|
Name |
Accession |
Description |
Interval |
E-value |
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-235 |
6.45e-107 |
|
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: 309.65 E-value: 6.45e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDD 91
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:COG1122 87 QLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 172 PMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELA 235
Cdd:COG1122 167 PRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLE 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-278 |
3.49e-96 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 284.28 E-value: 3.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENvLKLHPRDIY---RKVGLVFQN 88
Cdd:PRK13639 8 KYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP-IKYDKKSLLevrKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 PDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:PRK13639 87 PDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 169 GLDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHIAELI 248
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRLPRVAHLI 245
|
250 260 270
....*....|....*....|....*....|
gi 1948769844 249 YQLKHEEGFSFsRLPLTIGEARREMVEAMQ 278
Cdd:PRK13639 246 EILNKEDNLPI-KMGYTIGEARRNIKELLK 274
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-275 |
4.69e-95 |
|
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: 281.26 E-value: 4.69e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGT----VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVL---KLHPRDI 78
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 79 YRKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLLAMG 157
Cdd:TIGR04521 81 RKKVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 158 HEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANV 237
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDELEKI 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 1948769844 238 KLRLPHIAELIYQLKhEEGFSFSRLPLTIGEARREMVE 275
Cdd:TIGR04521 241 GLDVPEITELARKLK-EKGLPVPKDPLTVEEAADEILK 277
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-217 |
1.10e-87 |
|
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: 260.09 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDG-TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPD 90
Cdd:cd03225 6 SFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:cd03225 86 DQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1948769844 171 DPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGR 217
Cdd:cd03225 166 DPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-276 |
7.68e-87 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 260.06 E-value: 7.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVL-KLHPRDIYRKVG 83
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:TIGR04520 81 MVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPH 243
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQVELLKEIGLDVPF 239
|
250 260 270
....*....|....*....|....*....|...
gi 1948769844 244 IAELIYQLKhEEGFSFSRLPLTIgearREMVEA 276
Cdd:TIGR04520 240 ITELAKALK-KRGIPLPPDILTE----EELVDE 267
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-278 |
8.96e-85 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 255.54 E-value: 8.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTRISVDLESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGEnvlklhPRDIYR 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK------PIDYSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 81 K--------VGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAG 152
Cdd:PRK13636 75 KglmklresVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 153 LLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1948769844 233 ELANVKLRLPHIAELIYQLKHEEGFSFSRLPLTIGEARREMVEAMQ 278
Cdd:PRK13636 235 MLRKVNLRLPRIGHLMEILKEKDGFVFDELDLTISQARKTLNSWKN 280
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-280 |
1.65e-83 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 251.96 E-value: 1.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLV 85
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 166 PTAGLDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPeEVFTAPDELANVKLRLPHIA 245
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGLRLPLVA 242
|
250 260 270
....*....|....*....|....*....|....*
gi 1948769844 246 ELiyqLKHEEGFSFSRLPLTIGEARREMVEAMQRS 280
Cdd:PRK13647 243 QI---FEDLPELGQSKLPLTVKEAVQIIRKLLTKG 274
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-202 |
5.86e-73 |
|
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: 221.91 E-value: 5.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVL--KLHPRDIYRKVGLVFQNPDDQ 92
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysRKGLLERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 93 LFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP 172
Cdd:TIGR01166 81 LFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 1948769844 173 MGEYRMMELLTRLnRDQGVTIVMATHSVDL 202
Cdd:TIGR01166 161 AGREQMLAILRRL-RAEGMTVVISTHDVDL 189
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-275 |
1.18e-70 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 219.53 E-value: 1.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGT----VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVL--KLHPRDIY 79
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 80 RKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASV--DMAEFAGKGIHNLSYGQKKRVCIAGLLAMG 157
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 158 HEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANV 237
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESI 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 1948769844 238 KLRLPHIAELIYQLKhEEGFSFSRLPLTIGEARREMVE 275
Cdd:PRK13637 243 GLAVPQVTYLVRKLR-KKGFNIPDDIFTIEEAKEEILK 279
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-279 |
1.38e-69 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 216.49 E-value: 1.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDG-----TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKL-HPRDIYRKVGLV 85
Cdd:PRK13633 11 SYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:PRK13633 91 FQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 166 PTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHIA 245
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKEVEMMKKIGLDVPQVT 249
|
250 260 270
....*....|....*....|....*....|....
gi 1948769844 246 ELIYQLKhEEGFSFSRLPLTIgearREMVEAMQR 279
Cdd:PRK13633 250 ELAYELK-KEGVDIPSDILTI----DEMVNELCQ 278
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-278 |
4.52e-69 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 215.65 E-value: 4.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLdGENVLKLHPR-----DIYRKVGLVFQ 87
Cdd:PRK13634 14 YKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkklkPLRKKVGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 NPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEP 166
Cdd:PRK13634 93 FPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 167 TAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHIAE 246
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGLDLPETVK 252
|
250 260 270
....*....|....*....|....*....|..
