|
Name |
Accession |
Description |
Interval |
E-value |
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-364 |
9.11e-39 |
|
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: 144.66 E-value: 9.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL-------CQRHNVFLDDQDFCERKDY---SLLSAVFQDPSSQILATTLEDELRL 83
Cdd:COG1123 28 TIAPGETVALVGESGSGKSTLALALMgllphggRISGEVLLDGRDLLELSEAlrgRRIGMVFQDPMTQLNPVTVGDQIAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 84 MSHFHHVNF-EIGKRL--------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSIPK 154
Cdd:COG1123 108 ALENLGLSRaEARARVlelleavgLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 155 -------GSLISEHRTKHLLNLVQRVYLL-------SGDVREV--DKEKLEDQEFLRRNG---------------LRGFQ 203
Cdd:COG1123 188 lqrergtTVLLITHDLGVVAEIADRVVVMddgriveDGPPEEIlaAPQALAAVPRLGAARgraapaaaaaeplleVRNLS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 204 IEY-QRGSPGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTI-----------------------------LRKLSKKI 253
Cdd:COG1123 268 KRYpVRGKGGVRAVD---DVSLTLRRGETLGLVGESGSGKSTLarlllgllrptsgsilfdgkdltklsrrsLRELRRRV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 254 YSVFQNLDLQFF-HETVADEVGN-----------------DDALSLFGL-TELRERSPFTLSLGQKMRVLIASAYASGYK 314
Cdd:COG1123 345 QMVFQDPYSSLNpRMTVGDIIAEplrlhgllsraerrervAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPK 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2619813829 315 VIGLDEPTTAMDgdgLQNFVKMVELLRE--ERRGL--ILATHDKDVIP-ICDQII 364
Cdd:COG1123 425 LLILDEPTSALD---VSVQAQILNLLRDlqRELGLtyLFISHDLAVVRyIADRVA 476
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
203-367 |
2.24e-38 |
|
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: 136.44 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 203 QIEYQRGSPGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILR--------------------------KLSKKIYSV 256
Cdd:cd03225 4 NLSFSYPDGARPALD---DISLTIKKGEFVLIVGPNGSGKSTLLRllngllgptsgevlvdgkdltklslkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 257 FQNLDLQFFHETVADEV----GN------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDE 320
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVafglENlglpeeeieervEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2619813829 321 PTTAMDGDGLQNFVKMVELLREERRGLILATHD-KDVIPICDQIISLS 367
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLE 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
211-364 |
4.80e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 130.92 E-value: 4.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILR--------------------------KLSKKIYSVFQNLDLQF 264
Cdd:COG1122 12 GGTPALD---DVSLSIEKGEFVAIIGPNGSGKSTLLRllngllkptsgevlvdgkditkknlrELRRKVGLVFQNPDDQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 265 FHETVADEVG----N------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD 328
Cdd:COG1122 89 FAPTVEEDVAfgpeNlglpreeirervEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2619813829 329 GLQNFVKMVELLREERRGLILATHD-KDVIPICDQII 364
Cdd:COG1122 169 GRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVI 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
208-366 |
1.27e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.52 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 208 RGSPGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLS-----------------------KKIYSVFQNLDLQF 264
Cdd:cd03226 8 SYKKGTEILD---DLSLDLYAGEIIALTGKNGAGKTTLAKILAglikessgsillngkpikakerrKSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 265 FHETVADEV--GNDDA----------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQN 332
Cdd:cd03226 85 FTDSVREELllGLKELdagneqaetvLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190
....*....|....*....|....*....|....*
gi 2619813829 333 FVKMVELLREERRGLILATHDKDVIP-ICDQIISL 366
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEFLAkVCDRVLLL 199
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
212-357 |
1.26e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 101.73 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLS----------------------------KKIYSVFQNLDLQ 263
Cdd:TIGR01166 4 GPEVLK---GLNFAAERGEVLALLGANGAGKSTLLLHLNgllrpqsgavlidgepldysrkgllerrQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 FFHETVADEVG----N------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG 327
Cdd:TIGR01166 81 LFAADVDQDVAfgplNlglseaeverrvREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 2619813829 328 DGLQNFVKMVELLREERRGLILATHDKDVI 357
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-177 |
3.76e-25 |
|
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: 101.00 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINsILC-----QRHNVFLDDQDFCERKDYSLLSA---VFQDPSSQILATTLEDELRL-M 84
Cdd:cd03225 23 TIKKGEFVLIVGPNGSGKSTLLR-LLNgllgpTSGEVLVDGKDLTKLSLKELRRKvglVFQNPDDQFFGPTVEEEVAFgL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 85 SHFHHVNFEIGKRL--------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSI---- 152
Cdd:cd03225 102 ENLGLPEEEIEERVeealelvgLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLkklk 181
|
170 180
....*....|....*....|....*..
gi 2619813829 153 --PKGSLISEHRTKHLLNLVQRVYLLS 177
Cdd:cd03225 182 aeGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
221-367 |
1.14e-22 |
|
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: 94.47 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLSK-------KIY------------------------------SVFQNLDLQ 263
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGllppsagEVLwngepirdaredyrrrlaylghadglkpelTVRENLRFW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 F-FHETVADEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLRE 342
Cdd:COG4133 100 AaLYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLA 179
|
170 180
....*....|....*....|....*
gi 2619813829 343 ERRGLILATHDKDVIPiCDQIISLS 367
Cdd:COG4133 180 RGGAVLLTTHQPLELA-AARVLDLG 203
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-196 |
2.05e-21 |
|
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: 91.24 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTL---INSIL-CQRHNVFLDDQDFCERKDYSLLSA---VFQDPSSQILATTLEDE----LR 82
Cdd:COG1122 23 SIEKGEFVAIIGPNGSGKSTLlrlLNGLLkPTSGEVLVDGKDITKKNLRELRRKvglVFQNPDDQLFAPTVEEDvafgPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 83 lmshfhhvNF-----EIGKRL--------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLV- 148
Cdd:COG1122 103 --------NLglpreEIRERVeealelvgLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELl 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 149 --LGSIPKGS---LISEHRTKHLLNLVQRVYLLS-------GDVREVdkekLEDQEFLRR 196
Cdd:COG1122 175 elLKRLNKEGktvIIVTHDLDLVAELADRVIVLDdgrivadGTPREV----FSDYELLEE 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
199-364 |
4.15e-21 |
|
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: 94.58 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 199 LRGFQIEYQRGSPgsEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKL----------------------------- 249
Cdd:COG1123 7 VRDLSVRYPGGDV--PAVD---GVSLTIAPGETVALVGESGSGKSTLALALmgllphggrisgevlldgrdllelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 250 SKKIYSVFQNLDLQFFHETVADEVGN----------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGY 313
Cdd:COG1123 82 GRRIGMVFQDPMTQLNPVTVGDQIAEalenlglsraeararvLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2619813829 314 KVIGLDEPTTAMDGDG-LQNFVKMVELLREERRGLILATHDKDVI-PICDQII 364
Cdd:COG1123 162 DLLIADEPTTALDVTTqAEILDLLRELQRERGTTVLLITHDLGVVaEIADRVV 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
224-366 |
1.19e-20 |
|
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: 88.74 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILR---------------------KLSKKIYSVFQNLDLQF-FHETVADEVGN------ 275
Cdd:cd03235 20 FEVKPGEFLAIVGPNGAGKSTLLKailgllkptsgsirvfgkpleKERKRIGYVPQRRSIDRdFPISVRDVVLMglyghk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 --------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLR 341
Cdd:cd03235 100 glfrrlskadkakvDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR 179
|
170 180
....*....|....*....|....*.
gi 2619813829 342 EERRGLILATHD-KDVIPICDQIISL 366
Cdd:cd03235 180 REGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
206-364 |
1.19e-20 |
|
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: 90.20 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSPGSE--ILDVQvglrLKVRGGEVVCLIGKNGVGKTTI-----------------------------LRKLSKKIY 254
Cdd:TIGR04521 10 YQPGTPFEKkaLDDVS----LTIEDGEFVAIIGHTGSGKSTLiqhlngllkptsgtvtidgrditakkkkkLKDLRKKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 255 SVFQNLDLQFFHETVADEV-------GNDD---------ALSLFGLTE-LRERSPFTLSLGQKMRVLIASAYASGYKVIG 317
Cdd:TIGR04521 86 LVFQFPEHQLFEETVYKDIafgpknlGLSEeeaeervkeALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2619813829 318 LDEPTTAMDGDGLQNFVKMV-ELLREERRGLILATHD-KDVIPICDQII 364
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFkRLHKEKGLTVILVTHSmEDVAEYADRVI 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
211-364 |
2.26e-20 |
|
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: 87.11 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSK-------KIYsvFQNLDL-QFFHETVADEVGN-DDALSL 281
Cdd:cd03214 10 GGRTVLD---DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGllkpssgEIL--LDGKDLaSLSPKELARKIAYvPQALEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 282 FGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdgLQNFVKMVELLR----EERRGLILATHDKD-V 356
Cdd:cd03214 85 LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD---IAHQIELLELLRrlarERGKTVVMVLHDLNlA 161
|
....*...
gi 2619813829 357 IPICDQII 364
Cdd:cd03214 162 ARYADRVI 169
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
221-364 |
8.38e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 84.34 E-value: 8.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR-------------------------KLSKKIYSVFQNLD----------LQFF 265
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRmllgllrptsgevrvlgedvardpaEVRRRIGYVPQEPAlypdltvrenLRFF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 -------HETVADEVgnDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVE 338
Cdd:COG1131 98 arlyglpRKEARERI--DELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLR 175
|
170 180
....*....|....*....|....*..
gi 2619813829 339 LLREERRGLILATHD-KDVIPICDQII 364
Cdd:COG1131 176 ELAAEGKTVLLSTHYlEEAERLCDRVA 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
212-359 |
8.39e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTT-------ILR---------------------KLSKKIYSVFQNLDLQ 263
Cdd:PRK13639 14 GTEALK---GINFKAEKGEMVALLGPNGAGKSTlflhfngILKptsgevlikgepikydkksllEVRKTVGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 FFHETVADEVG----------------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG 327
Cdd:PRK13639 91 LFAPTVEEDVAfgplnlglskeevekrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190
....*....|....*....|....*....|..
gi 2619813829 328 DGLQNFVKMVELLREERRGLILATHDKDVIPI 359
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPV 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
221-364 |
1.02e-18 |
|
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: 84.14 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIY-------------------------------------SVFQNLDLQ 263
Cdd:COG4555 19 DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpdsgsilidgedvrkeprearrqigvlpderglydrlTVRENIRYF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 F-FHETVADEVGN--DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELL 340
Cdd:COG4555 99 AeLYGLFDEELKKriEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL 178
|
170 180
....*....|....*....|....*
gi 2619813829 341 REERRGLILATHD-KDVIPICDQII 364
Cdd:COG4555 179 KKEGKTVLFSSHImQEVEALCDRVV 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
211-366 |
1.03e-18 |
|
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: 81.91 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIYSVFQNLDLqffhetvadevgNDDALSLFGLTELRER 290
Cdd:cd00267 10 GGRTALD---NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI------------DGKDIAKLPLEELRRR 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2619813829 291 SP--FTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHD-KDVIPICDQIISL 366
Cdd:cd00267 75 IGyvPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVL 153
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
224-366 |
1.56e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 84.30 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLS--------------------------KKIYSVFQNLDLQFFHETVADEVG--- 274
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNglllpeagtitvggmvlseetvwdvrRQVGMVFQNPDNQFVGATVQDDVAfgl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 -N------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLR 341
Cdd:PRK13635 108 eNigvpreemvervDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLK 187
|
170 180
....*....|....*....|....*.
gi 2619813829 342 EERRGLILA-THDKDVIPICDQIISL 366
Cdd:PRK13635 188 EQKGITVLSiTHDLDEAAQADRVIVM 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
206-364 |
1.90e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 84.30 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSP--GSEILDVQVglrlKVRGGEVVCLIGKNGVGKTTI------------------------------LRKLSKKI 253
Cdd:PRK13634 12 YQYKTPfeRRALYDVNV----SIPSGSYVAIIGHTGSGKSTLlqhlngllqptsgtvtigervitagkknkkLKPLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 254 YSVFQNLDLQFFHETVADE---------VGNDDA-------LSLFGLTE-LRERSPFTLSLGQKMRVLIASAYASGYKVI 316
Cdd:PRK13634 88 GIVFQFPEHQLFEETVEKDicfgpmnfgVSEEDAkqkaremIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2619813829 317 GLDEPTTAMDGDGLQNFVKMVELLREErRGL--ILATHD-KDVIPICDQII 364
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKE-KGLttVLVTHSmEDAARYADQIV 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
212-366 |
3.61e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 83.25 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTIL--------------------------RKLSKKIYSVFQNLDLQFF 265
Cdd:PRK13647 17 GTKALK---GLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgrvkvmgrevnaeneKWVRSKVGLVFQDPDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 HETVADEVG----------------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDG 329
Cdd:PRK13647 94 SSTVWDDVAfgpvnmgldkdeverrVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2619813829 330 LQNFVKMVELLREERRGLILATHDKD-VIPICDQIISL 366
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVL 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
205-367 |
4.17e-18 |
|
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: 82.15 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 205 EYQRGSPGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLS------------------------------KKIY 254
Cdd:cd03255 9 TYGGGGEKVQALK---GVSLSIEKGEFVAIVGPSGSGKSTLLNILGgldrptsgevrvdgtdisklsekelaafrrRHIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 255 SVFQ------------NLDLQFFHETVADEVGNDDALSLF---GLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLD 319
Cdd:cd03255 86 FVFQsfnllpdltaleNVELPLLLAGVPKKERRERAEELLervGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2619813829 320 EPTTAMDGDGLQNFVK-MVELLREERRGLILATHDKDVIPICDQIISLS 367
Cdd:cd03255 166 EPTGNLDSETGKEVMElLRELNKEAGTTIVVVTHDPELAEYADRIIELR 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
221-364 |
4.23e-18 |
|
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: 80.90 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR-------------------------KLSKKIYSVFQNLDLqFFHETVADevgN 275
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGKTTLIKiilgllkpdsgeikvlgkdikkepeEVKRRIGYLPEEPSL-YENLTVRE---N 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 ddalslfgltelrerspFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHD-K 354
Cdd:cd03230 94 -----------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIlE 156
|
170
....*....|
gi 2619813829 355 DVIPICDQII 364
Cdd:cd03230 157 EAERLCDRVA 166
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
222-367 |
4.96e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.73 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 222 LRLKVRGGEVVCLIGKNGVGKTTI--------------------------LRKLSKKIYSVFQNLDLQFFHETVADEVG- 274
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTIskiltgllkpqsgeikidgitiskenLKEIRKKIGIIFQNPDNQFIGATVEDDIAf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 ---N------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVK-MVE 338
Cdd:PRK13632 108 gleNkkvppkkmkdiiDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKiMVD 187
|
170 180
....*....|....*....|....*....
gi 2619813829 339 LLREERRGLILATHDKDVIPICDQIISLS 367
Cdd:PRK13632 188 LRKTRKKTLISITHDMDEAILADKVIVFS 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
226-364 |
9.54e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.09 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 226 VRGGEVVCLIGKNGVGKTTILR--------------------------KLSKKIYSVFQNLDLQFFHETVADEVG----- 274
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRlidglleaesgqiiidgdllteenvwDIRHKIGMVFQNPDNQFVGATVEDDVAfglen 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 -----------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREE 343
Cdd:PRK13650 110 kgipheemkerVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDD 189
|
170 180
....*....|....*....|..
gi 2619813829 344 RR-GLILATHDKDVIPICDQII 364
Cdd:PRK13650 190 YQmTVISITHDLDEVALSDRVL 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
221-367 |
4.02e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.66 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR----------------------------KLSKKIYSVFQNLDLQFFHETV--- 269
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQnlngilkpssgrilfdgkpidysrkglmKLRESVGMVFQDPDNQLFSASVyqd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 270 -----------ADEVGN--DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKM 336
Cdd:PRK13636 104 vsfgavnlklpEDEVRKrvDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL 183
|
170 180 190
....*....|....*....|....*....|...
gi 2619813829 337 V-ELLREERRGLILATHDKDVIPI-CDQIISLS 367
Cdd:PRK13636 184 LvEMQKELGLTIIIATHDIDIVPLyCDNVFVMK 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
224-367 |
5.23e-17 |
|
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: 79.16 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTI-----------------------------LRKLSKKIYSVFQNLDLqFFHETVADEV- 273
Cdd:cd03258 26 LSVPKGEIFGIIGRSGAGKSTLircinglerptsgsvlvdgtdltllsgkeLRKARRRIGMIFQHFNL-LSSRTVFENVa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 274 ------GNDDA---------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNfvkMVE 338
Cdd:cd03258 105 lpleiaGVPKAeieervlelLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQS---ILA 181
|
170 180 190
....*....|....*....|....*....|....
gi 2619813829 339 LLRE--ERRGL--ILATHDKDVI-PICDQIISLS 367
Cdd:cd03258 182 LLRDinRELGLtiVLITHEMEVVkRICDRVAVME 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
211-366 |
1.48e-16 |
|
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: 76.31 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTilrkLSKKIYSVFQnldlqffhetvADEvGNddaLSLFGlTELRER 290
Cdd:cd03216 11 GGVKALD---GVSLSVRRGEVHALLGENGAGKST----LMKILSGLYK-----------PDS-GE---ILVDG-KEVSFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 291 SP-----------FTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHD-KDVIP 358
Cdd:cd03216 68 SPrdarragiamvYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFE 147
|
....*...
gi 2619813829 359 ICDQIISL 366
Cdd:cd03216 148 IADRVTVL 155
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
206-367 |
2.39e-16 |
|
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: 77.13 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSPGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKL---------------------SKKIYSVFQNlDLQF 264
Cdd:cd03293 10 YGGGGGAVTALE---DISLSVEEGEFVALVGPSGCGKSTLLRIIaglerptsgevlvdgepvtgpGPDRGYVFQQ-DALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 265 FHETVADEV-------GN---------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG- 327
Cdd:cd03293 86 PWLTVLDNValglelqGVpkaeareraEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAl 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2619813829 328 --DGLQNFvkMVELLREERRGLILATHDKD-VIPICDQIISLS 367
Cdd:cd03293 166 trEQLQEE--LLDIWRETGKTVLLVTHDIDeAVFLADRVVVLS 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
218-357 |
2.87e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 218 VQVGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIY-----SVFQNLDLQFFHE-TVADEVGNDD-------ALSLFGL 284
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtpvaGCVDVPDNQFGREaSLIDAIGRKGdfkdaveLLNAVGL 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2619813829 285 TE--LRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQnFV--KMVELLREERRGLILATHDKDVI 357
Cdd:COG2401 125 SDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK-RVarNLQKLARRAGITLVVATHHYDVI 200
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
221-364 |
3.41e-16 |
|
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: 76.40 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLSK-------KIYS-----------------VFQNLDLqFFHETVADEVG-- 274
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlerpdsgEILIdgrdvtgvpperrnigmVFQDYAL-FPHLTVAENIAfg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 --------------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG---DGLQNFVKmv 337
Cdd:cd03259 97 lklrgvpkaeirarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAklrEELREELK-- 174
|
170 180
....*....|....*....|....*...
