEG------GIT---------LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489998165 168 MDAHARVLVWE-LIDALRRDGVTVVLTT--HHLKEaeelADRLVIIDHGVTVAAGTPAEL 224
Cdd:TIGR01271 579 LDVVTEKEIFEsCLCKLMSNKTRILVTSklEHLKK----ADKILLLHEGVCYFYGTFSEL 634
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
124-195 |
7.07e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.67 E-value: 7.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489998165 124 TLGLTEAARATYRRLSGGQQQRLALACALV-------GRPQLVFLDEPTAGMDAHARVLVWELIDALRRDGVTVVLTTH 195
Cdd:COG3593 149 SLRIEDGKELPLDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
138-195 |
8.26e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.79 E-value: 8.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489998165 138 LSGGQQQRLALACALVGRPQLVFLDEPTAGMDAHArVLvWeLIDALRRDGVTVVLTTH 195
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-VA-W-LEQFLHDYPGTVVAVTH 218
|
|
| |