gi 1948769844 247 LIYQLKHEEGFSFSRLPLTIGEARREMVEAMQ 278
Cdd:PRK13634 253 FKRALEEKFGISFPKPCLTLEELAHEVVQLLR 284
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-279 |
2.18e-65 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 205.81 E-value: 2.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDD 91
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PRK13652 90 QIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 172 PMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHIAELIYQL 251
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPSLPKLIRSL 249
|
250 260
....*....|....*....|....*...
gi 1948769844 252 KhEEGFSFSrLPLTIGEARREMVEAMQR 279
Cdd:PRK13652 250 Q-AQGIAID-MAYTYQEAEDAFLKAFGK 275
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-270 |
4.10e-64 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 202.67 E-value: 4.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLE--SYKYPDGT----VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---- 75
Cdd:PRK13649 1 MGINLQnvSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 76 RDIYRKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLL 154
Cdd:PRK13649 81 KQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 155 AMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDqGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDEL 234
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFL 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 1948769844 235 ANVKLRLPHIAELIYQLKhEEGFSFSRLPLTIGEAR 270
Cdd:PRK13649 240 EEKQLGVPKITKFAQRLA-DRGISFSSLPITIEEFR 274
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-237 |
4.68e-63 |
|
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: 198.73 E-value: 4.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDD 91
Cdd:COG1120 8 SVGYGGRPV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QlFATTVFEDAAFG--P--RNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPT 167
Cdd:COG1120 87 P-FGLTVRELVALGryPhlGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 168 AGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTaPDELANV 237
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT-PELLEEV 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-282 |
9.21e-63 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 199.09 E-value: 9.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTRISVDLESYKYPDGT-VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDG-----ENVLklh 74
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVW--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 75 prDIYRKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLL 154
Cdd:PRK13635 78 --DVRRQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 155 AMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFTAPDEL 234
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKSGHML 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1948769844 235 ANVKLRLPHIAELIYQLKhEEGFSFSRLPLTIGearrEMVEAMQRSRS 282
Cdd:PRK13635 235 QEIGLDVPFSVKLKELLK-RNGILLPNTYLTME----SLVDELWTLHS 277
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-237 |
7.83e-61 |
|
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: 200.90 E-value: 7.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKG---YKGEVLLDGENVLKLHPRDIYRK 81
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 82 VGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:COG1123 85 IGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 162 LLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANV 237
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-231 |
2.67e-60 |
|
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: 199.36 E-value: 2.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---RDIYRKVGLVFQNPDDQ 92
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYSS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 93 LFAT-TVFEDAAFGPRNMGCGD-AEVKTRVEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAG 169
Cdd:COG1123 355 LNPRmTVGDIIAEPLRLHGLLSrAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSA 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 170 LDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:COG1123 435 LDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-261 |
2.00e-56 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 183.08 E-value: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTRISVDLESYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLI---KGYKGEVLLDGENVLKLHPR 76
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 77 DIYRKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAM 156
Cdd:PRK13640 81 DIREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 157 GHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFTAPDELAN 236
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKE 239
|
250 260
....*....|....*....|....*
gi 1948769844 237 VKLRLPHIAELIYQLKhEEGFSFSR 261
Cdd:PRK13640 240 IGLDIPFVYKLKNKLK-EKGISVPQ 263
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-252 |
7.40e-56 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 180.96 E-value: 7.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGT-VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGL 84
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:PRK13632 88 IFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHI 244
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNNKEILEKAKIDSPFI 246
|
....*...
gi 1948769844 245 AELIYQLK 252
Cdd:PRK13632 247 YKLSKKLK 254
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
12-268 |
5.08e-55 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 179.64 E-value: 5.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGT----VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENV--------LKlhprDIY 79
Cdd:PRK13641 9 DYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnknLK----KLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 80 RKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLLAMGH 158
Cdd:PRK13641 85 KKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 159 EILLLDEPTAGLDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVK 238
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHY 243
|
250 260 270
....*....|....*....|....*....|
gi 1948769844 239 LRLPHIAELIYQLKhEEGFSFSRLPLTIGE 268
Cdd:PRK13641 244 LDEPATSRFASKLE-KGGFKFSEMPLTIDE 272
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-262 |
1.55e-54 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 177.89 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGE--NVLKLHPRDIYRKVGLVFQNPD 90
Cdd:PRK13638 9 FRYQDEPV-LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:PRK13638 88 QQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 171 DPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHIAELIYQ 250
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQPWLVKLHTQ 246
|
250
....*....|....*..