gi 2619813829 338 ELLREERRGLILATHDK-DVIPICDQII 364
Cdd:cd03259 175 ELQRELGITTIYVTHDQeEALALADRIA 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
212-364 |
4.08e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 77.05 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILR---------------------KLSKKI-YsVFQ--NLDLQFF-- 265
Cdd:COG1121 18 GRPVLE---DVSLTIPPGEFVAIVGPNGAGKSTLLKailgllpptsgtvrlfgkpprRARRRIgY-VPQraEVDWDFPit 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 -HETVA------------------DEVgnDDALSLFGLTELRERsPF-TLSLGQKMRVLIASAYASGYKVIGLDEPTTAM 325
Cdd:COG1121 94 vRDVVLmgrygrrglfrrpsradrEAV--DEALERVGLEDLADR-PIgELSGGQQQRVLLARALAQDPDLLLLDEPFAGV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2619813829 326 DGDGLQNFVKMVELLREERRGLILATHD-KDVIPICDQII 364
Cdd:COG1121 171 DAATEEALYELLRELRREGKTILVVTHDlGAVREYFDRVL 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
221-363 |
1.33e-15 |
|
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: 75.41 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR--------------------------KLSKKIYSVFQNLDLqFFHETVADEVG 274
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKminrlieptsgeifidgedireqdpvELRRKIGYVIQQIGL-FPHMTVEENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 ----------------NDDALSLFGL--TELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG---DGLQNf 333
Cdd:cd03295 98 lvpkllkwpkekirerADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrDQLQE- 176
|
170 180 190
....*....|....*....|....*....|.
gi 2619813829 334 vKMVELLREERRGLILATHDKD-VIPICDQI 363
Cdd:cd03295 177 -EFKRLQQELGKTIVFVTHDIDeAFRLADRI 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
166-366 |
1.42e-15 |
|
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: 77.95 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 166 LLNLVQRVYLLS------GDVREVDKEKLEDQEFLRRNGLRGfQIE-------YQRGSPgsEILDvqvGLRLKVRGGEVV 232
Cdd:COG2274 431 LIGLLQRFQDAKialerlDDILDLPPEREEGRSKLSLPRLKG-DIElenvsfrYPGDSP--PVLD---NISLTIKPGERV 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 233 CLIGKNGVGKTTILRKLSK-------KIY-------------------SVFQnlDLQFFHETVADEV--GNDD------- 277
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLGlyeptsgRILidgidlrqidpaslrrqigVVLQ--DVFLFSGTIRENItlGDPDatdeeii 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 278 -ALSLFGL------------TELRERSpFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVkmvELLREER 344
Cdd:COG2274 583 eAARLAGLhdfiealpmgydTVVGEGG-SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL---ENLRRLL 658
|
250 260
....*....|....*....|....
gi 2619813829 345 RG--LILATHDKDVIPICDQIISL 366
Cdd:COG2274 659 KGrtVIIIAHRLSTIRLADRIIVL 682
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
224-366 |
1.95e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.81 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTIL-------------------------------RKLSKKIYSVFQNLDLQFFHETVADE 272
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIqltngliisetgqtivgdyaipanlkkikevKRLRKEIGLVFQFPEYQLFQETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 273 V-------GND---------DALSLFGL-TELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVK 335
Cdd:PRK13645 112 IafgpvnlGENkqeaykkvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFIN 191
|
170 180 190
....*....|....*....|....*....|...
gi 2619813829 336 MVELL-REERRGLILATHDKD-VIPICDQIISL 366
Cdd:PRK13645 192 LFERLnKEYKKRIIMVTHNMDqVLRIADEVIVM 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
221-364 |
4.87e-15 |
|
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: 72.22 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR----------------------------KLSKKIYSVFQNLDLqFFHETVADE 272
Cdd:cd03229 18 DVSLNIEAGEIVALLGPSGSGKSTLLRciagleepdsgsilidgedltdledelpPLRRRIGMVFQDFAL-FPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 273 VGnddalslfgltelrerspFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD---GDGLQNFVKmvELLREERRGLIL 349
Cdd:cd03229 97 IA------------------LGLSGGQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLK--SLQAQLGITVVL 156
|
170
....*....|....*.
gi 2619813829 350 ATHD-KDVIPICDQII 364
Cdd:cd03229 157 VTHDlDEAARLADRVV 172
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
222-366 |
5.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.45 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 222 LRLKVRGGEVVCLIGKNGVGKTTILRKLS-----------------------------KKIYSVFQNLDLQFFHETVADE 272
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINglllpddnpnskitvdgitltaktvwdirEKVGIVFQNPDNQFVGATVGDD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 273 VG----------------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKM 336
Cdd:PRK13640 106 VAfglenravprpemikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL 185
|
170 180 190
....*....|....*....|....*....|.
gi 2619813829 337 VELLREERRGLILA-THDKDVIPICDQIISL 366
Cdd:PRK13640 186 IRKLKKKNNLTVISiTHDIDEANMADQVLVL 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
217-357 |
7.24e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.27 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 217 DVQVGLRLKVRGGEVVCLIGKNGVGKTTIL---------------RKLSKKIYSVFQNLDL-QFFHETVADEVGN----- 275
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLkvlagvlrptsgtvrRAGGARVAYVPQRSEVpDSLPLTVRDLVAMgrwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 ---------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELL 340
Cdd:NF040873 86 rglwrrltrddraavDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEE 165
|
170
....*....|....*..
gi 2619813829 341 REERRGLILATHDKDVI 357
Cdd:NF040873 166 HARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
206-364 |
9.08e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.93 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSP-GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTI----------------------------LRKLSKKIYSV 256
Cdd:PRK13637 12 YMEGTPfEKKALD---NVNIEIEDGEFVGLIGHTGSGKSTLiqhlngllkptsgkiiidgvditdkkvkLSDIRKKVGLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 257 FQNLDLQFFHETVA--------------DEVGN--DDALSLFGLT--ELRERSPFTLSLGQKMRVLIASAYASGYKVIGL 318
Cdd:PRK13637 89 FQYPEYQLFEETIEkdiafgpinlglseEEIENrvKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2619813829 319 DEPTTAMDGDGLQNFVKMVELLREERR-GLILATHD-KDVIPICDQII 364
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSmEDVAKLADRII 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
222-367 |
1.53e-14 |
|
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: 70.17 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 222 LRLKVRGGEVVCLIGKNGVGKTTILRKLSKK------IYSVFQNLDLQFFHEtvadevgnddalslfgltelrerspftL 295
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGElepdegIVTWGSTVKIGYFEQ---------------------------L 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2619813829 296 SLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQnfvKMVELLREERRGLILATHDKDVI-PICDQIISLS 367
Cdd:cd03221 72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE---ALEEALKEYPGTVILVSHDRYFLdQVATKIIELE 141
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
207-360 |
1.78e-14 |
|
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: 72.42 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 207 QRGspGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIYSVFQNlDLQFF--------------------- 265
Cdd:COG1119 12 RRG--GKTILD---DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN-DVRLFgerrggedvwelrkriglvsp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 --------HETVAD--------------EVGNDD------ALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIG 317
Cdd:COG1119 86 alqlrfprDETVLDvvlsgffdsiglyrEPTDEQrerareLLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2619813829 318 LDEPTTAMDGDGLQNFVKMVELL-REERRGLILATHDKDVIPIC 360
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPG 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
221-323 |
1.85e-14 |
|
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: 69.98 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR--------------------------KLSKKIYSVFQNLDLqFFHETVADEVG 274
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKliagllsptegtilldgqdltdderkSLRKEIGYVFQDPQL-FPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2619813829 275 N----------------DDALSLFGLTELRER----SPFTLSLGQKMRVLIASAYASGYKVIGLDEPTT 323
Cdd:pfam00005 82 LglllkglskrekdaraEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-176 |
3.04e-14 |
|
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: 70.12 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILCQRH----NVFLDDQDFCERKD--YSLLSAVFQDPSsqilattLEDELRLMshf 87
Cdd:cd03230 22 TVEKGEIYGLLGPNGAGKTTLIKIILGLLKpdsgEIKVLGKDIKKEPEevKRRIGYLPEEPS-------LYENLTVR--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 88 hhvnfeigkrlmgpyfstDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSI------PKGSLISEH 161
Cdd:cd03230 92 ------------------ENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLrelkkeGKTILLSSH 153
|
170
....*....|....*
gi 2619813829 162 RTKHLLNLVQRVYLL 176
Cdd:cd03230 154 ILEEAERLCDRVAIL 168
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
221-353 |
3.47e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.70 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR----------------------------------KLSKKIYSVFQNLDLqFFH 266
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTLLRcinlleqpeagtirvgditidtarslsqqkglirQLRQHVGFVFQNFNL-FPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 267 ETVADEV----------GNDDA-------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDG 329
Cdd:PRK11264 100 RTVLENIiegpvivkgePKEEAtararelLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180
....*....|....*....|....
gi 2619813829 330 LQNFVKMVELLREERRGLILATHD 353
Cdd:PRK11264 180 VGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
224-367 |
5.49e-14 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 70.26 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILR---------------------KLSKKIYSVFQNLDLQ------------------- 263
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRailglippakgtvkvagaspgKGWRHIGYVPQRHEFAwdfpisvahtvmsgrtghi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 --FFHETVADEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLR 341
Cdd:TIGR03771 81 gwLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180
....*....|....*....|....*..
gi 2619813829 342 EERRGLILATHD-KDVIPICDQIISLS 367
Cdd:TIGR03771 161 GAGTAILMTTHDlAQAMATCDRVVLLN 187
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
221-352 |
7.48e-14 |
|
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: 69.69 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS-------------------------------------KKIYSVFQNLdlQ 263
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAgllrpdsgevrwngtplaeqrdephenilylghlpglKPELSALENL--H 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 FFHETVADEVGN-DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFvkmVELLRE 342
Cdd:TIGR01189 96 FWAAIHGGAQRTiEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL---AGLLRA 172
|
170
....*....|...
gi 2619813829 343 --ERRGL-ILATH 352
Cdd:TIGR01189 173 hlARGGIvLLTTH 185
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
221-353 |
7.82e-14 |
|
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: 69.87 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR----------------------------KLSKKIYSVFQNLDLqFFHETV--- 269
Cdd:cd03262 18 GIDLTVKKGEVVVIIGPSGSGKSTLLRcinlleepdsgtiiidglkltddkkninELRQKVGMVFQQFNL-FPHLTVlen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 270 ---------------ADEVGnDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFV 334
Cdd:cd03262 97 itlapikvkgmskaeAEERA-LELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170
....*....|....*....
gi 2619813829 335 KMVELLREERRGLILATHD 353
Cdd:cd03262 176 DVMKDLAEEGMTMVVVTHE 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
206-355 |
8.32e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.93 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSP--GSEILDVQvglrLKVRGGEVVCLIGKNGVGKTTILRKLS------------------------------KKI 253
Cdd:PRK13649 12 YQAGTPfeGRALFDVN----LTIEDGSYTAFIGHTGSGKSTIMQLLNglhvptqgsvrvddtlitstsknkdikqirKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 254 YSVFQNLDLQFFHETVADEVG---------NDDA-------LSLFGLTE-LRERSPFTLSLGQKMRVLIASAYASGYKVI 316
Cdd:PRK13649 88 GLVFQFPESQLFEETVLKDVAfgpqnfgvsQEEAealarekLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 2619813829 317 GLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKD 355
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
199-364 |
1.16e-13 |
|
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: 69.46 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 199 LRGFQIEYQRGSPGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILR-----------------------------KL 249
Cdd:cd03257 4 VKNLSVSFPTGGGSVKALD---DVSFSIKKGETLGLVGESGSGKSTLARailgllkptsgsiifdgkdllklsrrlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 250 SKKIYSVFQN----LD------------LQFFHETVADE---VGNDDALSLFGLTELRERS-PFTLSLGQKMRVLIASAY 309
Cdd:cd03257 81 RKEIQMVFQDpmssLNprmtigeqiaepLRIHGKLSKKEarkEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 310 ASGYKVIGLDEPTTAMDGDgLQnfVKMVELLREERR----GLILATHDKDVI-PICDQII 364
Cdd:cd03257 161 ALNPKLLIADEPTSALDVS-VQ--AQILDLLKKLQEelglTLLFITHDLGVVaKIADRVA 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
212-367 |
1.90e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILR--------------------------KLSKKIYSVFQNLDLQF- 264
Cdd:PRK09536 15 DTTVLD---GVDLSVREGSLVGLVGPNGAGKTTLLRaingtltptagtvlvagddvealsarAASRRVASVPQDTSLSFe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 265 F------------H------ETVADEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD 326
Cdd:PRK09536 92 FdvrqvvemgrtpHrsrfdtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2619813829 327 gdgLQNFVKMVELLR---EERRGLILATHDKDVIP-ICDQIISLS 367
Cdd:PRK09536 172 ---INHQVRTLELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLA 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
217-353 |
2.55e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 217 DVQV--GLRLKVRGGEVVCLIGKNGVGKTTILRKLSK--KIYS--------------------------VFQNLDLqFFH 266
Cdd:PRK09493 13 PTQVlhNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKleEITSgdlivdglkvndpkvderlirqeagmVFQQFYL-FPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 267 ETVADEV--------------GNDDALSLFGLTELRERS---PFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDG 329
Cdd:PRK09493 92 LTALENVmfgplrvrgaskeeAEKQARELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180
....*....|....*....|....
gi 2619813829 330 LQNFVKMVELLREERRGLILATHD 353
Cdd:PRK09493 172 RHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-190 |
2.94e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 68.55 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILCQRH----NVFLDDQDFCE--RKDYSLLSAVFQDPSSqILATTLEDELRLMSHF 87
Cdd:COG1131 22 TVEPGEIFGLLGPNGAGKTTTIRMLLGLLRptsgEVRVLGEDVARdpAEVRRRIGYVPQEPAL-YPDLTVRENLRFFARL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 88 HHVNFEIGKRLMGPYFstDFFKLSD-----------GYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLgsipkgS 156
Cdd:COG1131 101 YGLPRKEARERIDELL--ELFGLTDaadrkvgtlsgGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELW------E 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2619813829 157 LISEHRTK--------HLLNLVQRVY-----------LLSGDVREVDKEKLED 190
Cdd:COG1131 173 LLRELAAEgktvllstHYLEEAERLCdrvaiidkgriVADGTPDELKARLLED 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
221-352 |
4.22e-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: 67.52 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS-------------------------------------KKIYSVFQNLdlQ 263
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAglspplagrvllnggpldfqrdsiargllylghapgiKTTLSVLENL--R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 FFHETVADEvGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREE 343
Cdd:cd03231 96 FWHADHSDE-QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCAR 174
|
....*....
gi 2619813829 344 RRGLILATH 352
Cdd:cd03231 175 GGMVVLTTH 183
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
221-366 |
4.71e-13 |
|
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: 67.85 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIY----SV-----------------------FQNLDLqFFHETVADEV 273
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgSVlfdgeditglppheiarlgigrtFQIPRL-FPELTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 274 --------GN------------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG 327
Cdd:cd03219 97 mvaaqartGSglllararreereareraEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2619813829 328 DGLQNFVKMVELLREERRGLILATHDKDVI-PICDQIISL 366
Cdd:cd03219 177 EETEELAELIRELRERGITVLLVEHDMDVVmSLADRVTVL 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
221-366 |
6.34e-13 |
|
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: 67.39 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS------------------KKIYSVFQNL-----------------DLQFF 265
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAgllepdagfatvdgfdvvKEPAEARRRLgfvsdstglydrltareNLEYF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 ---HETVADEVGN--DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELL 340
Cdd:cd03266 103 aglYGLKGDELTArlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL 182
|
170 180
....*....|....*....|....*..
gi 2619813829 341 REERRGLILATHD-KDVIPICDQIISL 366
Cdd:cd03266 183 RALGKCILFSTHImQEVERLCDRVVVL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
221-353 |
6.69e-13 |
|
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: 67.26 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS------------------------KKIYSVFQNLDLqFFHETVADEVG-- 274
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgfetptsgeilldgkditnlpphkRPVNTVFQNYAL-FPHLTVFENIAfg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 --------------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdglqnfVKMVELL 340
Cdd:cd03300 97 lrlkklpkaeikerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD-------LKLRKDM 169
|
170 180
....*....|....*....|.
gi 2619813829 341 REERRGL--------ILATHD 353
Cdd:cd03300 170 QLELKRLqkelgitfVFVTHD 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
232-358 |
8.33e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 232 VCLIGKNGVGKTTI--------------------------LRKLSKKIYSVFQNLDLQFFHETVADEVG----------- 274
Cdd:PRK13652 33 IAVIGPNGAGKSTLfrhfngilkptsgsvlirgepitkenIREVRKFVGLVFQNPDDQIFSPTVEQDIAfgpinlgldee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 -----NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREER-RGLI 348
Cdd:PRK13652 113 tvahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgMTVI 192
|
170
....*....|
gi 2619813829 349 LATHDKDVIP 358
Cdd:PRK13652 193 FSTHQLDLVP 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
225-366 |
8.45e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.85 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 225 KVRGGEVVCLIGKNGVGKTTI--------------------------LRKLSKKIYSVFQNLDLQFFHETVADEVG---- 274
Cdd:PRK13648 31 NIPKGQWTSIVGHNGSGKSTIaklmigiekvksgeifynnqaitddnFEKLRKHIGIVFQNPDNQFVGSIVKYDVAfgle 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 -----NDD-------ALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLRE 342
Cdd:PRK13648 111 nhavpYDEmhrrvseALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKS 190
|
170 180
....*....|....*....|....*
gi 2619813829 343 ERRGLILA-THDKDVIPICDQIISL 366
Cdd:PRK13648 191 EHNITIISiTHDLSEAMEADHVIVM 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
221-363 |
1.56e-12 |
|
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: 65.99 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS------------------KKIYSVFQNL------D-----------LQFF 265
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgelrptsgtayingysirTDRKAARQSLgycpqfDalfdeltvrehLRFY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 ------HETVADEVGNDDaLSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgDGLQNFVkmVEL 339
Cdd:cd03263 100 arlkglPKSEIKEEVELL-LRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PASRRAI--WDL 175
|
170 180
....*....|....*....|....*..
gi 2619813829 340 LREERRG--LILATHDKDVIPI-CDQI 363
Cdd:cd03263 176 ILEVRKGrsIILTTHSMDEAEAlCDRI 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-176 |
1.59e-12 |
|
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: 66.42 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINsILC-----QRHNVFLDDQDFcERKDYSLLSAVFQDPSSQIL--ATTLEDELRLMSH 86
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLR-MLAgllkpDSGSILIDGEDV-RKEPREARRQIGVLPDERGLydRLTVRENIRYFAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 87 FHHVNFEIGKRL---------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSI----- 152
Cdd:COG4555 101 LYGLFDEELKKRieeliellgLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILralkk 180
|
170 180
....*....|....*....|....*
gi 2619813829 153 -PKGSLISEHRTKHLLNLVQRVYLL 176
Cdd:COG4555 181 eGKTVLFSSHIMQEVEALCDRVVIL 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
217-357 |
1.64e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 217 DVQV--GLRLKVRGGEVVCLIGKNGVGKTTILRKLS----------------------------KKIYSVFQNLDLQFFH 266
Cdd:PRK13638 13 DEPVlkGLNLDFSLSPVTGLVGANGCGKSTLFMNLSgllrpqkgavlwqgkpldyskrgllalrQQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 267 ETV--------------ADEVGN--DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGL 330
Cdd:PRK13638 93 TDIdsdiafslrnlgvpEAEITRrvDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180
....*....|....*....|....*..
gi 2619813829 331 QNFVKMVELLREERRGLILATHDKDVI 357
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLI 199
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-176 |
2.21e-12 |
|
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: 64.19 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCERKDYSL---LSAVFQdpssqilattledelrlms 85
Cdd:cd00267 20 LTLKAGEIVALVGPNGSGKSTLLRAIAgllkPTSGEILIDGKDIAKLPLEELrrrIGYVPQ------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 86 hfhhvnfeigkrlmgpyfstdffkLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSI----PKGS--LIS 159
Cdd:cd00267 81 ------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLrelaEEGRtvIIV 136
|
170
....*....|....*..