gi 1948769844 251 L-----KHEEGFsFSRL 262
Cdd:PRK13638 247 LglplcKTETEF-FHRM 262
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-226 |
9.93e-54 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 174.09 E-value: 9.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY---RKVGLVFQn 88
Cdd:COG2884 8 SKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRIGVVFQ- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 pDDQLFAT-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPT 167
Cdd:COG2884 87 -DFRLLPDrTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 168 AGLDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEE 226
Cdd:COG2884 166 GNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-231 |
1.07e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.51 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYpDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRdiyrkVGLVFQNPD- 90
Cdd:COG1121 13 TVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IGYVPQRAEv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFG-PRNMGCG---DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEP 166
Cdd:COG1121 87 DWDFPITVRDVVLMGrYGRRGLFrrpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 167 TAGLDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRgRLIRGGAPEEVFTAP 231
Cdd:COG1121 167 FAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEVLTPE 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-278 |
2.46e-53 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 175.20 E-value: 2.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTV----ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDG----ENVLKLHP-R 76
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEvK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 77 DIYRKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMA-EFAGKGIHNLSYGQKKRVCIAGLLA 155
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 156 MGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELA 235
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLT 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1948769844 236 NVKLRLPHIAELIYQLKHEEGFSFSRLPLTIGEARREMVEAMQ 278
Cdd:PRK13645 247 KIEIDPPKLYQLMYKLKNKGIDLLNKNIRTIEEFAKELAKVLK 289
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-255 |
6.31e-53 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 173.63 E-value: 6.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK-VGLVFQNPD 90
Cdd:PRK13644 8 SYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlVGIVFQNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:PRK13644 88 TQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 171 DPMGEYRMMELLTRLNRdQGVTIVMATHSvdlvpifLHQLH------ILSRGRLIRGGAPEEVFTAPdELANVKLRLPHI 244
Cdd:PRK13644 168 DPDSGIAVLERIKKLHE-KGKTIVYITHN-------LEELHdadriiVMDRGKIVLEGEPENVLSDV-SLQTLGLTPPSL 238
|
250
....*....|.
gi 1948769844 245 AELIYQLKHEE 255
Cdd:PRK13644 239 IELAENLKMHG 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-268 |
2.12e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 173.00 E-value: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLdGENVL-----KLHPRDIYRKVGLVFQNPD 90
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVsstskQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMA-EFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAG 169
Cdd:PRK13643 95 SQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 170 LDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHIAELIY 249
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGVPKATHFAD 253
|
250
....*....|....*....
gi 1948769844 250 QLKHEEGFSFSRLPLTIGE 268
Cdd:PRK13643 254 QLQKTGAVTFEKLPITRAE 272
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-201 |
1.33e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 169.89 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTRISVDLE----SYKYPDG-TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP 75
Cdd:COG1116 1 MSAAAPALELRgvskRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 76 RdiyrkVGLVFQNPddQLFA-TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLL 154
Cdd:COG1116 81 D-----RGVVFQEP--ALLPwLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1948769844 155 AMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVD 201
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVD 200
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-227 |
2.64e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.32 E-value: 2.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYpDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLVFQNP-- 89
Cdd:COG1131 7 TKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPal 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 DDQLfatTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAglLAMGH--EILLLDEPT 167
Cdd:COG1131 85 YPDL---TVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLA--LALLHdpELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 168 AGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:COG1131 160 SGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-265 |
4.25e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 169.14 E-value: 4.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGT--VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVG 83
Cdd:PRK13650 5 IEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:PRK13650 85 MVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLhILSRGRLIRGGAPEEVFTAPDELANVKLRLPH 243
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVL-VMKNGQVESTSTPRELFSRGNDLLQLGLDIPF 243
|
250 260
....*....|....*....|..
gi 1948769844 244 IAELIYQLKhEEGFSFSRLPLT 265
Cdd:PRK13650 244 TTSLVQSLR-QNGYDLPEGYLT 264
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
15-227 |
6.76e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 167.54 E-value: 6.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY---RKVGLVFQNPD- 90
Cdd:COG3638 12 YPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRIGMIFQQFNl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 -DQLfatTVFEDAAFG-------PRNM-GCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:COG3638 92 vPRL---SVLTNVLAGrlgrtstWRSLlGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 162 LLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:COG3638 169 LADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-222 |
5.79e-50 |
|
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: 162.99 E-value: 5.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQnpdd 91
Cdd:cd03214 6 SVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 qlfattvfedaafgprnmgcgdaevktrveaALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:cd03214 81 -------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 172 PMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGG 222
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-257 |
2.60e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 164.15 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKY-PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPD 90
Cdd:PRK13648 14 SFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:PRK13648 94 NQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 171 DPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpifLHQLHI--LSRGRLIRGGAPEEVFTAPDELANVKLRLPHIAELI 248
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEA---MEADHVivMNKGTVYKEGTPTEIFDHAEELTRIGLDLPFPIKIN 250
|
....*....