gi 2619813829 160 EHRTKHLLNLVQRVYLL 176
Cdd:cd00267 137 THDPELAELAADRVIVL 153
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
235-355 |
2.30e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.03 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 235 IGKNGVGKTTILRKLSKKIYSVFQNLDLQFFHETVADE---------VGNDDA-------LSLFGLTE-LRERSPFTLSL 297
Cdd:PRK13651 89 IQKTRFKKIKKIKEIRRRVGVVFQFAEYQLFEQTIEKDiifgpvsmgVSKEEAkkraakyIELVGLDEsYLQRSPFELSG 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2619813829 298 GQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKD 355
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
221-366 |
2.44e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.66 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR--------------------------KLSKKIYSVFQNLDLQFFHETVADEVG 274
Cdd:PRK13642 25 GVSFSITKGEWVSIIGQNGSGKSTTARlidglfeefegkvkidgelltaenvwNLRRKIGMVFQNPDNQFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 ----------------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVE 338
Cdd:PRK13642 105 fgmenqgipreemikrVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH 184
|
170 180
....*....|....*....|....*....
gi 2619813829 339 LLREERRGLILA-THDKDVIPICDQIISL 366
Cdd:PRK13642 185 EIKEKYQLTVLSiTHDLDEAASSDRILVM 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
206-355 |
2.50e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.68 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSP--GSEILDVQvglrLKVRGGEVVCLIGKNGVGKTTILRKLS------------------------------KKI 253
Cdd:PRK13643 11 YQPNSPfaSRALFDID----LEVKKGSYTALIGHTGSGKSTLLQHLNgllqptegkvtvgdivvsstskqkeikpvrKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 254 YSVFQNLDLQFFHETVADEVG----------------NDDALSLFGLT-ELRERSPFTLSLGQKMRVLIASAYASGYKVI 316
Cdd:PRK13643 87 GVVFQFPESQLFEETVLKDVAfgpqnfgipkekaekiAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 2619813829 317 GLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKD 355
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
205-364 |
3.72e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.88 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 205 EYQRGSPGSEILDVQvGLRLKVRGGEVVCLIGKNGVGKTTILRKL-------SKKIYS--------------------VF 257
Cdd:PRK13633 13 KYESNEESTEKLALD-DVNLEVKKGEFLVILGRNGSGKSTIAKHMnallipsEGKVYVdgldtsdeenlwdirnkagmVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 258 QNLDLQFFHETVADEVG----N------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEP 321
Cdd:PRK13633 92 QNPDNQIVATIVEEDVAfgpeNlgippeeirervDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2619813829 322 TTAMDGDGLQNFVKMV-ELLREERRGLILATHDKDVIPICDQII 364
Cdd:PRK13633 172 TAMLDPSGRREVVNTIkELNKKYGITIILITHYMEEAVEADRII 215
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
214-366 |
4.32e-12 |
|
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: 64.56 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 214 EILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKL----------------------SKKIYS--------VFQNLDLq 263
Cdd:TIGR03608 12 VILD---DLNLTIEKGKMYAIIGESGSGKSTLLNIIgllekfdsgqvylngqetpplnSKKASKfrreklgyLFQNFAL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 FFHETVADevgNDD-------------------ALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTA 324
Cdd:TIGR03608 88 IENETVEE---NLDlglkykklskkekrekkkeALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2619813829 325 MDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQIISL 366
Cdd:TIGR03608 165 LDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-190 |
4.89e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.84 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 4 ITHPYLPG-----------KVELERDEIVGLVGRNGSGKTTLI---NSIL-CQRHNVFLDDQDFCE--------RKDYSL 60
Cdd:PRK13637 8 LTHIYMEGtpfekkaldnvNIEIEDGEFVGLIGHTGSGKSTLIqhlNGLLkPTSGKIIIDGVDITDkkvklsdiRKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 61 lsaVFQDPSSQILATTLEDELRlmshFHHVNF-----EIGKR------LMG----PYFSTDFFKLSDGYRKRFVISSVLS 125
Cdd:PRK13637 88 ---VFQYPEYQLFEETIEKDIA----FGPINLglseeEIENRvkramnIVGldyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 126 YGPEYLLIDEPLSNLDDEGIKLVLGSIPK-------GSLISEHRTKHLLNLVQRVYL-------LSGDVREVDKE--KLE 189
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKElhkeynmTIILVSHSMEDVAKLADRIIVmnkgkceLQGTPREVFKEveTLE 240
|
.
gi 2619813829 190 D 190
Cdd:PRK13637 241 S 241
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
211-364 |
5.21e-12 |
|
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: 64.53 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDVQvGLRLKVRGGEVVCLIGKNGVGKTTILR--------------------------KLSKKIYSVFQNLDLqf 264
Cdd:cd03245 13 PNQEIPALD-NVSLTIRAGEKVAIIGRVGSGKSTLLKllaglykptsgsvlldgtdirqldpaDLRRNIGYVPQDVTL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 265 FHETVAD--EVGN---DD-----ALSLFGLTELRERSP-----------FTLSLGQKMRVLIASAYASGYKVIGLDEPTT 323
Cdd:cd03245 90 FYGTLRDniTLGAplaDDerilrAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2619813829 324 AMDgdgLQNFVKMVELLREERRG--LILATHDKDVIPICDQII 364
Cdd:cd03245 170 AMD---MNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRII 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-154 |
6.84e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTL---INSILC-QRHNVFLDDQDFCERKDY----SLLSAVFQDPSSQILATTLEDELRlms 85
Cdd:PRK13633 32 EVKKGEFLVILGRNGSGKSTIakhMNALLIpSEGKVYVDGLDTSDEENLwdirNKAGMVFQNPDNQIVATIVEEDVA--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 86 hFHHVNF-----EIGKRL--------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSI 152
Cdd:PRK13633 109 -FGPENLgippeEIRERVdeslkkvgMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTI 187
|
..
gi 2619813829 153 PK 154
Cdd:PRK13633 188 KE 189
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
206-362 |
1.62e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.82 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSPGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILR---------------------KLSK--------KIYSV 256
Cdd:PRK11153 11 FPQGGRTIHALN---NVSLHIPAGEIFGVIGASGAGKSTLIRcinllerptsgrvlvdgqdltALSEkelrkarrQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 257 FQNLDLqFFHETVADEV-------GNDDA---------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDE 320
Cdd:PRK11153 88 FQHFNL-LSSRTVFDNValplelaGTPKAeikarvtelLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2619813829 321 PTTAMDGDGLQNfvkMVELLRE--ERRGL--ILATHDKDVIP-ICDQ 362
Cdd:PRK11153 167 ATSALDPATTRS---ILELLKDinRELGLtiVLITHEMDVVKrICDR 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
212-326 |
1.67e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.97 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLS------------------------KKIYSVFQNLDLqFFHE 267
Cdd:PRK09452 26 GKEVIS---NLDLTINNGEFLTLLGPSGCGKTTVLRLIAgfetpdsgrimldgqdithvpaenRHVNTVFQSYAL-FPHM 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2619813829 268 TVADEVG---------ND-------DALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD 326
Cdd:PRK09452 102 TVFENVAfglrmqktpAAeitprvmEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-200 |
1.78e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.99 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 15 LERDEIVGLVGRNGSGKTTLI---NSI-LCQRHNVFLDDQDFCERKDYSLLSAV---FQDPSSQILATTLEDELRlmshF 87
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLlhlNGIyLPQRGRVKVMGREVNAENEKWVRSKVglvFQDPDDQVFSSTVWDDVA----F 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 88 HHVNFEIGK-----------RLMGPYfstDF-----FKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG------I 145
Cdd:PRK13647 104 GPVNMGLDKdeverrveealKAVRMW---DFrdkppYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGqetlmeI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2619813829 146 KLVLGSIPKGSLISEHRTKHLLNLVQRVYLL-SGDV-REVDKEKLEDQEFLRRNGLR 200
Cdd:PRK13647 181 LDRLHNQGKTVIVATHDVDLAAEWADQVIVLkEGRVlAEGDKSLLTDEDIVEQAGLR 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
247-367 |
1.92e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.49 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 247 RKLSKKIYSVFQNLDLQFFHET---------VADEVGNDDA-------LSLFGLTE-LRERSPFTLSLGQKMRVLIASAY 309
Cdd:PRK13631 112 KELRRRVSMVFQFPEYQLFKDTiekdimfgpVALGVKKSEAkklakfyLNKMGLDDsYLERSPFGLSGGQKRRVAIAGIL 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2619813829 310 ASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKD-VIPICDQIISLS 367
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEhVLEVADEVIVMD 250
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
206-364 |
2.23e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.85 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSPGSEildvqvGLRLKVRGGEVVCLIGKNGVGKTTI---------------------------LRKLSKKIYSVFQ 258
Cdd:PRK13644 11 YPDGTPALE------NINLVIKKGEYIGIIGKNGSGKSTLalhlngllrpqkgkvlvsgidtgdfskLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 259 NLDLQFFHETVADEVG----------------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPT 322
Cdd:PRK13644 85 NPETQFVGRTVEEDLAfgpenlclppieirkrVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2619813829 323 TAMDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQII 364
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
14-138 |
2.68e-11 |
|
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: 61.12 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCERKDYSL---LSAVFQDPsSQILATTLEDELRLMSH 86
Cdd:pfam00005 7 TLNPGEILALVGPNGAGKSTLLKLIAgllsPTEGTILLDGQDLTDDERKSLrkeIGYVFQDP-QLFPRLTVRENLRLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2619813829 87 FHHV-----------------NFEIGKRLMGPYFSTdffkLSDGYRKRFVISSVLSYGPEYLLIDEPLS 138
Cdd:pfam00005 86 LKGLskrekdaraeealeklgLGDLADRPVGERPGT----LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
221-364 |
4.07e-11 |
|
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: 60.86 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTIL--------------------------RKLSKKIYSVFQnlDLQFFHETVADEVg 274
Cdd:cd03228 20 DVSLTIKPGEKVAIVGPSGSGKSTLLklllrlydptsgeilidgvdlrdldlESLRKNIAYVPQ--DPFLFSGTIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 nddalslfgltelrerspftLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGdglQNFVKMVELLREERRG--LILATH 352
Cdd:cd03228 97 --------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP---ETEALILEALRALAKGktVIVIAH 153
|
170
....*....|..
gi 2619813829 353 DKDVIPICDQII 364
Cdd:cd03228 154 RLSTIRDADRII 165
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
210-355 |
5.56e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.54 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 210 SPGSEI----LDvqvGLRLKVRGGEVVCLIGKNGVGKTTI------------------------------LRKLSKKIYS 255
Cdd:PRK13641 13 SPGTPMekkgLD---NISFELEEGSFVALVGHTGSGKSTLmqhfnallkpssgtitiagyhitpetgnknLKKLRKKVSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 256 VFQNLDLQFFHETVADEV---------GNDDA-------LSLFGLTE-LRERSPFTLSLGQKMRVLIASAYASGYKVIGL 318
Cdd:PRK13641 90 VFQFPEAQLFENTVLKDVefgpknfgfSEDEAkekalkwLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2619813829 319 DEPTTAMDGDGLQnfvKMVELLREERRG---LILATHDKD 355
Cdd:PRK13641 170 DEPAAGLDPEGRK---EMMQLFKDYQKAghtVILVTHNMD 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
229-353 |
1.10e-10 |
|
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: 60.77 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 229 GEVVCLIGKNGVGKTTILRKLS------------------------------KKIYSVFQNLDLqFFHETVA-------- 270
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAglekpdggtivlngtvlfdsrkkinlppqqRKIGLVFQQYAL-FPHLNVRenlafglk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 271 ------DEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG---DGLQNFVKmvELLR 341
Cdd:cd03297 102 rkrnreDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRalrLQLLPELK--QIKK 179
|
170
....*....|..
gi 2619813829 342 EERRGLILATHD 353
Cdd:cd03297 180 NLNIPVIFVTHD 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
199-364 |
1.21e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.82 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 199 LRGFQIEYQRGSpgsEILDVQVGLRLKVRGGEVVCLIGKNGVGKTTI------LRKLSKKIYSV---------------- 256
Cdd:PRK10535 7 LKDIRRSYPSGE---EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLmnilgcLDKPTSGTYRVagqdvatldadalaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 257 --------FQNLDLqFFHETVADEV-------GNDDA---------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASG 312
Cdd:PRK10535 84 rrehfgfiFQRYHL-LSHLTAAQNVevpavyaGLERKqrllraqelLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2619813829 313 YKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQII 364
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
221-354 |
1.35e-10 |
|
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: 60.82 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS------------------------KKIYSVFQNLDLqFFHETVADEVG-- 274
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAglerpdsgtilfggedatdvpvqeRNVGFVFQHYAL-FRHMTVFDNVAfg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 ------------------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDglqnfvkm 336
Cdd:cd03296 99 lrvkprserppeaeirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK-------- 170
|
170
....*....|....*...
gi 2619813829 337 velLREERRGLILATHDK 354
Cdd:cd03296 171 ---VRKELRRWLRRLHDE 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
110-362 |
1.55e-10 |
|
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: 62.51 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 110 LSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSIPKGS-------LISEHRTKHLLNLVQR-VYLLSGDVR 181
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkasgismVLTSHWPEVIEDLSDKaIWLENGEIK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 182 EV-------------------DKEKLEDQEFLRRNGLRGFQIEYQRGspgseILDVQVGLRLKVRGGEVVCLIGKNGVGK 242
Cdd:TIGR03269 249 EEgtpdevvavfmegvsevekECEVEVGEPIIKVRNVSKRYISVDRG-----VVKAVDNVSLEVKEGEIFGIVGTSGAGK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 243 TTILRKL---------------------------------SKKIYSVFQNLDLqFFHETV------------ADEVGNDD 277
Cdd:TIGR03269 324 TTLSKIIagvleptsgevnvrvgdewvdmtkpgpdgrgraKRYIGILHQEYDL-YPHRTVldnlteaiglelPDELARMK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 278 A---LSLFGLTELRERS-----PFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREE-RRGLI 348
Cdd:TIGR03269 403 AvitLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFI 482
|
330
....*....|....*
gi 2619813829 349 LATHDKD-VIPICDQ 362
Cdd:TIGR03269 483 IVSHDMDfVLDVCDR 497
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
199-326 |
1.58e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 199 LRGFQIEYQRGspGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIYSVF--------------------- 257
Cdd:PRK13548 3 LEARNLSVRLG--GRTLLD---DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSgevrlngrpladwspaelarr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 258 -----QNLDLQF-F--HETVA----------DEVGN--DDALSLFGLTELRERSPFTLSLGQKMRVLIA------SAYAS 311
Cdd:PRK13548 78 ravlpQHSSLSFpFtvEEVVAmgraphglsrAEDDAlvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlaqlWEPDG 157
|
170
....*....|....*
gi 2619813829 312 GYKVIGLDEPTTAMD 326
Cdd:PRK13548 158 PPRWLLLDEPTSALD 172
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
224-364 |
1.63e-10 |
|
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: 60.82 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLS-------------------KKIYSV--------FQNLDLqFFHETVADevgN- 275
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITgfyrptsgrilfdgrditgLPPHRIarlgiartFQNPRL-FPELTVLE---Nv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 ---------------------------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPT 322
Cdd:COG0411 101 lvaaharlgrgllaallrlprarreereareraEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2619813829 323 TAMDGDGLQNFVKMVELLREER-RGLILATHDKDVI-PICDQII 364
Cdd:COG0411 181 AGLNPEETEELAELIRRLRDERgITILLIEHDMDLVmGLADRIV 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
224-367 |
1.69e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 61.64 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILR-----------KLS-------------KKIYSVFQNLDLqFFHETVADEVG----- 274
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRiiaglehqtsgHIRfhgtdvsrlhardRKVGFVFQHYAL-FRHMTVFDNIAfgltv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 -------NDDA--------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVEL 339
Cdd:PRK10851 102 lprrerpNAAAikakvtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQ 181
|
170 180 190
....*....|....*....|....*....|
gi 2619813829 340 LREERR-GLILATHDK-DVIPICDQIISLS 367
Cdd:PRK10851 182 LHEELKfTSVFVTHDQeEAMEVADRVVVMS 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
224-363 |
1.96e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.25 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTI-----------------------------LRKLSKKIYSVFQNLDLqfFHE-TVADEV 273
Cdd:COG1135 26 LTIEKGEIFGIIGYSGAGKSTLircinllerptsgsvlvdgvdltalsereLRAARRKIGMIFQHFNL--LSSrTVAENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 274 -------GNDDA---------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNfvkMV 337
Cdd:COG1135 104 alpleiaGVPKAeirkrvaelLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRS---IL 180
|
170 180 190
....*....|....*....|....*....|.
gi 2619813829 338 ELLRE--ERRGL--ILATHDKDVI-PICDQI 363
Cdd:COG1135 181 DLLKDinRELGLtiVLITHEMDVVrRICDRV 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-141 |
2.18e-10 |
|
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: 60.21 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILcqRHN------VFLDDQDFCERKDYSL------LSAVFQDPSS---------QI 72
Cdd:cd03257 27 SIKKGETLGLVGESGSGKSTLARAIL--GLLkptsgsIIFDGKDLLKLSRRLRkirrkeIQMVFQDPMSslnprmtigEQ 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2619813829 73 LATTLEdelrlmSHFHHVNFEIGKRLMGPYF-----STDFFK-----LSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:cd03257 105 IAEPLR------IHGKLSKKEARKEAVLLLLvgvglPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-176 |
2.31e-10 |
|
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: 58.93 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCERKDYSL---LSAVFQDPssQILATTLEDELrlmsh 86
Cdd:cd03228 24 TIKPGEKVAIVGPSGSGKSTLLKLLLrlydPTSGEILIDGVDLRDLDLESLrknIAYVPQDP--FLFSGTIRENI----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 87 fhhvnfeigkrlmgpyfstdffkLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG---IKLVLGSIPKGS---LISe 160
Cdd:cd03228 97 -----------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETealILEALRALAKGKtviVIA- 152
|
170
....*....|....*.
gi 2619813829 161 HRtKHLLNLVQRVYLL 176
Cdd:cd03228 153 HR-LSTIRDADRIIVL 167
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
215-366 |
2.59e-10 |
|
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: 59.82 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 215 ILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILR-----------------------------KLSKKIYSVFQNLDLqFF 265
Cdd:cd03261 15 VLK---GVDLDVRRGEILAIIGPSGSGKSTLLRlivgllrpdsgevlidgedisglseaelyRLRRRMGMLFQSGAL-FD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 HETVADEVG-------NDDA----------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD 328
Cdd:cd03261 91 SLTVFENVAfplrehtRLSEeeireivlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2619813829 329 GLQNFVKMVELLREErRGL--ILATHDKD-VIPICDQIISL 366
Cdd:cd03261 171 ASGVIDDLIRSLKKE-LGLtsIMVTHDLDtAFAIADRIAVL 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-200 |
2.90e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 15 LERDEIVGLVGRNGSGKTTL---INSILCQRHNVFLDDQDFCERKDYSLLSA------VFQDPSSQILATTLEDELRlms 85
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLflhFNGILKPTSGEVLIKGEPIKYDKKSLLEVrktvgiVFQNPDDQLFAPTVEEDVA--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 86 hFHHVNF-----EIGKRL--------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG----IKLV 148
Cdd:PRK13639 102 -FGPLNLglskeEVEKRVkealkavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGasqiMKLL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2619813829 149 LGSIPKGS--LISEHRTKHLLNLVQRVYLLSGD--VRE-VDKEKLEDQEFLRRNGLR 200
Cdd:PRK13639 181 YDLNKEGItiIISTHDVDLVPVYADKVYVMSDGkiIKEgTPKEVFSDIETIRKANLR 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-176 |
3.26e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 7 PYLPG-KVELERDEIVGLVGRNGSGKTTL---INSILCQRHNVFL---DDQDFCERKDYSL---LSAVFQDPSSQILATT 76
Cdd:PRK13638 15 PVLKGlNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLRPQKGAVLwqgKPLDYSKRGLLALrqqVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 77 LEDELRL-MSHFHHVNFEIGKRLMGPYFSTD--FFK------LSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG--- 144
Cdd:PRK13638 95 IDSDIAFsLRNLGVPEAEITRRVDEALTLVDaqHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGrtq 174
|
170 180 190
....*....|....*....|....*....|....*
gi 2619813829 145 -IKLVLGSIPKGS--LISEHRTKHLLNLVQRVYLL 176
Cdd:PRK13638 175 mIAIIRRIVAQGNhvIISSHDIDLIYEISDAVYVL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-141 |
3.65e-10 |
|
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: 58.60 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCE--RKDYSLLSAVfqdpSSQILATTledelrLMSH 86
Cdd:cd03214 20 LSIEAGEIVGILGPNGAGKSTLLKTLAgllkPSSGEILLDGKDLASlsPKELARKIAY----VPQALELL------GLAH 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2619813829 87 FHHVNFEigkrlmgpyfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:cd03214 90 LADRPFN---------------ELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
221-352 |
3.94e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS-----------------------------------KKIYSVFQNLDL-QF 264
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAgllppaagtikldggdiddpdvaeachylghrnamKPALTVAENLEFwAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 265 FHETvaDEVGNDDALSLFGLTELRERsPF-TLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGlqnfVKMV-ELLRE 342
Cdd:PRK13539 100 FLGG--EELDIAAALEAVGLAPLAHL-PFgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA----VALFaELIRA 172
|
170
....*....|...
gi 2619813829 343 ERRG---LILATH 352
Cdd:PRK13539 173 HLAQggiVIAATH 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
221-353 |
8.17e-10 |
|
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: 58.35 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR---------------------------------KLSKKIYSVFQNLDLqfFHE 267
Cdd:cd03260 18 DISLDIPKGEITALIGPSGCGKSTLLRllnrlndlipgapdegevlldgkdiydldvdvlELRRRVGMVFQKPNP--FPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 268 TVADEV----------GND-------DALSLFGLTE--LRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGd 328
Cdd:cd03260 96 SIYDNVayglrlhgikLKEelderveEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP- 174
|
170 180
....*....|....*....|....*..
gi 2619813829 329 glQNFVKMVELLRE--ERRGLILATHD 353
Cdd:cd03260 175 --ISTAKIEELIAElkKEYTIVIVTHN 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
229-357 |
8.29e-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: 56.61 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 229 GEVVCLIGKNGVGKTTILRKLSkkiysvfQNLDLQFFHETVADEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASA 308
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA-------RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2619813829 309 YASGYKVIGLDEPTTAMDGDGLQNFVKMVEL------LREERRGLILATHDKDVI 357
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllKSEKNLTVILTTNDEKDL 129
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-364 |
1.60e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.31 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSILCQRH----NVFLD--------DQDFCERKDYSLLSAVFQD--PSSQILA---- 74
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEpdsgEVSIPkglrigylPQEPPLDDDLTVLDTVLDGdaELRALEAelee 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 75 -----TTLEDELRLMSHFHHVNFEIG--------KRLM------GPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDE 135
Cdd:COG0488 99 leaklAEPDEDLERLAELQEEFEALGgweaearaEEILsglgfpEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 136 PLSNLDDEGI----KLVLGSipKGSL--ISEHRtkHLLNLV---------QRVYLLSGD-------------VREVDKEK 187
Cdd:COG0488 179 PTNHLDLESIewleEFLKNY--PGTVlvVSHDR--YFLDRVatrileldrGKLTLYPGNysayleqraerleQEAAAYAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 188 LED-----QEFLRRNGLRG-------------------------------FQIEYQRGSPGSEILDVQVG---------L 222
Cdd:COG0488 255 QQKkiakeEEFIRRFRAKArkakqaqsrikaleklereepprrdktveirFPPPERLGKKVLELEGLSKSygdktllddL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 223 RLKVRGGEVVCLIGKNGVGKTTILRKLSKKI------YSVFQNLDLQFF---------HETVADEV--GNDDA------- 278
Cdd:COG0488 335 SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELepdsgtVKLGETVKIGYFdqhqeeldpDKTVLDELrdGAPGGteqevrg 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 279 -LSLFGLTELRERSPF-TLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD-------GDGLQNFvkmvellreerRG-LI 348
Cdd:COG0488 415 yLGRFLFSGDDAFKPVgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDietlealEEALDDF-----------PGtVL 483
|
490
....*....|....*..
gi 2619813829 349 LATHDKDVIP-ICDQII 364
Cdd:COG0488 484 LVSHDRYFLDrVATRIL 500
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-141 |
2.03e-09 |
|
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: 57.36 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSILCQRH----NVFLDDQDFCE--RKDYS-LLSAVFQDPSSQILATTLedELRLMS 85
Cdd:COG1120 22 LSLPPGEVTALLGPNGSGKSTLLRALAGLLKpssgEVLLDGRDLASlsRRELArRIAYVPQEPPAPFGLTVR--ELVALG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 86 HFHHVNF---------EIGKRLM-----GPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:COG1120 100 RYPHLGLfgrpsaedrEAVEEALertglEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
212-364 |
2.08e-09 |
|
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: 57.30 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILR-----------------------------KLSKKI--------- 253
Cdd:COG1127 17 DRVVLD---GVSLDVPRGEILAIIGGSGSGKSVLLKliigllrpdsgeilvdgqditglsekelyELRRRIgmlfqggal 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 254 ---YSVFQNLDL---QFFH---ETVADEVgnDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTA 324
Cdd:COG1127 94 fdsLTVFENVAFplrEHTDlseAEIRELV--LEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2619813829 325 MDGDGLQNFvkmVELLREERRGL----ILATHDKD-VIPICDQII 364
Cdd:COG1127 172 LDPITSAVI---DELIRELRDELgltsVVVTHDLDsAFAIADRVA 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-180 |
2.21e-09 |
|
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: 56.77 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSILCQ----RHNVFLDDQDFceRKDYSLLSAVFQ----DPSSQILAttleDELRLM 84
Cdd:cd03235 20 FEVKPGEFLAIVGPNGAGKSTLLKAILGLlkptSGSIRVFGKPL--EKERKRIGYVPQrrsiDRDFPISV----RDVVLM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 85 SHFHHVNF----------------------EIGKRLMGpyfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDD 142
Cdd:cd03235 94 GLYGHKGLfrrlskadkakvdealervglsELADRQIG--------ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2619813829 143 EGIKLVLGSIP------KGSLISEHRTKHLLNLVQRVYLLSGDV 180
Cdd:cd03235 166 KTQEDIYELLRelrregMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
224-363 |
2.23e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLS---------------------------KKIYSVFQNLDLqFFHETVAD----- 271
Cdd:COG1129 25 LELRPGEVHALLGENGAGKSTLMKILSgvyqpdsgeilldgepvrfrsprdaqaAGIAIIHQELNL-VPNLSVAEniflg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 272 -EVGN-------------DDALSLFGLtELRERSP-FTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKM 336
Cdd:COG1129 104 rEPRRgglidwramrrraRELLARLGL-DIDPDTPvGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRI 182
|
170 180
....*....|....*....|....*...
gi 2619813829 337 VELLREERRGLILATHD-KDVIPICDQI 363
Cdd:COG1129 183 IRRLKAQGVAIIYISHRlDEVFEIADRV 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
206-364 |
2.35e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 206 YQRGSPGS-EILDvqvGLRLKVRGGEVVCLIGKNGVGKTTI------------------------------LRKLSKKIY 254
Cdd:PRK13646 12 YQKGTPYEhQAIH---DVNTEFEQGKYYAIVGQTGSGKSTLiqninallkpttgtvtvdditithktkdkyIRPVRKRIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 255 SVFQNLDLQFFHETVA--------------DEVGND--DALSLFGLT-ELRERSPFTLSLGQKMRVLIASAYASGYKVIG 317
Cdd:PRK13646 89 MVFQFPESQLFEDTVEreiifgpknfkmnlDEVKNYahRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2619813829 318 LDEPTTAMDGDGLQNFVKMVELLR-EERRGLILATHD-KDVIPICDQII 364
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVI 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-154 |
2.47e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.69 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 15 LERDEIVGLVGRNGSGKTTL---INSIL-CQRHNVFLDDQDFCerkDYS-------LLSAVFQDPSSQILATTLEDELRl 83
Cdd:PRK13644 25 IKKGEYIGIIGKNGSGKSTLalhLNGLLrPQKGKVLVSGIDTG---DFSklqgirkLVGIVFQNPETQFVGRTVEEDLA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 84 mshFHHVNF-----EIGKRL--------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLG 150
Cdd:PRK13644 101 ---FGPENLclppiEIRKRVdralaeigLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
....
gi 2619813829 151 SIPK 154
Cdd:PRK13644 178 RIKK 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
217-353 |
2.71e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 217 DVQVGLRLKVRGGEVVCLIGKNGVGKTTILR---------------------------------------KLSKKIYSVF 257
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRcinflekpsegsivvngqtinlvrdkdgqlkvadknqlrLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 258 QNLDLqFFHETVADEVgNDDALSLFGLT--ELRERS-----------------PFTLSLGQKMRVLIASAYASGYKVIGL 318
Cdd:PRK10619 99 QHFNL-WSHMTVLENV-MEAPIQVLGLSkqEARERAvkylakvgideraqgkyPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190
....*....|....*....|....*....|....*
gi 2619813829 319 DEPTTAMDGDGLQNFVKMVELLREERRGLILATHD 353
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
221-352 |
3.31e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS--------------KKIYSV----FQNL-----------------DLQFF 265
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAglarpdagevlwqgEPIRRQrdeyHQDLlylghqpgikteltaleNLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 HEtVADEVGND---DALSLFGLTElRERSPF-TLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGlqnfVKMVE-LL 340
Cdd:PRK13538 99 QR-LHGPGDDEalwEALAQVGLAG-FEDVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG----VARLEaLL 172
|
170
....*....|....*
gi 2619813829 341 RE--ERRGL-ILATH 352
Cdd:PRK13538 173 AQhaEQGGMvILTTH 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-177 |
4.94e-09 |
|
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: 56.01 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCE-------RKDYSLL---SAVFQDpssqilaTTLE 78
Cdd:cd03218 21 LSVKQGEIVGLLGPNGAGKTTTFYMIVglvkPDSGKILLDGQDITKlpmhkraRLGIGYLpqeASIFRK-------LTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 79 DELRLMSHFHHVNF-EIGKRLmgPYFSTDF----------FKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKL 147
Cdd:cd03218 94 ENILAVLEIRGLSKkEREEKL--EELLEEFhithlrkskaSSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQD 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 2619813829 148 VLGSIPK------GSLISEHRTKHLLNLVQRVYLLS 177
Cdd:cd03218 172 IQKIIKIlkdrgiGVLITDHNVRETLSITDRAYIIY 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
221-357 |
5.17e-09 |
|
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: 55.88 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILR-----------------------------KLSKKIYSVFQNLDLqFFHETVAD 271
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKliykeelptsgtirvngqdvsdlrgraipYLRRKIGVVFQDFRL-LPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 272 EV----------GND------DALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDglqNFVK 335
Cdd:cd03292 98 NVafalevtgvpPREirkrvpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD---TTWE 174
|
170 180
....*....|....*....|....*
gi 2619813829 336 MVELLRE-ERRG--LILATHDKDVI 357
Cdd:cd03292 175 IMNLLKKiNKAGttVVVATHAKELV 199
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
221-367 |
5.72e-09 |
|
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: 55.80 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS-------------------------KKIYSVF------------------ 257
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSgllqptsgevrvaglvpwkrrkkflRRIGVVFgqktqlwwdlpvidsfyl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 258 ----QNLDLQFFHETVadevgndDALS-LFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD---GDG 329
Cdd:cd03267 119 laaiYDLPPARFKKRL-------DELSeLLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvvaQEN 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 2619813829 330 LQNFVKmvELLREERRGLILATHD-KDVIPICDQIISLS 367
Cdd:cd03267 192 IRNFLK--EYNRERGTTVLLTSHYmKDIEALARRVLVID 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-179 |
6.78e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 53.99 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILCQrhnvflddqdfcerkdysllsavfQDPSSQILAttledelrlmshfHHVNFE 93
Cdd:cd03221 22 TINPGDRIGLVGRNGAGKSTLLKLIAGE------------------------LEPDEGIVT-------------WGSTVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 94 IGkrlmgpYFStdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLV---LGSIPKGSLISEHRTKHLLNLV 170
Cdd:cd03221 65 IG------YFE----QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALeeaLKEYPGTVILVSHDRYFLDQVA 134
|
....*....
gi 2619813829 171 QRVYLLSGD 179
Cdd:cd03221 135 TKIIELEDG 143
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
221-363 |
7.50e-09 |
|
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: 55.45 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS-------------------------KKIYSVFQNLDLQ---------FFH 266
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTtllkptsgratvaghdvvreprevrRRIGIVFQDLSVDdeltgwenlYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 267 ETVADEVGN------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD---GDGLQNFVKmv 337
Cdd:cd03265 98 ARLYGVPGAerreriDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDpqtRAHVWEYIE-- 175
|
170 180
....*....|....*....|....*..
gi 2619813829 338 ELLREERRGLILATHDKD-VIPICDQI 363
Cdd:cd03265 176 KLKEEFGMTILLTTHYMEeAEQLCDRV 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
224-355 |
8.18e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.77 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLS------------------------KKIYSVFQNLDLqFFHETV---------- 269
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAgfeqptagqimldgvdlshvppyqRPINMMFQSYAL-FPHMTVeqniafglkq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 270 ----ADEVGN--DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG---DGLQnfVKMVELL 340
Cdd:PRK11607 119 dklpKAEIASrvNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrDRMQ--LEVVDIL 196
|
170
....*....|....*..
gi 2619813829 341 reERRGL--ILATHDKD 355
Cdd:PRK11607 197 --ERVGVtcVMVTHDQE 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
276-361 |
1.16e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.66 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHD-K 354
Cdd:PRK15056 124 TAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNlG 203
|
....*..
gi 2619813829 355 DVIPICD 361
Cdd:PRK15056 204 SVTEFCD 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-162 |
1.43e-08 |
|
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: 54.41 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLIN-----------SILCQRHNVFLDDQDFCERkdyslLSAVFQDPSsQILATTLEDELR 82
Cdd:COG4133 24 TLAAGEALALTGPNGSGKTTLLRilagllppsagEVLWNGEPIRDAREDYRRR-----LAYLGHADG-LKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 83 LMSHFHHVNFEIGKRL-------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGsipkg 155
Cdd:COG4133 98 FWAALYGLRADREAIDealeavgLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAE----- 172
|
....*..
gi 2619813829 156 sLISEHR 162
Cdd:COG4133 173 -LIAAHL 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
212-345 |
2.25e-08 |
|
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: 53.98 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSK--KIYS---VFQNLDL--------------------QFFH 266
Cdd:cd03224 12 KSQILF---GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPRSgsiRFDGRDItglppheraragigyvpegrRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 267 E-TVAD--EVGN------------DDALSLF-GLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTamdgdGL 330
Cdd:cd03224 89 ElTVEEnlLLGAyarrrakrkarlERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE-----GL 163
|
170
....*....|....*..
gi 2619813829 331 Q-NFVKMV-ELLREERR 345
Cdd:cd03224 164 ApKIVEEIfEAIRELRD 180
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
221-364 |
2.33e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.09 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTT-------IL------------------RKLSKKIYSVF---QNL--DLqffheTVA 270
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTtikmltgILvptsgevrvlgyvpfkrrKEFARRIGVVFgqrSQLwwDL-----PAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 271 D---------EVGND------DALS-LFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD---GDGLQ 331
Cdd:COG4586 115 DsfrllkaiyRIPDAeykkrlDELVeLLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvsKEAIR 194
|
170 180 190
....*....|....*....|....*....|....
gi 2619813829 332 NFVKmvELLREERRGLILATHD-KDVIPICDQII 364
Cdd:COG4586 195 EFLK--EYNRERGTTILLTSHDmDDIEALCDRVI 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
224-352 |
2.34e-08 |
|
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: 53.65 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLS------------------------KKIYSVFQNLDLqFFHETVADEVG----- 274
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAgfetpqsgrvlingvdvtaappadRPVSMLFQENNL-FAHLTVEQNVGlglsp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 -----------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDG---DGLQNFVkmVELL 340
Cdd:cd03298 98 glkltaedrqaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPalrAEMLDLV--LDLH 175
|
170
....*....|..
gi 2619813829 341 REERRGLILATH 352
Cdd:cd03298 176 AETKMTVLMVTH 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
224-362 |
3.21e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTT--------------------------------------------ILRKLSkkiysVFQN 259
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTtfymvvgivprdagniiiddedisllplhararrgigylpqeasIFRRLS-----VYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 260 LD--LQFFHETVADEVGN--DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVK 335
Cdd:PRK10895 99 LMavLQIRDDLSAEQREDraNELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180
....*....|....*....|....*...
gi 2619813829 336 MVELLREERRGLILATHD-KDVIPICDQ 362
Cdd:PRK10895 179 IIEHLRDSGLGVLITDHNvRETLAVCER 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-152 |
3.78e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.87 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINS----ILCQRHNVFLDDQDFCE------RKDYSLlsaVFQDPSSQILATTLEDEL- 81
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLlnglLLPEAGTITVGGMVLSEetvwdvRRQVGM---VFQNPDNQFVGATVQDDVa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 82 ---------------RLMSHFHHVNfeigkrlMGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIK 146
Cdd:PRK13635 105 fglenigvpreemveRVDQALRQVG-------MEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
....*.
gi 2619813829 147 LVLGSI 152
Cdd:PRK13635 178 EVLETV 183
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
221-366 |
3.87e-08 |
|
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: 53.05 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIYS-----VFQNLDLQFFH----------------ETVADEV------ 273
Cdd:cd03269 18 DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdsgevLFDGKPLDIAArnrigylpeerglypkMKVIDQLvylaql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 274 ----------GNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREE 343
Cdd:cd03269 98 kglkkeearrRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA 177
|
170 180
....*....|....*....|....
gi 2619813829 344 RRGLILATHDKD-VIPICDQIISL 366
Cdd:cd03269 178 GKTVILSTHQMElVEELCDRVLLL 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-141 |
4.38e-08 |
|
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: 52.57 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 15 LERDEIVGLVGRNGSGKTTLINSILC----QRHNVFLDDQDFCERKDYSL-----LSAVFQDPSsqilattledelrLMS 85
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCIAGleepDSGSILIDGEDLTDLEDELPplrrrIGMVFQDFA-------------LFP 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2619813829 86 HfhhvnFEIGKRLMgpyfstdfFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:cd03229 90 H-----LTVLENIA--------LGLSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-176 |
5.83e-08 |
|
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: 54.45 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 19 EIVGLVGRNGSGKTTLINsILC-----QRHNVFLDDQDfceRKDYSL------LSAVFQDPssQILATTLEDELRL---- 83
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLK-LLLglyepTSGRILIDGID---LRQIDPaslrrqIGVVLQDV--FLFSGTIRENITLgdpd 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 84 -----------MSHFHHvnfEIGKRLMGpyFST----DFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLV 148
Cdd:COG2274 576 atdeeiieaarLAGLHD---FIEALPMG--YDTvvgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII 650
|
170 180 190
....*....|....*....|....*....|...
gi 2619813829 149 LGSI-----PKGSLISEHRTkHLLNLVQRVYLL 176
Cdd:COG2274 651 LENLrrllkGRTVIIIAHRL-STIRLADRIIVL 682
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-154 |
6.04e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.27 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 23 LVGRNGSGKTT---LINSILCQRHN----VFLDDQDFCERKDYSL---LSAVFQDPSSQILATTLEDEL----------- 81
Cdd:PRK13640 38 LIGHNGSGKSTiskLINGLLLPDDNpnskITVDGITLTAKTVWDIrekVGIVFQNPDNQFVGATVGDDVafglenravpr 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 82 -RLMSHFHHVNFEIGkrlMGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSIPK 154
Cdd:PRK13640 118 pEMIKIVRDVLADVG---MLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRK 188
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
224-361 |
7.71e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 52.72 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTT-------ILRKLSKKIY--------------------------SVFQNLdlqffheTVA 270
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTtfymivgLVKPDSGRIFldgedithlpmhkrarlgigylpqeaSIFRKL-------TVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 271 D------EVGNDDA----------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD----GDgL 330
Cdd:COG1137 97 DnilavlELRKLSKkereerleelLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavAD-I 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2619813829 331 QnfvKMVELLREerRGL-ILAThDKDV---IPICD 361
Cdd:COG1137 176 Q---KIIRHLKE--RGIgVLIT-DHNVretLGICD 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-183 |
7.74e-08 |
|
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: 52.44 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILCQ----RHNVFLDDQDFCERKDYSL----LSAVFQDPssQILAT-TLEDELRLM 84
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFlrptSGSVLFDGEDITGLPPHEIarlgIGRTFQIP--RLFPElTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 85 SHFHHVNFEIGKRLMGPYFST--------DFFKLSDgyrKRFVISSVLSYG--------------PEYLLIDEPLSNLDD 142
Cdd:cd03219 100 AQARTGSGLLLARARREEREAreraeellERVGLAD---LADRPAGELSYGqqrrleiaralatdPKLLLLDEPAAGLNP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 143 E---GIKLVLGSIPKGS---LISEHRTKHLLNLVQRVYLL-------SGDVREV 183
Cdd:cd03219 177 EeteELAELIRELRERGitvLLVEHDMDVVMSLADRVTVLdqgrviaEGTPDEV 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-162 |
8.87e-08 |
|
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: 52.23 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 19 EIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCERKDYSL---LSAVFQDPSsqILATTLEDELRLMS------ 85
Cdd:cd03254 30 ETVAIVGPTGAGKTTLINLLMrfydPQKGQILIDGIDIRDISRKSLrsmIGVVLQDTF--LFSGTIMENIRLGRpnatde 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 86 ---------HFHHvnfeIGKRL-------MGPYFSTdffkLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLV- 148
Cdd:cd03254 108 evieaakeaGAHD----FIMKLpngydtvLGENGGN----LSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIq 179
|
170
....*....|....*...
gi 2619813829 149 --LGSIPKG--SLISEHR 162
Cdd:cd03254 180 eaLEKLMKGrtSIIIAHR 197
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
199-353 |
8.99e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 199 LRGFQIEYQRGSpgseiLDVQVGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIYSVFQNLDL------QFFHETVA-- 270
Cdd:PRK10253 8 LRGEQLTLGYGK-----YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqHYASKEVArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 271 -------------------------------------DEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGY 313
Cdd:PRK10253 83 igllaqnattpgditvqelvargryphqplftrwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2619813829 314 KVIGLDEPTTAMDgdgLQNFVKMVELLREERR--GLILAT--HD 353
Cdd:PRK10253 163 AIMLLDEPTTWLD---ISHQIDLLELLSELNRekGYTLAAvlHD 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
211-363 |
9.33e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLS------------KKIYSVFQNL-------------DLQFF 265
Cdd:PRK11288 15 PGVKALD---DISFDCRAGQVHALMGENGAGKSTLLKILSgnyqpdagsiliDGQEMRFASTtaalaagvaiiyqELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 266 HE-TVADE-----------VGNDDALSLFGLTELRER----SPFT----LSLGQKMRVLIASAYASGYKVIGLDEPTTAM 325
Cdd:PRK11288 92 PEmTVAENlylgqlphkggIVNRRLLNYEAREQLEHLgvdiDPDTplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 2619813829 326 DGDGLQNFVKMVELLREERRGLILATHDKDVI-PICDQI 363
Cdd:PRK11288 172 SAREIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAI 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
229-356 |
1.06e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 229 GEVVCLIGKNGVGKTTILR--------------------------------KLSKKIYSVFQNLDLqFFHETV------- 269
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRvlnllemprsgtlniagnhfdfsktpsdkairELRRNVGMVFQQYNL-WPHLTVqqnliea 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 270 -------ADEVGNDDALSLFG---LTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVEL 339
Cdd:PRK11124 107 pcrvlglSKDQALARAEKLLErlrLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE 186
|
170
....*....|....*..
gi 2619813829 340 LREERRGLILATHDKDV 356
Cdd:PRK11124 187 LAETGITQVIVTHEVEV 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-141 |
1.13e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTT-------LINSilcqRHNVFLDDQDFCERKDYSLL------SAVFQDPSS---------Q 71
Cdd:PRK15134 308 TLRPGETLGLVGESGSGKSTtglallrLINS----QGEIWFDGQPLHNLNRRQLLpvrhriQVVFQDPNSslnprlnvlQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 72 ILATTL----------EDELRLMSHFHHVNFEIGKRLMGPyfsTDFfklSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:PRK15134 384 IIEEGLrvhqptlsaaQREQQVIAVMEEVGLDPETRHRYP---AEF---SGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-141 |
1.26e-07 |
|
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: 51.80 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINsiLCQRHN-----------VFLDDQDFCERkDYSLLSA------VFQDPSsqILAT 75
Cdd:cd03260 21 LDIPKGEITALIGPSGCGKSTLLR--LLNRLNdlipgapdegeVLLDGKDIYDL-DVDVLELrrrvgmVFQKPN--PFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 76 TLEDelrlmshfhhvNFEIGKRLMG---------------------PYFS--TDFFKLSDGYRKRFVISSVLSYGPEYLL 132
Cdd:cd03260 96 SIYD-----------NVAYGLRLHGiklkeelderveealrkaalwDEVKdrLHALGLSGGQQQRLCLARALANEPEVLL 164
|
....*....
gi 2619813829 133 IDEPLSNLD 141
Cdd:cd03260 165 LDEPTSALD 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
221-352 |
1.32e-07 |
|
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: 51.45 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS-----------------KKIYSVFQN----LDLQFF--HETVADEVGN-- 275
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILglikpdsgeitfdgksyQKNIEALRRigalIEAPGFypNLTARENLRLla 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 ----------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERR 345
Cdd:cd03268 98 rllgirkkriDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGI 177
|
....*..
gi 2619813829 346 GLILATH 352
Cdd:cd03268 178 TVLISSH 184
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
221-353 |
1.66e-07 |
|
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: 51.49 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKL-------SKKIY-----------------SVFQNLDLqFFHETVADEVGN- 275
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIagleeptSGRIYiggrdvtdlppkdrdiaMVFQNYAL-YPHMTVYDNIAFg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 ---------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD-GLQNFVKMVEL 339
Cdd:cd03301 97 lklrkvpkdeidervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKlRVQMRAELKRL 176
|
170
....*....|....
gi 2619813829 340 LREERRGLILATHD 353
Cdd:cd03301 177 QQRLGTTTIYVTHD 190
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
221-366 |
2.35e-07 |
|
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: 50.29 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKL-------SKKIYsvFQNLDLQFFHET-VADEVG---NDDalSLFGLTeLRE 289
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLIlgllrptSGRVR--LDGADISQWDPNeLGDHVGylpQDD--ELFSGS-IAE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2619813829 290 RspfTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQIISL 366
Cdd:cd03246 95 N---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
229-366 |
2.56e-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: 50.01 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 229 GEVVCLIGKNGVGKTTILRKLSKKIYSVFQNLDLQFFHETVADEVGNDDALSLFGLTELR-ERSPFTLSLGQKMRVLIAS 307
Cdd:cd03238 21 NVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGYLTlGQKLSTLSGGELQRVKLAS 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2619813829 308 AYASGYK--VIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQIISL 366
Cdd:cd03238 101 ELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
203-366 |
3.04e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.99 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 203 QIEYQRGspGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLS---------------KKIYSVFQNLDLqFFHE 267
Cdd:COG0488 3 NLSKSFG--GRPLLD---DVSLSINPGDRIGLVGRNGAGKSTLLKILAgelepdsgevsipkgLRIGYLPQEPPL-DDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 268 TVADEVGNDDA------------------------------------------------LSLFGLTELRERSPF-TLSLG 298
Cdd:COG0488 77 TVLDTVLDGDAelraleaeleeleaklaepdedlerlaelqeefealggweaearaeeiLSGLGFPEEDLDRPVsELSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2619813829 299 QKMRVLIASAYASGYKVIGLDEPTTAMDGDG---LQNFvkmvelLREERRGLILATHDKDVI-PICDQIISL 366
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESiewLEEF------LKNYPGTVLVVSHDRYFLdRVATRILEL 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
224-367 |
3.14e-07 |
|
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: 50.64 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILR-----------------------------KLSKKIYSVFQNLDL------------ 262
Cdd:cd03256 22 LSINPGEFVALIGPSGAGKSTLLRclnglveptsgsvlidgtdinklkgkalrQLRRQIGMIFQQFNLierlsvlenvls 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 263 -------------QFFHEtvADEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGdg 329
Cdd:cd03256 102 grlgrrstwrslfGLFPK--EEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDP-- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2619813829 330 lQNFVKMVELLRE--ERRGL--ILATHDKDVI-PICDQIISLS 367
Cdd:cd03256 178 -ASSRQVMDLLKRinREEGItvIVSLHQVDLArEYADRIVGLK 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-177 |
5.06e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.28 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 19 EIVGLVGRNGSGKTTLINSI--LCQRH--NVFLDDQD-----------------------FCERKDYSLLSAVFQDPSSQ 71
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVvgIVPRDagNIIIDDEDisllplhararrgigylpqeasiFRRLSVYDNLMAVLQIRDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 72 ILATTLEDELRLMSHFH--HVNFEIGKRLMGpyfstdffklsdGYRKRFVISSVLSYGPEYLLIDE------PLSNLDDE 143
Cdd:PRK10895 110 SAEQREDRANELMEEFHieHLRDSMGQSLSG------------GERRRVEIARALAANPKFILLDEpfagvdPISVIDIK 177
|
170 180 190
....*....|....*....|....*....|....
gi 2619813829 144 GIKLVLGSIPKGSLISEHRTKHLLNLVQRVYLLS 177
Cdd:PRK10895 178 RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVS 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
277-366 |
5.17e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.02 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 277 DALSLFGLTELRERSpFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD---GDGLQNfVKMVELLREERRGLILATHD 353
Cdd:cd03290 124 DLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALDihlSDHLMQ-EGILKFLQDDKRTLVLVTHK 201
|
90
....*....|...
gi 2619813829 354 KDVIPICDQIISL 366
Cdd:cd03290 202 LQYLPHADWIIAM 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-173 |
6.19e-07 |
|
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: 49.51 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 19 EIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCE------RKDYSLLSavfQDPS-------SQI-LATTLEDE 80
Cdd:cd03245 31 EKVAIIGRVGSGKSTLLKLLAglykPTSGSVLLDGTDIRQldpadlRRNIGYVP---QDVTlfygtlrDNItLGAPLADD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 81 LRLMS-------------HFHHVNFEIGKRLMGpyfstdffkLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKL 147
Cdd:cd03245 108 ERILRaaelagvtdfvnkHPNGLDLQIGERGRG---------LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180 190
....*....|....*....|....*....|.
gi 2619813829 148 VLGSI-----PKGSLISEHRTKhLLNLVQRV 173
Cdd:cd03245 179 LKERLrqllgDKTLIIITHRPS-LLDLVDRI 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-146 |
6.67e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.21 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLIN------------------SILCQRHNVFLDDQdfceRKDYSLlsaVFQDPSSQILA- 74
Cdd:PRK13641 29 ELEEGSFVALVGHTGSGKSTLMQhfnallkpssgtitiagyHITPETGNKNLKKL----RKKVSL---VFQFPEAQLFEn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 75 TTLEDelrlmSHFHHVNFEIG---------KRLMGPYFSTDF-----FKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNL 140
Cdd:PRK13641 102 TVLKD-----VEFGPKNFGFSedeakekalKWLKKVGLSEDLiskspFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
....*.
gi 2619813829 141 DDEGIK 146
Cdd:PRK13641 177 DPEGRK 182
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-222 |
7.39e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.23 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTL---INSIL-CQRHNVFLDDQ--DFCERKDYSLLSA---VFQDPSSQILATTL------ 77
Cdd:PRK13636 27 INIKKGEVTAILGGNGAGKSTLfqnLNGILkPSSGRILFDGKpiDYSRKGLMKLRESvgmVFQDPDNQLFSASVyqdvsf 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 78 --------EDELRlmshfHHVNFEIGKRLMGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGI---- 145
Cdd:PRK13636 107 gavnlklpEDEVR-----KRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVseim 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 146 KLVLgSIPKGSLISEHRTKHLLNLV----QRVYLLS-------GDVREVdkekledqeFLRRNGLRGFQIEYQRGSPGSE 214
Cdd:PRK13636 182 KLLV-EMQKELGLTIIIATHDIDIVplycDNVFVMKegrvilqGNPKEV---------FAEKEMLRKVNLRLPRIGHLME 251
|
....*...
gi 2619813829 215 ILDVQVGL 222
Cdd:PRK13636 252 ILKEKDGF 259
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-173 |
8.90e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.75 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 23 LVGRNGSGKTTLIN-----------SILCQRHNVflDDQDFCE-RKDYSLlsaVFQDPSSQILATTLEDELRLMSHFHHV 90
Cdd:PRK13648 40 IVGHNGSGKSTIAKlmigiekvksgEIFYNNQAI--TDDNFEKlRKHIGI---VFQNPDNQFVGSIVKYDVAFGLENHAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 91 NFEIGKRL---------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGiklvlgsipkgsliseh 161
Cdd:PRK13648 115 PYDEMHRRvsealkqvdMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA----------------- 177
|
170
....*....|..
gi 2619813829 162 rTKHLLNLVQRV 173
Cdd:PRK13648 178 -RQNLLDLVRKV 188
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
14-117 |
9.23e-07 |
|
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: 50.57 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQ--DFCERKDY-SLLSAVFQD---------PSSQILATTL 77
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTglyrPESGEILLDGQpvTADNREAYrQLFSAVFSDfhlfdrllgLDGEADPARA 433
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2619813829 78 EDELRLMSHFHHVNFEIGKrlmgpyFSTdfFKLSDGYRKR 117
Cdd:COG4615 434 RELLERLELDHKVSVEDGR------FST--TDLSQGQRKR 465
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
221-364 |
9.34e-07 |
|
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: 50.05 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTT----ILR--------------------KLS---------KKIYSVFQN----LD-- 261
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTlaraILGllpppgitsgeilfdgedllKLSekelrkirgREIQMIFQDpmtsLNpv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 262 ---LQFFHETVA--DEVGNDDA-------LSLFGLTELRERS---PFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD 326
Cdd:COG0444 103 mtvGDQIAEPLRihGGLSKAEAreraielLERVGLPDPERRLdryPHELSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2619813829 327 gdglqnfV----KMVELLRE--ERRGL--ILATHDKDVIP-ICDQII 364
Cdd:COG0444 183 -------VtiqaQILNLLKDlqRELGLaiLFITHDLGVVAeIADRVA 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-141 |
1.19e-06 |
|
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: 48.87 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINsILC-------QRHNVfLDDQDFCERKDY-SLLSAVFQDPSSQILATTLEDELRLMS 85
Cdd:cd03267 43 TIEKGEIVGFIGPNGAGKTTTLK-ILSgllqptsGEVRV-AGLVPWKRRKKFlRRIGVVFGQKTQLWWDLPVIDSFYLLA 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2619813829 86 HFHHVN-FEIGKRL--------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:cd03267 121 AIYDLPpARFKKRLdelselldLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
221-364 |
1.20e-06 |
|
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: 50.07 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTI----------------------------LRKLSKKIYSVFQN------------- 259
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLglallrlipsegeirfdgqdldglsrraLRPLRRRMQVVFQDpfgslsprmtvgq 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 260 -----LDLQFFHETVAD---EVgnDDALSLFGLT-ELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgDGL 330
Cdd:COG4172 384 iiaegLRVHGPGLSAAErraRV--AEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSV 460
|
170 180 190
....*....|....*....|....*....|....*....
gi 2619813829 331 QnfVKMVELLRE--ERRGL--ILATHDKDVIP-ICDQII 364
Cdd:COG4172 461 Q--AQILDLLRDlqREHGLayLFISHDLAVVRaLAHRVM 497
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-141 |
1.32e-06 |
|
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: 48.67 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSI--LCQ--RHNVFLDDQDFC----ERKDYSLlsaVFQD------------------ 67
Cdd:cd03259 22 TVEPGEFLALLGPSGCGKTTLLRLIagLERpdSGEILIDGRDVTgvppERRNIGM---VFQDyalfphltvaeniafglk 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2619813829 68 ----PSSQIlaTTLEDELRLMSHFHHVnfeiGKRLmgPYfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:cd03259 99 lrgvPKAEI--RARVRELLELVGLEGL----LNRY--PH------ELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
211-363 |
1.42e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKkIYS------VFQNLDLQF-------------FHE---- 267
Cdd:PRK10762 15 PGVKALS---GAALNVYPGRVMALVGENGAGKSTMMKVLTG-IYTrdagsiLYLGKEVTFngpkssqeagigiIHQelnl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 268 ----TVAD------EVGN--------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTT 323
Cdd:PRK10762 91 ipqlTIAEniflgrEFVNrfgridwkkmyaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2619813829 324 AMDGDGLQNFVKMVELLREERRGLILATHD-KDVIPICDQI 363
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQGRGIVYISHRlKEIFEICDDV 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
13-178 |
1.48e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.87 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQD-----------------------FceRKdyslLS--- 62
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVglvkPDSGRIFLDGEDithlpmhkrarlgigylpqeasiF--RK----LTved 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 63 ---AV--FQDPSSQILATTLEDelrLMSHFH--HVnfeigKRLMGpyfstdfFKLSDGYRKRFVISSVLSYGPEYLLIDE 135
Cdd:COG1137 98 nilAVleLRKLSKKEREERLEE---LLEEFGitHL-----RKSKA-------YSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2619813829 136 PLSNLD---------------DEGIklvlgsipkGSLISEHRTKHLLNLVQRVYLLSG 178
Cdd:COG1137 163 PFAGVDpiavadiqkiirhlkERGI---------GVLITDHNVRETLGICDRAYIISE 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-163 |
1.59e-06 |
|
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: 48.77 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCERKDYSL---LSAVFQDPSsqILATTLEDELRL--- 83
Cdd:cd03251 24 DIPAGETVALVGPSGSGKSTLVNLIPrfydVDSGRILIDGHDVRDYTLASLrrqIGLVSQDVF--LFNDTVAENIAYgrp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 84 ------------MSHFHHV--NFE------IGKRLMgpyfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDE 143
Cdd:cd03251 102 gatreeveeaarAANAHEFimELPegydtvIGERGV---------KLSGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
170 180
....*....|....*....|
gi 2619813829 144 GIKLVLGSIPKgslISEHRT 163
Cdd:cd03251 173 SERLVQAALER---LMKNRT 189
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-161 |
1.64e-06 |
|
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: 48.37 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 16 ERDEIVGLVGRNGSGKTTLINSILCQRH----NVFLDDQDFCE-----------------------RKDYSLLSAVFQDP 68
Cdd:cd03268 24 KKGEIYGFLGPNGAGKTTTMKIILGLIKpdsgEITFDGKSYQKniealrrigalieapgfypnltaRENLRLLARLLGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 69 SSQIlattleDELRLMSHFHHvnfeIGKRLMGPYfstdffklSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIK-- 146
Cdd:cd03268 104 KKRI------DEVLDVVGLKD----SAKKKVKGF--------SLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKel 165
|
170
....*....|....*....
gi 2619813829 147 ----LVLGSIPKGSLISEH 161
Cdd:cd03268 166 reliLSLRDQGITVLISSH 184
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-141 |
1.71e-06 |
|
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: 48.27 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINsILCQRH-----NVFLDDQDFCERKD--YSLLSAVFQDpssQILATTL--EDELRL 83
Cdd:cd03263 23 LNVYKGEIFGLLGHNGAGKTTTLK-MLTGELrptsgTAYINGYSIRTDRKaaRQSLGYCPQF---DALFDELtvREHLRF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2619813829 84 MSHFHHVNFEIGKRLMGPYFSTdfFKLSDgYRKRFVISsvLSYG--------------PEYLLIDEPLSNLD 141
Cdd:cd03263 99 YARLKGLPKSEIKEEVELLLRV--LGLTD-KANKRART--LSGGmkrklslaialiggPSVLLLDEPTSGLD 165
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-144 |
1.73e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.94 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 15 LERDEIVGLVGRNGSGKTT---LINSILCQRHNVF-LDDQDFCERKDYSL---LSAVFQDPSSQILATTLEDELRL-MSH 86
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTtarLIDGLFEEFEGKVkIDGELLTAENVWNLrrkIGMVFQNPDNQFVGATVEDDVAFgMEN 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2619813829 87 FHHVNFEIGKRLMGPYFSTDFF--------KLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG 144
Cdd:PRK13642 110 QGIPREEMIKRVDEALLAVNMLdfktrepaRLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-185 |
1.82e-06 |
|
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: 47.91 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL------CQRHNVFLDDQDFC-----ERKDYSLLSAvFQDPsSQILATTLEDELR 82
Cdd:cd03217 22 TIKKGEVHALMGPNGSGKSTLAKTIMghpkyeVTEGEILFKGEDITdlppeERARLGIFLA-FQYP-PEIPGVKNADFLR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 83 lmshfhHVNfeigkrlMGpyfstdffkLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLV------LGSIPKGS 156
Cdd:cd03217 100 ------YVN-------EG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVaevinkLREEGKSV 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2619813829 157 LISEHRtKHLLNLVQ--RVYLL-------SGDVREVDK 185
Cdd:cd03217 158 LIITHY-QRLLDYIKpdRVHVLydgrivkSGDKELALE 194
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-144 |
1.85e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.83 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTlINSILC-----QRHNVFLDDQDFCE------RKDyslLSAVFQDPSSQILATTLEDEL 81
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKST-ISKILTgllkpQSGEIKIDGITISKenlkeiRKK---IGIIFQNPDNQFIGATVEDDI 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2619813829 82 RLMSHFHHVNFEIGKRL---------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG 144
Cdd:PRK13632 106 AFGLENKKVPPKKMKDIiddlakkvgMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKG 177
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
222-354 |
2.26e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.95 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 222 LRLKVRGGEVVCLIGKNGVGKTTILRKLS------------------------KKIYSVFQNLDLqFFHETVADEVGN-- 275
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAglekptegqifidgedvthrsiqqRDICMVFQSYAL-FPHMSLGENVGYgl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 --------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNfvkMVELLR 341
Cdd:PRK11432 104 kmlgvpkeerkqrvKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS---MREKIR 180
|
170
....*....|....*..
gi 2619813829 342 EERRGL----ILATHDK 354
Cdd:PRK11432 181 ELQQQFnitsLYVTHDQ 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
224-366 |
2.26e-06 |
|
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: 47.85 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTIL-------RKLSKKIY-----------------SVFQN------LDLQFFHETV-ADE 272
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLsallgelEKLSGSVSvpgsiayvsqepwiqngTIRENilfgkpFDEERYEKVIkACA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 273 VGND-DALSLFGLTELRERSpFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMV--ELLREER-RglI 348
Cdd:cd03250 106 LEPDlEILPDGDLTEIGEKG-INLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCilGLLLNNKtR--I 182
|
170
....*....|....*...
gi 2619813829 349 LATHDKDVIPICDQIISL 366
Cdd:cd03250 183 LVTHQLQLLPHADQIVVL 200
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
221-367 |
2.49e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.09 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLSK-------------KIYSVF------QNLDLQFFHETVADEV-------- 273
Cdd:PRK11231 20 DLSLSLPTGKITALIGPNGCGKSTLLKCFARlltpqsgtvflgdKPISMLssrqlaRRLALLPQHHLTPEGItvrelvay 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 274 GNDDALSLFG------------------LTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdgLQNFVK 335
Cdd:PRK11231 100 GRSPWLSLWGrlsaednarvnqameqtrINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD---INHQVE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2619813829 336 MVELLREerrgliLATHDKDVIPI----------CDQIISLS 367
Cdd:PRK11231 177 LMRLMRE------LNTQGKTVVTVlhdlnqasryCDHLVVLA 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-141 |
2.58e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.62 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLI---NSILCQRH-NVFLDDQDFCER-KDYSL------LSAVFQDPSSQILATTLEDELR 82
Cdd:PRK13646 29 EFEQGKYYAIVGQTGSGKSTLIqniNALLKPTTgTVTVDDITITHKtKDKYIrpvrkrIGMVFQFPESQLFEDTVEREII 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2619813829 83 LMSHFHHVNFEIGKR-----LMGPYFSTDF-----FKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:PRK13646 109 FGPKNFKMNLDEVKNyahrlLMDLGFSRDVmsqspFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
203-367 |
3.11e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 203 QIEYQRGspGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIYS-----VFQNLDLQ-------------- 263
Cdd:PRK10247 12 NVGYLAG--DAKILN---NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPtsgtlLFEGEDIStlkpeiyrqqvsyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 264 -----FFHETVAD------EVGND--------DALSLFGLTE-LRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTT 323
Cdd:PRK10247 87 aqtptLFGDTVYDnlifpwQIRNQqpdpaiflDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2619813829 324 AMDGDGLQNFVKMV-ELLREERRGLILATHDKDVIPICDQIISLS 367
Cdd:PRK10247 167 ALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-146 |
3.18e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.26 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 16 ERDEIVGLVGRNGSGKTTL---INSILCQRHNVFLDDQDFCERKDY----SLLSAVFQDPSSQILATTLEDEL------- 81
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLfrhFNGILKPTSGSVLIRGEPITKENIrevrKFVGLVFQNPDDQIFSPTVEQDIafgpinl 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 82 ---------RLMSHFHHVNFEiGKRLMGPYfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIK 146
Cdd:PRK13652 108 gldeetvahRVSSALHMLGLE-ELRDRVPH------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-141 |
3.38e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.01 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 19 EIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFcerKDYSL------LSAVFQDPssQILATTLEDELRL----- 83
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLrfydPTSGRILIDGVDI---RDLTLeslrrqIGVVPQDT--FLFSGTIRENIRYgrpda 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2619813829 84 ----------MSHFHHV--------NFEIGKRlmGpyfstdfFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:COG1132 442 tdeeveeaakAAQAHEFiealpdgyDTVVGER--G-------VNLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
276-367 |
4.93e-06 |
|
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: 46.80 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdgLQNFVKMVELLRE--ERRGLILATHD 353
Cdd:cd03264 112 DEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD---PEERIRFRNLLSElgEDRIVILSTHI 188
|
90
....*....|....*
gi 2619813829 354 -KDVIPICDQIISLS 367
Cdd:cd03264 189 vEDVESLCNQVAVLN 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
226-353 |
5.23e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 226 VRGGEVVCLIGKNGVGKTTILRKLS-------------------------KKIYSVFQNL--------------DL--QF 264
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipnlgdyeeepswdevlkrfrgTELQNYFKKLyngeikvvhkpqyvDLipKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 265 FHETV------ADEVGN-DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdgLQNFVKMV 337
Cdd:PRK13409 176 FKGKVrellkkVDERGKlDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQRLNVA 252
|
170
....*....|....*...
gi 2619813829 338 ELLRE--ERRGLILATHD 353
Cdd:PRK13409 253 RLIRElaEGKYVLVVEHD 270
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
277-353 |
5.28e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.81 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 277 DALSLFGLTELRER---SPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVK-MVELLREERRGLILATH 352
Cdd:PRK11022 133 DLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIElLLELQQKENMALVLITH 212
|
.
gi 2619813829 353 D 353
Cdd:PRK11022 213 D 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-162 |
5.49e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 46.79 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSI---LCQRH-NVFLDDQDfcerkdysllsAVFQDPSSQI----------LATTLED 79
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIaglLPPAAgTIKLDGGD-----------IDDPDVAEAChylghrnamkPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 80 ELRLMSHFHhvnfeiGKRLMGPYFSTDFFKLSD-----------GYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLV 148
Cdd:PRK13539 93 NLEFWAAFL------GGEELDIAAALEAVGLAPlahlpfgylsaGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170
....*....|....
gi 2619813829 149 LGsipkgsLISEHR 162
Cdd:PRK13539 167 AE------LIRAHL 174
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
278-353 |
5.50e-06 |
|
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: 48.14 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 278 ALSLFGLTELRE------RSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdglqnfV----KMVELLREERR-- 345
Cdd:COG4172 134 ALELLERVGIPDperrldAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD-------VtvqaQILDLLKDLQRel 206
|
90
....*....|
gi 2619813829 346 --GLILATHD 353
Cdd:COG4172 207 gmALLLITHD 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
224-366 |
5.95e-06 |
|
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: 46.84 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTI--------------------------LRKLSKKIYSVFQNLDLqfFHETVADEV--GN 275
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLvnliprfydvdsgrilidghdvrdytLASLRRQIGLVSQDVFL--FNDTVAENIayGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 DD--------ALSLFGLTELRERSP-----------FTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKM 336
Cdd:cd03251 101 PGatreeveeAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAA 180
|
170 180 190
....*....|....*....|....*....|
gi 2619813829 337 VELLREERRGLILAtHDKDVIPICDQIISL 366
Cdd:cd03251 181 LERLMKNRTTFVIA-HRLSTIENADRIVVL 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
212-366 |
6.15e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.70 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDVQVGLRLKVRGGEVVCLIGKNGVGKTTILRKLS------------------------------KKIYSVFQ--- 258
Cdd:PRK10584 19 GEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAglddgssgevslvgqplhqmdeearaklraKHVGFVFQsfm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 259 ---------NLDLQFFHETVADEVGNDDALSLF---GLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD 326
Cdd:PRK10584 99 liptlnaleNVELPALLRGESSRQSRNGAKALLeqlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2619813829 327 ---GDGLQNFvkMVELLREERRGLILATHDKDVIPICDQIISL 366
Cdd:PRK10584 179 rqtGDKIADL--LFSLNREHGTTLILVTHDLQLAARCDRRLRL 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-146 |
7.01e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.05 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 23 LVGRNGSGKTT---LINSILC-QRHNVFLDDQDFCE----------RKDYSLlsaVFQDPSSQILA-TTLEDelrlmSHF 87
Cdd:PRK13649 38 FIGHTGSGKSTimqLLNGLHVpTQGSVRVDDTLITStsknkdikqiRKKVGL---VFQFPESQLFEeTVLKD-----VAF 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2619813829 88 HHVNFEIGK-----------RLMG---PYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIK 146
Cdd:PRK13649 110 GPQNFGVSQeeaealareklALVGiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-39 |
7.41e-06 |
|
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: 46.66 E-value: 7.41e-06
10 20
....*....|....*....|....*.
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL 39
Cdd:cd03224 22 TVPEGEIVALLGRNGAGKTTLLKTIM 47
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
221-353 |
9.60e-06 |
|
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: 46.17 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKL-------SKKIY-----------------SVFQNLDLqFFHETVADEVGN- 275
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIagfikpdSGKILlngkditnlppekrdisYVPQNYAL-FPHMTVYKNIAYg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 276 ---------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdgLQNFVKMVELL 340
Cdd:cd03299 96 lkkrkvdkkeierkvLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD---VRTKEKLREEL 172
|
170
....*....|....*..
gi 2619813829 341 REERRGL----ILATHD 353
Cdd:cd03299 173 KKIRKEFgvtvLHVTHD 189
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
211-353 |
1.04e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.23 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKI-YS--------------------VFQN---LDLQFFH 266
Cdd:PRK11248 12 GGKPALE---DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVpYQhgsitldgkpvegpgaergvVFQNeglLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 267 ETVA------------DEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGdglqnFV 334
Cdd:PRK11248 89 DNVAfglqlagvekmqRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA-----FT 163
|
170 180
....*....|....*....|....*
gi 2619813829 335 K--MVELL----REERRGLILATHD 353
Cdd:PRK11248 164 ReqMQTLLlklwQETGKQVLLITHD 188
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-143 |
1.10e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.44 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSI--LCQ-------RHNVFLDDQDFCeRKDYSLL----SAVFQDPS---------- 69
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLRVFnrLIElypearvSGEVYLDGQDIF-KMDVIELrrrvQMVFQIPNpipnlsifen 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 70 -------SQILATTLEDELRLMSHFHHVNF--EIGKRLMGPYFstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNL 140
Cdd:PRK14247 103 valglklNRLVKSKKELQERVRWALEKAQLwdEVKDRLDAPAG-----KLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
...
gi 2619813829 141 DDE 143
Cdd:PRK14247 178 DPE 180
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
229-357 |
1.29e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 229 GEVVCLIGKNGVGKTTILRKLS-------------------------KKIYSVFQNL--------------DL--QFFHE 267
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSgelkpnlgdydeepswdevlkrfrgTELQDYFKKLangeikvahkpqyvDLipKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 268 TV------ADEVGN-DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdgLQNFVKMVELL 340
Cdd:COG1245 179 TVrellekVDERGKlDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQRLNVARLI 255
|
170
....*....|....*..
gi 2619813829 341 REerrgliLATHDKDVI 357
Cdd:COG1245 256 RE------LAEEGKYVL 266
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
221-363 |
1.31e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.14 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS---------------------------KKIYSVFQNLDLqFFHETV---- 269
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTgfykptggtillrgqhieglpghqiarMGVVRTFQHVRL-FREMTVienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 270 ------------------------ADEVGNDDA---LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPT 322
Cdd:PRK11300 102 lvaqhqqlktglfsgllktpafrrAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2619813829 323 TAM---DGDGLQNFVkmVELLREERRGLILATHD-KDVIPICDQI 363
Cdd:PRK11300 182 AGLnpkETKELDELI--AELRNEHNVTVLLIEHDmKLVMGISDRI 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-144 |
1.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.26 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 19 EIVGLVGRNGSGKTT---LINSIL-CQRHNVFLDDQDFCERKDYSL---LSAVFQDPSSQILATTLED------ELRLMS 85
Cdd:PRK13650 34 EWLSIIGHNGSGKSTtvrLIDGLLeAESGQIIIDGDLLTEENVWDIrhkIGMVFQNPDNQFVGATVEDdvafglENKGIP 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2619813829 86 HfhhvnFEIGKRL--------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG 144
Cdd:PRK13650 114 H-----EEMKERVnealelvgMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-141 |
1.47e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 46.27 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSI--LCQ--RHNVFLDD---QDFCERKDYS----LLSAVFQDPSSQILATTLEDEL 81
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLngLLQptEGKVTVGDivvSSTSKQKEIKpvrkKVGVVFQFPESQLFEETVLKDV 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 82 RlmshFHHVNFEIGKR--------------LMGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:PRK13643 107 A----FGPQNFGIPKEkaekiaaeklemvgLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-38 |
1.60e-05 |
|
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: 45.74 E-value: 1.60e-05
10 20
....*....|....*....|....*
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSI 38
Cdd:COG0410 25 EVEEGEIVALLGRNGAGKTTLLKAI 49
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-141 |
1.70e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 12 KVELERDEIVGLVGRNGSGKTTLINSILCQRHN------VFLDDQDFCErkDYSLLSAVFQDPSS----QILATT-LEDE 80
Cdd:COG2401 50 NLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtpvagcVDVPDNQFGR--EASLIDAIGRKGDFkdavELLNAVgLSDA 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2619813829 81 LRLMSHFHHvnfeigkrlmgpyfstdffkLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:COG2401 128 VLWLRRFKE--------------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
286-364 |
1.76e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.26 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 286 ELRERS---PFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD-GLQNFVKMVELLREERRGLILATHDKDVIP-IC 360
Cdd:PRK09473 150 EARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTvQAQIMTLLNELKREFNTAIIMITHDLGVVAgIC 229
|
....
gi 2619813829 361 DQII 364
Cdd:PRK09473 230 DKVL 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-176 |
1.91e-05 |
|
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: 44.34 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINsILCQRH-----NVFLDDQDFCerkdysllsavFQDPSsqilattleDELRLmshfh 88
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMK-ILSGLYkpdsgEILVDGKEVS-----------FASPR---------DARRA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 89 hvnfeiGKRLmgpyfstdFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSIpkGSLISE-------- 160
Cdd:cd03216 76 ------GIAM--------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI--RRLRAQgvavifis 139
|
170
....*....|....*.
gi 2619813829 161 HRTKHLLNLVQRVYLL 176
Cdd:cd03216 140 HRLDEVFEIADRVTVL 155
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
223-353 |
2.08e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.44 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 223 RLKV-RGGEVVCLIGKNGVGKTTILRKLSKK----------------IYSVFQNLDLQFFHETV---------------- 269
Cdd:cd03236 19 RLPVpREGQVLGLVGPNGIGKSTALKILAGKlkpnlgkfddppdwdeILDEFRGSELQNYFTKLlegdvkvivkpqyvdl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 270 ---------------ADEVGN-DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNF 333
Cdd:cd03236 99 ipkavkgkvgellkkKDERGKlDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180
....*....|....*....|
gi 2619813829 334 VKMVELLREERRGLILATHD 353
Cdd:cd03236 179 ARLIRELAEDDNYVLVVEHD 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
224-366 |
2.11e-05 |
|
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: 45.22 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLSkKIYSVFQN-----------LDLQ-FFHEtvaDEVGNDDA---LSLFGLT--E 286
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLA-GIYPPDSGtvtvrgrvsslLGLGgGFNP---ELTGRENIylnGRLLGLSrkE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 287 LRERSPF----------------TLSLGQKMRVLIASAYASGYKVIGLDEPTTAmdGDglQNFV-KMVELLREER---RG 346
Cdd:cd03220 119 IDEKIDEiiefselgdfidlpvkTYSSGMKARLAFAIATALEPDILLIDEVLAV--GD--AAFQeKCQRRLRELLkqgKT 194
|
170 180
....*....|....*....|.
gi 2619813829 347 LILATHD-KDVIPICDQIISL 366
Cdd:cd03220 195 VILVSHDpSSIKRLCDRALVL 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
222-366 |
2.24e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.55 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 222 LRLKVRGGEVVCLIGKNGVGKTTILRKL--------------------------SKKIYSVFQNL---DLQFFHETVA-- 270
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLgrhqppsegeilldaqpleswsskafARKVAYLPQQLpaaEGMTVRELVAig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 271 --------------DEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKM 336
Cdd:PRK10575 110 rypwhgalgrfgaaDREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190
....*....|....*....|....*....|...
gi 2619813829 337 VELLREErRGL--ILATHDKDVIP-ICDQIISL 366
Cdd:PRK10575 190 VHRLSQE-RGLtvIAVLHDINMAArYCDYLVAL 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
212-352 |
2.25e-05 |
|
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: 44.83 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTilrkLSKKI-----YSV------FQNLDLQF--------------FH 266
Cdd:cd03217 12 GKEILK---GVNLTIKKGEVHALMGPNGSGKST----LAKTImghpkYEVtegeilFKGEDITDlppeerarlgiflaFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 267 ETVA-DEVGNDDALSlfgltELRErspfTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERR 345
Cdd:cd03217 85 YPPEiPGVKNADFLR-----YVNE----GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGK 155
|
....*..
gi 2619813829 346 GLILATH 352
Cdd:cd03217 156 SVLIITH 162
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
221-367 |
2.53e-05 |
|
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: 44.95 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTIL-------------------------RKLSKKIYSVFQNLDLQFFHETVA----- 270
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLdaisgrvegggttsgqilfngqprkPDQFQKCVAYVRQDDILLPGLTVRetlty 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 271 ---------------DEVGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVK 335
Cdd:cd03234 105 tailrlprkssdairKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS 184
|
170 180 190
....*....|....*....|....*....|....
gi 2619813829 336 MVELLREERRGLILATHD--KDVIPICDQIISLS 367
Cdd:cd03234 185 TLSQLARRNRIVILTIHQprSDLFRLFDRILLLS 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
217-366 |
2.59e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 46.25 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 217 DVQV--GLRLKVRGGEVVCLIGKNGVGKTTI---------------------LRK-----LSKKIYSVFQN--------- 259
Cdd:TIGR00958 493 DVPVlkGLTFTLHPGEVVALVGPSGSGKSTVaallqnlyqptggqvlldgvpLVQydhhyLHRQVALVGQEpvlfsgsvr 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 260 ----LDLQFFHE----TVADEVGNDDALSLFGL---TELRERSPFtLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD 328
Cdd:TIGR00958 573 eniaYGLTDTPDeeimAAAKAANAHDFIMEFPNgydTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190
....*....|....*....|....*....|....*...
gi 2619813829 329 GLQNFvkmVELLREERRGLILATHDKDVIPICDQIISL 366
Cdd:TIGR00958 652 CEQLL---QESRSRASRTVLLIAHRLSTVERADQILVL 686
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-38 |
2.60e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.07 E-value: 2.60e-05
10 20
....*....|....*....|....*
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSI 38
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKLI 72
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
224-366 |
2.67e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.79 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLS--KKIYS----------------------VFQNLDLqFFHETVADEVG----- 274
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAglEDITSgdlfigekrmndvppaergvgmVFQSYAL-YPHLSVAENMSfglkl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 -----------NDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD-GLQNFVKMVELLRE 342
Cdd:PRK11000 103 agakkeeinqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlRVQMRIEISRLHKR 182
|
170 180
....*....|....*....|....*
gi 2619813829 343 ERRGLILATHDK-DVIPICDQIISL 366
Cdd:PRK11000 183 LGRTMIYVTHDQvEAMTLADKIVVL 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-143 |
2.93e-05 |
|
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: 44.71 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSILCQ----RHNVFLDDQDFCERKDYSL------LSAVFQDpssqilattledeLR 82
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEelptSGTIRVNGQDVSDLRGRAIpylrrkIGVVFQD-------------FR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 83 LMSH---FHHVNF----------EIGKR------LMGPYFSTDFF--KLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:cd03292 89 LLPDrnvYENVAFalevtgvpprEIRKRvpaaleLVGLSHKHRALpaELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
..
gi 2619813829 142 DE 143
Cdd:cd03292 169 PD 170
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
229-366 |
3.99e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 229 GEVVCLIGKNGVGKTTILRKLskkIYSVFQnldlQFFHETVADEVGNDD--ALSLFGLTELRerspFTLSLGQKMRVLIA 306
Cdd:cd03227 21 GSLTIITGPNGSGKSTILDAI---GLALGG----AQSATRRRSGVKAGCivAAVSAELIFTR----LQLSGGEKELSALA 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 307 SAYAS----GYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQIISL 366
Cdd:cd03227 90 LILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
211-366 |
5.08e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKkIYS------VFQNLDLQFFHETVADEVGnddaLSLFG- 283
Cdd:PRK10982 9 PGVKALD---NVNLKVRPHSIHALMGENGAGKSTLLKCLFG-IYQkdsgsiLFQGKEIDFKSSKEALENG----ISMVHq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 284 -LTELRERS--------------PF----------------------------TLSLGQKMRVLIASAYASGYKVIGLDE 320
Cdd:PRK10982 81 eLNLVLQRSvmdnmwlgryptkgMFvdqdkmyrdtkaifdeldididprakvaTLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2619813829 321 PTTAMDGDGLQNFVKMVELLREERRGLILATHDKDVI-PICDQIISL 366
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITIL 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-141 |
5.33e-05 |
|
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: 44.10 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIlcqrhN---------VFLDDQDFCERKDYSLLSA------VFQDPSsqilattLE 78
Cdd:cd03256 23 SINPGEFVALIGPSGAGKSTLLRCL-----NglveptsgsVLIDGTDINKLKGKALRQLrrqigmIFQQFN-------LI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 79 DELR-----LMSHFHHVNF---------EIGKRL---------MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDE 135
Cdd:cd03256 91 ERLSvlenvLSGRLGRRSTwrslfglfpKEEKQRalaalervgLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
....*.
gi 2619813829 136 PLSNLD 141
Cdd:cd03256 171 PVASLD 176
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-141 |
5.83e-05 |
|
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: 44.03 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILCQRH----NVFLDDQDFC---ERKDYSL---LSAVFQDP---SS----QILA-- 74
Cdd:cd03261 22 DVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgEVLIDGEDISglsEAELYRLrrrMGMLFQSGalfDSltvfENVAfp 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 75 ----TTLEDEL---RLMSHFHHVNFEIGKRLMgPYfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:cd03261 102 lrehTRLSEEEireIVLEKLEAVGLRGAEDLY-PA------ELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-167 |
6.85e-05 |
|
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: 43.92 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILCQRH-----NVFLDDQDFCE------RKDYSLLSAVFQD--PSS----QILATT 76
Cdd:COG1119 25 TVKPGEHWAILGPNGAGKSTLLSLITGDLPptygnDVRLFGERRGGedvwelRKRIGLVSPALQLrfPRDetvlDVVLSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 77 LEDELRLMSHFHHVNFEIGKRLM-----GPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGS 151
Cdd:COG1119 105 FFDSIGLYREPTDEQRERARELLellglAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL 184
|
170
....*....|....*.
gi 2619813829 152 IpkgSLISEHRTKHLL 167
Cdd:COG1119 185 L---DKLAAEGAPTLV 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-143 |
7.01e-05 |
|
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: 43.63 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSILC----QRHNVFLDDQDF--CERKDYSLLSA-----VFQDPS------------ 69
Cdd:cd03255 25 LSIEKGEFVAIVGPSGSGKSTLLNILGGldrpTSGEVRVDGTDIskLSEKELAAFRRrhigfVFQSFNllpdltalenve 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2619813829 70 -SQILATTL--EDELRLMSHFHHVNfeIGKRLmgpyfsTDF-FKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDE 143
Cdd:cd03255 105 lPLLLAGVPkkERRERAEELLERVG--LGDRL------NHYpSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
290-364 |
7.02e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 7.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2619813829 290 RSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREE-RRGLILATHDKDVIP-ICDQII 364
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAeIADRVL 240
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
221-357 |
7.31e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.71 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRK-----------------------------LSKKIYSVFQNLDLqFFHETVAD 271
Cdd:PRK10908 20 GVTFHMRPGEMAFLTGHSGAGKSTLLKLicgierpsagkiwfsghditrlknrevpfLRRQIGMIFQDHHL-LMDRTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 272 EVG---------NDD-------ALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVK 335
Cdd:PRK10908 99 NVAipliiagasGDDirrrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180
....*....|....*....|..
gi 2619813829 336 MVELLREERRGLILATHDKDVI 357
Cdd:PRK10908 179 LFEEFNRVGVTVLMATHDIGLI 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-143 |
8.83e-05 |
|
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: 43.34 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 20 IVGLVGRNGSGKTTLINsILC-----QRHNVFLDDQDFCERKD--YSLLSAVFQDPS--SQIlatTLEDELRLM------ 84
Cdd:cd03264 27 MYGLLGPNGAGKTTLMR-ILAtltppSSGTIRIDGQDVLKQPQklRRRIGYLPQEFGvyPNF---TVREFLDYIawlkgi 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 85 --SHFHH--------VN-FEIGKRLMGpyfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDE 143
Cdd:cd03264 103 psKEVKArvdevlelVNlGDRAKKKIG--------SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
230-326 |
1.02e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 43.23 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 230 EVVCLIGKNGVGKTTILRKL-------------------SKKIYS--------------VFQ-----------NLDLQFF 265
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSInrmndlnpevtitgsivynGHNIYSprtdtvdlrkeigmVFQqpnpfpmsiyeNVVYGLR 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2619813829 266 HETVADEVGNDDAL--SLFGLT---ELRER---SPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD 326
Cdd:PRK14239 112 LKGIKDKQVLDEAVekSLKGASiwdEVKDRlhdSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
271-357 |
1.97e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 271 DEVGNDDALSLFGLtelrerSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERR-GLIL 349
Cdd:PRK10418 123 EAVGLENAARVLKL------YPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlGMLL 196
|
....*...
gi 2619813829 350 ATHDKDVI 357
Cdd:PRK10418 197 VTHDMGVV 204
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
229-354 |
2.40e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.86 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 229 GEVVCLIGKNGVGKTTILrKLSKKIYSVfQNLDLQFFHETVADE------------------------------------ 272
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLL-KLIAGLLNP-EKGEILFERQSIKKDlctyqkqlcfvghrsginpyltlrenclydihfspg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 273 -VGNDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILAT 351
Cdd:PRK13540 105 aVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTS 184
|
...
gi 2619813829 352 HDK 354
Cdd:PRK13540 185 HQD 187
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-135 |
2.48e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 10 PGKVELERDEIVGLVGRNGSGKTTLinSILC------QRHNVFLDDQ--DFCERKDY-SLLSAVFQD------------- 67
Cdd:PRK10522 341 PINLTIKRGELLFLIGGNGSGKSTL--AMLLtglyqpQSGEILLDGKpvTAEQPEDYrKLFSAVFTDfhlfdqllgpegk 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 68 -PSSQILATTLEdelRL-MShfHHVNFEIGKrlmgpyFSTdfFKLSDGYRKRFVISSVLSYGPEYLLIDE 135
Cdd:PRK10522 419 pANPALVEKWLE---RLkMA--HKLELEDGR------ISN--LKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
217-366 |
2.58e-04 |
|
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: 42.07 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 217 DVQV--GLRLKVRGGEVVCLIGKNGVGKTTIL--------------------------RKLSKKIYSVFQnlDLQFFHET 268
Cdd:cd03248 26 DTLVlqDVSFTLHPGEVTALVGPSGSGKSTVVallenfyqpqggqvlldgkpisqyehKYLHSKVSLVGQ--EPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 269 VADEV-------------------GNDDALSLFGL---TELRERSPfTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD 326
Cdd:cd03248 104 LQDNIayglqscsfecvkeaaqkaHAHSFISELASgydTEVGEKGS-QLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2619813829 327 GDGLQnfvKMVELLRE--ERRGLILATHDKDVIPICDQIISL 366
Cdd:cd03248 183 AESEQ---QVQQALYDwpERRTVLVIAHRLSTVERADQILVL 221
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-357 |
2.59e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 22 GLVGRNGSGKTTLINSIL----------CQRHNVfldDQDFCErKDYSLLSAVFqdpSSQILATTL-EDELRLMSHFHHV 90
Cdd:PLN03073 207 GLVGRNGTGKTTFLRYMAmhaidgipknCQILHV---EQEVVG-DDTTALQCVL---NTDIERTQLlEEEAQLVAQQREL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 91 NFE------------------IGKRLMGPY-----------------------FSTDFFK-----LSDGYRKRFVISSVL 124
Cdd:PLN03073 280 EFEtetgkgkgankdgvdkdaVSQRLEEIYkrlelidaytaearaasilaglsFTPEMQVkatktFSGGWRMRIALARAL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 125 SYGPEYLLIDEPLSNLDDEGI---KLVLGSIPKGSLISEHrTKHLLNLV---------QRVYLLSGDVREVDK---EKLE 189
Cdd:PLN03073 360 FIEPDLLLLDEPTNHLDLHAVlwlETYLLKWPKTFIVVSH-AREFLNTVvtdilhlhgQKLVTYKGDYDTFERtreEQLK 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 190 DQE---------------FL---RRNGLRG------------------------FQIEYQR-----------------GS 210
Cdd:PLN03073 439 NQQkafesnersrshmqaFIdkfRYNAKRAslvqsrikaldrlghvdavvndpdYKFEFPTpddrpgppiisfsdasfGY 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 211 PGSEIL--DVQVGLRLKVRggevVCLIGKNGVGKTTILRKLSKKIY----SVFQN--LDLQFFHETVAD----------- 271
Cdd:PLN03073 519 PGGPLLfkNLNFGIDLDSR----IAMVGPNGIGKSTILKLISGELQpssgTVFRSakVRMAVFSQHHVDgldlssnplly 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 272 ---------EVGNDDALSLFGLT-ELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLR 341
Cdd:PLN03073 595 mmrcfpgvpEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ 674
|
490
....*....|....*.
gi 2619813829 342 EerrGLILATHDKDVI 357
Cdd:PLN03073 675 G---GVLMVSHDEHLI 687
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
208-367 |
2.60e-04 |
|
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: 41.38 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 208 RGSPGSEILDVQVGLRLKVRGGEVVCLIGKNGVGKTTILR---------KLSKKIYSVFQNLDLQFFHETVAdEVGNDDA 278
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNalagrrtglGVSGEVLINGRPLDKRSFRKIIG-YVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 279 LSLFgLTeLRERSPFT-----LSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHD 353
Cdd:cd03213 93 LHPT-LT-VRETLMFAaklrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQ 170
|
170
....*....|....*.
gi 2619813829 354 --KDVIPICDQIISLS 367
Cdd:cd03213 171 psSEIFELFDKLLLLS 186
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-162 |
2.67e-04 |
|
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: 42.78 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 19 EIVGLVGRNGSGKTTLINSI----LCQRHNVFLDDQDFcerKDYSL------LSAVFQD--------------------P 68
Cdd:TIGR02203 359 ETVALVGRSGSGKSTLVNLIprfyEPDSGQILLDGHDL---ADYTLaslrrqVALVSQDvvlfndtianniaygrteqaD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 69 SSQIL-------ATTLEDELRLMSHfhhvnFEIGKRLMgpyfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:TIGR02203 436 RAEIEralaaayAQDFVDKLPLGLD-----TPIGENGV---------LLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180
....*....|....*....|....*.
gi 2619813829 142 DEGIKLV---LGSIPKG--SLISEHR 162
Cdd:TIGR02203 502 NESERLVqaaLERLMQGrtTLVIAHR 527
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-80 |
2.68e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 2.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 18 DEIVGLVGRNGSGKTTLINSI---LCQRHNVFLDDQDFCERKDYSL----LSAVFQDPSSQILATTLEDE 80
Cdd:COG3593 23 DDLTVLVGENNSGKSSILEALrllLGPSSSRKFDEEDFYLGDDPDLpeieIELTFGSLLSRLLRLLLKEE 92
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
283-357 |
2.72e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 283 GLTELRERSpfTLSLGQKM------RVLIASAYASGYKVIGLDEPTTAMDGDGLQNF-VKMVELLREERRG----LILAT 351
Cdd:TIGR00606 1190 GDTALDMRG--RCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLaHALVEIIKSRSQQrnfqLLVIT 1267
|
....*.
gi 2619813829 352 HDKDVI 357
Cdd:TIGR00606 1268 HDEDFV 1273
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-247 |
2.83e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.70 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINsILC--QRHN---VFLDDqdfcerKDYSLLS----------AVFQDPSsqiLATTL- 77
Cdd:COG1129 26 ELRPGEVHALLGENGAGKSTLMK-ILSgvYQPDsgeILLDG------EPVRFRSprdaqaagiaIIHQELN---LVPNLs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 78 -------EDELR---LMSH----------FHHVNFEIG-KRLMGpyfstdffKLSDGYRKrFV-ISSVLSYGPEYLLIDE 135
Cdd:COG1129 96 vaeniflGREPRrggLIDWramrrrarelLARLGLDIDpDTPVG--------DLSVAQQQ-LVeIARALSRDARVLILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 136 PLSNLDDEGIKLVLGSIpkGSL---------ISeHRTKHLLNLVQRV-------YLLSGDVREVDKEKL--------EDQ 191
Cdd:COG1129 167 PTASLTEREVERLFRII--RRLkaqgvaiiyIS-HRLDEVFEIADRVtvlrdgrLVGTGPVAELTEDELvrlmvgreLED 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2619813829 192 EFLRRnglrgfqieyqRGSPGSEILDVQvGLR---------LKVRGGEVVCLIGKNGVGKTTILR 247
Cdd:COG1129 244 LFPKR-----------AAAPGEVVLEVE-GLSvggvvrdvsFSVRAGEILGIAGLVGAGRTELAR 296
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-34 |
3.27e-04 |
|
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: 41.75 E-value: 3.27e-04
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
20-353 |
3.31e-04 |
|
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: 41.99 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 20 IVGLVGRNGSGKTTLINSI--LCQRHNVFLDDQDFCERKDysllsaVFQDPSSQILATTLEDELRLMSHFHH---VNFEI 94
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALrfLADFDALVIGLTDERSRNG------GIGGIPSLLNGIDPKEPIEFEISEFLedgVRYRY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 95 GKRLMGPYFSTDFFKLSDGYRKRFvissvlsYGPEYLLIDEPLSNLDDEGIKLVLGS-IPKGSLISEHRTKHLLNLVQRV 173
Cdd:pfam13304 75 GLDLEREDVEEKLSSKPTLLEKRL-------LLREDSEEREPKFPPEAEELRLGLDVeERIELSLSELSDLISGLLLLSI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 174 YLLSGDVREVDKEKLedqefLRRNGLRGFQIEYQRGSPGSEILDVQVGLRLKVRggevvcligkNGVGKTTILRKLSKKI 253
Cdd:pfam13304 148 ISPLSFLLLLDEGLL-----LEDWAVLDLAADLALFPDLKELLQRLVRGLKLAD----------LNLSDLGEGIEKSLLV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 254 YSVFQNLDLQFFHETVADEVgnddalslfgltelrerSPFTLSLG-QKMRVLIASAY--ASGYKVIGLDEPTTAMDGDGL 330
Cdd:pfam13304 213 DDRLRERGLILLENGGGGEL-----------------PAFELSDGtKRLLALLAALLsaLPKGGLLLIDEPESGLHPKLL 275
|
330 340
....*....|....*....|...
gi 2619813829 331 QNFVKMVELLREERRGLILATHD 353
Cdd:pfam13304 276 RRLLELLKELSRNGAQLILTTHS 298
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
222-353 |
4.06e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 41.74 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 222 LRLKVRGGEVVCLIGKNGVGKTTILRKLSKKI----------------------------------------------YS 255
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgarvtgdvtlngeplaaidaprlarlravlpqaaqpafaFS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 256 VFQNLDL-QFFHETVADEVGNDD------ALSLFGLTELRERSPFTLSLGQKMRVLIASAYA---------SGYKVIGLD 319
Cdd:PRK13547 100 AREIVLLgRYPHARRAGALTHRDgeiawqALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLLLD 179
|
170 180 190
....*....|....*....|....*....|....*
gi 2619813829 320 EPTTAMDGDGLQNFVKMV-ELLREERRGLILATHD 353
Cdd:PRK13547 180 EPTAALDLAHQHRLLDTVrRLARDWNLGVLAIVHD 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
224-363 |
4.43e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.08 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLSKkIYS-----------VFQNLDLQFFHE----------TVADE--------VG 274
Cdd:PRK09700 26 LTVYPGEIHALLGENGAGKSTLMKVLSG-IHEptkgtitinniNYNKLDHKLAAQlgigiiyqelSVIDEltvlenlyIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 275 NDDALSLFGL-----TELRERSPF----------------TLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNF 333
Cdd:PRK09700 105 RHLTKKVCGVniidwREMRVRAAMmllrvglkvdldekvaNLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL 184
|
170 180 190
....*....|....*....|....*....|.
gi 2619813829 334 VKMVELLREERRGLILATHD-KDVIPICDQI 363
Cdd:PRK09700 185 FLIMNQLRKEGTAIVYISHKlAEIRRICDRY 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
251-326 |
5.93e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.40 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 251 KKIYSVFQNLDLqFFHETVAdevGN-------------DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIG 317
Cdd:PRK11144 76 RRIGYVFQDARL-FPHYKVR---GNlrygmaksmvaqfDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLL 151
|
....*....
gi 2619813829 318 LDEPTTAMD 326
Cdd:PRK11144 152 MDEPLASLD 160
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
212-353 |
5.98e-04 |
|
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: 40.25 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 212 GSEILDVQVGlrlKVRGGEVVCLIGKNGVGKTTILRKLSkkiysvfqnldlqffhetvADEVGNDDALSLFGLTELRERS 291
Cdd:cd03222 11 GVFFLLVELG---VVKEGEVIGIVGPNGTGKTTAVKILA-------------------GQLIPNGDNDEWDGITPVYKPQ 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2619813829 292 PFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREE-RRGLILATHD 353
Cdd:cd03222 69 YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgKKTALVVEHD 131
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
285-366 |
6.70e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 285 TELRERSpFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQII 364
Cdd:PTZ00243 774 TEIGEKG-VNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVV 852
|
..
gi 2619813829 365 SL 366
Cdd:PTZ00243 853 AL 854
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
204-367 |
6.82e-04 |
|
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: 41.65 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 204 IEYQRGSpGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTiLRKLSKKIY----------------------------- 254
Cdd:TIGR01193 479 VSYSYGY-GSNILS---DISLTIKMNSKTTIVGMSGSGKST-LAKLLVGFFqarsgeillngfslkdidrhtlrqfinyl 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 255 ---------SVFQNLDLQFFHETVADEVgnDDALSL-----------FGL-TELRERSpFTLSLGQKMRVLIASAYASGY 313
Cdd:TIGR01193 554 pqepyifsgSILENLLLGAKENVSQDEI--WAACEIaeikddienmpLGYqTELSEEG-SSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 314 KVIGLDEPTTAMDGDGLQNFVKmvELLREERRGLILATHDKDVIPICDQIISLS 367
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVN--NLLNLQDKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
198-351 |
7.44e-04 |
|
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: 40.32 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 198 GLRGFQIEYQRGSPGSEILDvqvGLRLKVRGGEVVCLIGKNGVGKTTILRKLSKKIYS--------VFQNLDLQFFHETV 269
Cdd:cd03233 5 SWRNISFTTGKGRSKIPILK---DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsvegdiHYNGIPYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 270 ADE---VGNDD--------------ALSLFGLTELRerspfTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQN 332
Cdd:cd03233 82 PGEiiyVSEEDvhfptltvretldfALRCKGNEFVR-----GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170
....*....|....*....
gi 2619813829 333 FVKMVELLREERRGLILAT 351
Cdd:cd03233 157 ILKCIRTMADVLKTTTFVS 175
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-162 |
8.05e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.49 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 19 EIVGLVGRNGSGKTTLINsiLCQRhnVF--------LDDQDFCERKDYSL---LSAVFQDPSsqILATTLEDELRL---- 83
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLIN--LLQR--VFdpqsgrilIDGTDIRTVTRASLrrnIAVVFQDAG--LFNRSIEDNIRVgrpd 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 84 -------------------MSHFHHVNFEIGKRlmGPyfstdffKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG 144
Cdd:PRK13657 436 atdeemraaaeraqahdfiERKPDGYDTVVGER--GR-------QLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180
....*....|....*....|...
gi 2619813829 145 ---IKLVLGSIPKG--SLISEHR 162
Cdd:PRK13657 507 eakVKAALDELMKGrtTFIIAHR 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
269-366 |
9.81e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 269 VADEVGNDdalslfglTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERR-GL 347
Cdd:PRK15134 408 VMEEVGLD--------PETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAY 479
|
90 100
....*....|....*....|
gi 2619813829 348 ILATHDKDVI-PICDQIISL 366
Cdd:PRK15134 480 LFISHDLHVVrALCHQVIVL 499
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-39 |
1.07e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 40.48 E-value: 1.07e-03
10 20
....*....|....*....|....*.
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL 39
Cdd:COG4152 23 TVPKGEIFGLLGPNGAGKTTTIRIIL 48
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
110-148 |
1.29e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 39.83 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2619813829 110 LSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLV 148
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKI 188
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
237-364 |
1.30e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 237 KNGVGKTTILRKLSKKIYSVFQNLDLQFFH---------ETVADEV--GNDDALSLF---GLTELR-ERSPFTLSLGQKM 301
Cdd:PRK00635 404 GTGLGDYANAATWHGKTFAEFQQMSLQELFiflsqlpskSLSIEEVlqGLKSRLSILidlGLPYLTpERALATLSGGEQE 483
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2619813829 302 RVLIAS---AYASGYKVIgLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQII 364
Cdd:PRK00635 484 RTALAKhlgAELIGITYI-LDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-172 |
1.35e-03 |
|
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: 39.76 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDD---QDFCERKDYSLLSAVFQDPssQILATTLED------- 79
Cdd:cd03248 36 TLHPGEVTALVGPSGSGKSTVVALLEnfyqPQGGQVLLDGkpiSQYEHKYLHSKVSLVGQEP--VLFARSLQDniayglq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 80 --------ELRLMSHFHhvNFeIGKRLMGPYFSTD--FFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVL 149
Cdd:cd03248 114 scsfecvkEAAQKAHAH--SF-ISELASGYDTEVGekGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQ 190
|
170 180
....*....|....*....|....*..
gi 2619813829 150 GSIPKGsliSEHRT----KHLLNLVQR 172
Cdd:cd03248 191 QALYDW---PERRTvlviAHRLSTVER 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
14-142 |
1.50e-03 |
|
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: 40.08 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSI--LC--QRHNVFLDD---QDfcERKDYSL------LSAVFQDPssqilattlede 80
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIagLErpDSGRIRLGGevlQD--SARGIFLpphrrrIGYVFQEA------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 81 lRLmshFHH--V--NFEIGKRLMGPYFSTDFF------------------KLSDGYRKRFVISSVLSYGPEYLLIDEPLS 138
Cdd:COG4148 87 -RL---FPHlsVrgNLLYGRKRAPRAERRISFdevvellgighlldrrpaTLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
....
gi 2619813829 139 NLDD 142
Cdd:COG4148 163 ALDL 166
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
221-363 |
1.56e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLSK---------KIY--------------------------------SVFQN 259
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegEIIfegeelqasnirdteragiaiihqelalvkelSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 260 LDLQffHETVADEVGNDDALSLFGLTELRER----SPFT----LSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQ 331
Cdd:PRK13549 103 IFLG--NEITPGGIMDYDAMYLRAQKLLAQLkldiNPATpvgnLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETA 180
|
170 180 190
....*....|....*....|....*....|...
gi 2619813829 332 NFVKMVELLREERRGLILATHDKD-VIPICDQI 363
Cdd:PRK13549 181 VLLDIIRDLKAHGIACIYISHKLNeVKAISDTI 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
221-352 |
1.60e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 39.83 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKLS-------------------KKIYS--------------VFQNLDlQFFHE 267
Cdd:PRK14267 22 GVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelneearvegevrlfgRNIYSpdvdpievrrevgmVFQYPN-PFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 268 TVADEVGndDALSLFGLT----ELRER--------------------SPFTLSLGQKMRVLIASAYASGYKVIGLDEPTT 323
Cdd:PRK14267 101 TIYDNVA--IGVKLNGLVkskkELDERvewalkkaalwdevkdrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190
....*....|....*....|....*....|.
gi 2619813829 324 AMDGDGLQnfvKMVELLREERR--GLILATH 352
Cdd:PRK14267 179 NIDPVGTA---KIEELLFELKKeyTIVLVTH 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
255-352 |
1.61e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 255 SVFQNLDL--QFFH---ETVADEVgnDDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDG 329
Cdd:NF033858 355 TVRQNLELhaRLFHlpaAEIAARV--AEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
90 100
....*....|....*....|....
gi 2619813829 330 LQNFVK-MVELLREERRGLILATH 352
Cdd:NF033858 433 RDMFWRlLIELSREDGVTIFISTH 456
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
284-364 |
1.80e-03 |
|
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: 39.13 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 284 LTELRERspftLSLGQKM------RVLIASAYASGYKVIGLDEPTTAMDGDGLQNfvKMVELLREERRG----LILATHD 353
Cdd:cd03240 109 LLDMRGR----CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE--SLAEIIEERKSQknfqLIVITHD 182
|
90
....*....|.
gi 2619813829 354 KDVIPICDQII 364
Cdd:cd03240 183 EELVDAADHIY 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
17-167 |
1.94e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.51 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 17 RDEIVGLVGRNGSGKTTLINSILCQrhnvflddqdfcerkdysllsavFQDPSSQILATTLEDELRlmshfhhvnfEIGK 96
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE-----------------------LGPPGGGVIYIDGEDILE----------EVLD 47
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2619813829 97 RLMGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEGIKLVLGSIPKGSLISEHRTKHLL 167
Cdd:smart00382 48 QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT 118
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-144 |
1.98e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 39.61 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINS----ILCQRHNVFLDD-------QDFCERKDYSL-LSAVFQDPSSQILATTLEDE 80
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLtnglIISETGQTIVGDyaipanlKKIKEVKRLRKeIGLVFQFPEYQLFQETIEKD 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 81 LRLMS-HFHHVNFEIGKR---------LMGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLDDEG 144
Cdd:PRK13645 112 IAFGPvNLGENKQEAYKKvpellklvqLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
230-355 |
2.01e-03 |
|
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: 40.38 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 230 EVVCLIGKNGVGKTTIL------------------RKLSKKIYSVFQNL------DLQFFHETVADEV---------GND 276
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLsiltgllpptsgtvlvggKDIETNLDAVRQSLgmcpqhNILFHHLTVAEHIlfyaqlkgrSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 277 DA-------LSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNfvkMVELLREERRG--L 347
Cdd:TIGR01257 1037 EAqlemeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS---IWDLLLKYRSGrtI 1113
|
....*...
gi 2619813829 348 ILATHDKD 355
Cdd:TIGR01257 1114 IMSTHHMD 1121
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
222-367 |
2.13e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 222 LRLKVRGGEVVCLIGKNGVGKTTILRKLSKKI-YSVFQNLDLQ-----------FFHETVADEV--GND----------D 277
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRgsvayvpqvswIFNATVRENIlfGSDfeserywraiD 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 278 A------LSLFG---LTELRERSpFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD-GLQNFVKMVellREERRG- 346
Cdd:PLN03232 716 VtalqhdLDLLPgrdLTEIGERG-VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCM---KDELKGk 791
|
170 180
....*....|....*....|..
gi 2619813829 347 -LILATHDKDVIPICDQIISLS 367
Cdd:PLN03232 792 tRVLVTNQLHFLPLMDRIILVS 813
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-68 |
2.20e-03 |
|
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: 40.05 E-value: 2.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSIL---CQRHNVFLDDQDFCERKDYSLLSA------VFQDP 68
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALLrliPSEGEIRFDGQDLDGLSRRALRPLrrrmqvVFQDP 371
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-54 |
2.40e-03 |
|
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: 39.19 E-value: 2.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILCQRH----NVFLDDQDFCE 54
Cdd:COG1127 27 DVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsgEILVDGQDITG 71
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-70 |
2.48e-03 |
|
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: 39.27 E-value: 2.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL-------CQRHNVFLDDQDFCERKDYSL-------LSAVFQDPSS 70
Cdd:COG0444 27 DVRRGETLGLVGESGSGKSTLARAILgllpppgITSGEILFDGEDLLKLSEKELrkirgreIQMIFQDPMT 97
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
209-353 |
2.67e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.31 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 209 GSPGSEILDvQVGLRLKVRGgeVVCLIGKNGVGKTTILRKLSK---KIY-------------SVFQNLD-LQF------- 264
Cdd:PRK14271 30 GFAGKTVLD-QVSMGFPARA--VTSLMGPTGSGKTTFLRTLNRmndKVSgyrysgdvllggrSIFNYRDvLEFrrrvgml 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 265 ------FHETVADEV----------------GNDDA-LSLFGLTE-LRER---SPFTLSLGQKMRVLIASAYASGYKVIG 317
Cdd:PRK14271 107 fqrpnpFPMSIMDNVlagvrahklvprkefrGVAQArLTEVGLWDaVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 2619813829 318 LDEPTTAMDGDGLQnfvKMVELLRE--ERRGLILATHD 353
Cdd:PRK14271 187 LDEPTSALDPTTTE---KIEEFIRSlaDRLTVIIVTHN 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-39 |
2.68e-03 |
|
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: 38.80 E-value: 2.68e-03
10 20
....*....|....*....|....*.
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL 39
Cdd:cd03269 22 SVEKGEIFGLLGPNGAGKTTTIRMIL 47
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
216-326 |
2.76e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 216 LDVQVGlrlKVRGGEVVCLIGKNGVGKTTILRKLSKKIY----SVFQNLDLQF--------FHETVAD---EVGND---- 276
Cdd:PRK13409 355 LEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKpdegEVDPELKISYkpqyikpdYDGTVEDllrSITDDlgss 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2619813829 277 ----DALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMD 326
Cdd:PRK13409 432 yyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
110-141 |
2.81e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 39.24 E-value: 2.81e-03
10 20 30
....*....|....*....|....*....|..
gi 2619813829 110 LSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
224-250 |
2.86e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 38.91 E-value: 2.86e-03
10 20
....*....|....*....|....*..
gi 2619813829 224 LKVRGGEVVCLIGKNGVGKTTILRKLS 250
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIA 73
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
221-249 |
2.92e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 2.92e-03
10 20
....*....|....*....|....*....
gi 2619813829 221 GLRLKVRGGEVVCLIGKNGVGKTTILRKL 249
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTL 365
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
292-353 |
2.93e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 39.69 E-value: 2.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2619813829 292 PFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDgLQnfVKMVELLREERR----GLILATHD 353
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVS-VQ--AQILQLLRELQQelnmGLLFITHN 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-184 |
3.22e-03 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 38.55 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCE---RKDYSLLSAVFQDPSsqILATTLEDELRLMSH 86
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALFrfleAEEGKIEIDGIDISTiplEDLRSSLTIIPQDPT--LFSGTIRSNLDPFDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 87 FHHVnfEIGKRLMgpyFSTDFFKLSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD---DEGIKLVLGSIPKGS--LISEH 161
Cdd:cd03369 108 YSDE--EIYGALR---VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDyatDALIQKTIREEFTNStiLTIAH 182
|
170 180
....*....|....*....|...
gi 2619813829 162 RTKHLLNLVQRVYLLSGDVREVD 184
Cdd:cd03369 183 RLRTIIDYDKILVMDAGEVKEYD 205
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
217-326 |
3.48e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.76 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 217 DVQVGLRL-----KVRGGEVVCLIGKNGVGKTTILRKL------SKKIY------------------------------- 254
Cdd:PRK03695 5 DVAVSTRLgplsaEVRAGEILHLVGPNGAGKSTLLARMagllpgSGSIQfagqpleawsaaelarhraylsqqqtppfam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 255 SVFQNLDLQFFHETVADEVGN--DDALSLFGLTELRERSPFTLSLGQKMRVLIASAYASGYKVIG-------LDEPTTAM 325
Cdd:PRK03695 85 PVFQYLTLHQPDKTRTEAVASalNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDINpagqlllLDEPMNSL 164
|
.
gi 2619813829 326 D 326
Cdd:PRK03695 165 D 165
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-141 |
3.80e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 38.53 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 13 VELERDEIVGLVGRNGSGKTTLINSI--LCQRH--NVFLDDQDFCERKDYSL---LSAVFQDPSSQILAT---------- 75
Cdd:COG4604 22 LTIPKGGITALIGPNGAGKSTLLSMIsrLLPPDsgEVLVDGLDVATTPSRELakrLAILRQENHINSRLTvrelvafgrf 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2619813829 76 -------TLEDElrlmshfHHVNFEIGkrlmgpYFSTDFFK------LSDGYRKRFVISSVLSYGPEYLLIDEPLSNLD 141
Cdd:COG4604 102 pyskgrlTAEDR-------EIIDEAIA------YLDLEDLAdryldeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
109-148 |
3.91e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 38.29 E-value: 3.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2619813829 109 KLSDGYRKRFVISSV-LSYGPEYLLiDEPLSNLDDEGIKLV 148
Cdd:PRK13543 137 QLSAGQKKRLALARLwLSPAPLWLL-DEPYANLDLEGITLV 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
284-364 |
4.22e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 284 LTELRERSpFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD-GLQNFVKmveLLREERRG--LILATHDKDVIPIC 360
Cdd:PLN03130 731 LTEIGERG-VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDK---CIKDELRGktRVLVTNQLHFLSQV 806
|
....
gi 2619813829 361 DQII 364
Cdd:PLN03130 807 DRII 810
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
285-367 |
4.40e-03 |
|
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: 39.16 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 285 TELRERSpFTLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGD-GLQNFVKMV---ELLREERRglILATHDKDVIPIC 360
Cdd:TIGR00957 752 TEIGEKG-VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpeGVLKNKTR--ILVTHGISYLPQV 828
|
....*..
gi 2619813829 361 DQIISLS 367
Cdd:TIGR00957 829 DVIIVMS 835
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-68 |
6.49e-03 |
|
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: 37.47 E-value: 6.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2619813829 19 EIVGLVGRNGSGKTTLINSIL----CQRHNVFLDDQDFCE--RKDY-SLLSAVFQDP 68
Cdd:cd03244 31 EKVGIVGRTGSGKSSLLLALFrlveLSSGSILIDGVDISKigLHDLrSRISIIPQDP 87
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
288-366 |
7.18e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 37.72 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 288 RERSPFT-LSLGQKMRVLIASAYASGYKVIGLDEPTTAMDGDGLQNFVKMVELLREERRGLILATHDKDVIPICDQIISL 366
Cdd:PRK14246 146 RLNSPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-357 |
8.15e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.01 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 15 LERDEIVGLVGRNGSGKTTLINsILCQrhNVFLDDQDFCERKDYsLLSAVFQDPS------------------------- 69
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMK-ILNG--EVLLDDGRIIYEQDL-IVARLQQDPPrnvegtvydfvaegieeqaeylkry 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 70 ---SQILATTLEDEL-----RLMSHFHHVN---FE--IGKRL--MGPYFSTDFFKLSDGYRKRFVISSVLSYGPEYLLID 134
Cdd:PRK11147 102 hdiSHLVETDPSEKNlnelaKLQEQLDHHNlwqLEnrINEVLaqLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 135 EPLSNLDDEGIKLVLGSIP--KGSL--ISEHRTkHLLNLVQRV-----------------YLLSG--DVR-------EVD 184
Cdd:PRK11147 182 EPTNHLDIETIEWLEGFLKtfQGSIifISHDRS-FIRNMATRIvdldrgklvsypgnydqYLLEKeeALRveelqnaEFD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 185 KeKLEDQEFLRRNG--------------LRGFQIEYqrgspgSEILDVQVGLRLKV----RGGEVV-------------- 232
Cdd:PRK11147 261 R-KLAQEEVWIRQGikarrtrnegrvraLKALRRER------SERREVMGTAKMQVeeasRSGKIVfemenvnyqidgkq 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 233 ---------------CLIGKNGVGKTTILRKL-------SKKIYsVFQNLDLQFFHE---------TVADEVGNDD---- 277
Cdd:PRK11147 334 lvkdfsaqvqrgdkiALIGPNGCGKTTLLKLMlgqlqadSGRIH-CGTKLEVAYFDQhraeldpekTVMDNLAEGKqevm 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2619813829 278 -------ALSL---FGLTELRERSPF-TLSLGQKMRVLIASAYASGYKVIGLDEPTTAMDgdglqnfVKMVELLRE---E 343
Cdd:PRK11147 413 vngrprhVLGYlqdFLFHPKRAMTPVkALSGGERNRLLLARLFLKPSNLLILDEPTNDLD-------VETLELLEElldS 485
|
490
....*....|....*
gi 2619813829 344 RRG-LILATHDKDVI 357
Cdd:PRK11147 486 YQGtVLLVSHDRQFV 500
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
14-51 |
8.42e-03 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 37.33 E-value: 8.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2619813829 14 ELERDEIVGLVGRNGSGKTTLINSILCQRH----NVFLDDQD 51
Cdd:COG1136 30 SIEAGEFVAIVGPSGSGKSTLLNILGGLDRptsgEVLIDGQD 71
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-35 |
8.68e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 37.76 E-value: 8.68e-03
|
| |