gi 1948769844 249 YQLKHEEGF 257
Cdd:PRK13648 251 QMLGHQTSF 259
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
17-219 |
7.97e-49 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 161.15 E-value: 7.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQNPddQLFAT 96
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQDY--ALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 -TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:cd03259 87 lTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1948769844 176 YRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:cd03259 167 EELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
27-234 |
1.04e-48 |
|
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: 161.69 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY---RKVGLVFQNPddQLF-ATTVFEDA 102
Cdd:COG1127 26 LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRIGMLFQGG--ALFdSLTVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 103 AFGPR-NMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMEL 181
Cdd:COG1127 104 AFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 182 LTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDEL 234
Cdd:COG1127 184 IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPW 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-220 |
4.83e-48 |
|
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: 159.17 E-value: 4.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDG---TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRdiyrkV 82
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 83 GLVFQnpDDQLFA-TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:cd03293 76 GYVFQ--QDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 162 LLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpIFL-HQLHILSR--GRLIR 220
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEA-VFLaDRVVVLSArpGRIVA 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-216 |
1.04e-47 |
|
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: 158.08 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYpDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGEnvlklHPRDIYRKVGLVFQNPD- 90
Cdd:cd03235 6 TVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQRRSi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFGPRNMGCG----DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEP 166
Cdd:cd03235 80 DRDFPISVRDVVLMGLYGHKGLfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1948769844 167 TAGLDPMGEYRMMELLTRLNRDqGVTIVMATHSVDLVPIFLHQLHILSRG 216
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
1.56e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 161.80 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTRISVDLESYKYpDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyR 80
Cdd:COG3842 1 MAMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 81 KVGLVFQnpDDQLFA-TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHE 159
Cdd:COG3842 78 NVGMVFQ--DYALFPhLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 160 ILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVD--------LVpiflhqlhILSRGRLIRGGAPEEVFTAP 231
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEealaladrIA--------VMNDGRIEQVGTPEEIYERP 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-261 |
2.72e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 159.87 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLI------------------KGYKGEVLLDGENVLKLHPR------ 76
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlpdtgtiewifkdeknkkKTKEKEKVLEKLVIQKTRFKkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 77 DIYRKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLLA 155
Cdd:PRK13651 102 EIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 156 MGHEILLLDEPTAGLDPMGEYRMMELLTRLNrDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELA 235
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKFLI 260
|
250 260
....*....|....*....|....*.
gi 1948769844 236 NVKLRLPHIAELIYQLKhEEGFSFSR 261
Cdd:PRK13651 261 ENNMEPPKLLNFVNKLE-KKGIDVPK 285
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-231 |
3.46e-47 |
|
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: 157.36 E-value: 3.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 19 TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---RDIYRKVGLVFQNpdDQLFA 95
Cdd:cd03258 18 VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelRKARRRIGMIFQH--FNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 T-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMG 174
Cdd:cd03258 96 SrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 175 EYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:cd03258 176 TQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-220 |
9.91e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.97 E-value: 9.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDG---TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP--RDIYR--KVGL 84
Cdd:COG1136 11 TKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEreLARLRrrHIGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQNPddQLFAT-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:COG1136 91 VFQFF--NLLPElTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSrGRLIR 220
Cdd:COG1136 169 DEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRD-GRIVS 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-227 |
1.09e-46 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 157.12 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKvGLV--FQNPddQLFA 95
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL-GIArtFQNP--RLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 T-TVFE---------------DAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHE 159
Cdd:COG0411 93 ElTVLEnvlvaaharlgrgllAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 160 ILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-227 |
1.31e-46 |
|
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: 155.80 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYK-----GEVLLDGENVLKLHPRDIY--RKVGLV 85
Cdd:cd03260 7 NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLElrRRVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNPDdqLFATTVFEDAAFGPRNMGCGD-AEVKTRVEAALASVDMAEFAGKGIH--NLSYGQKKRVCIAGLLAMGHEILL 162
Cdd:cd03260 87 FQKPN--PFPGSIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 163 LDEPTAGLDPMGEYRMMELLTRLNRDqgVTIVMATHSvdlvpifLHQ-------LHILSRGRLIRGGAPEEV 227
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHN-------MQQaarvadrTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-232 |
2.82e-46 |
|
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: 155.29 E-value: 2.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK-VGLVFQNPddQLFAT 96
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIP--RLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 -TVFE----------DAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:cd03219 90 lTVLEnvmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 166 PTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:cd03219 170 PAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
12-265 |
6.29e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 156.09 E-value: 6.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGT----VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKL----HPRDIYRKVG 83
Cdd:PRK13646 9 SYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkYIRPVRKRIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMA-EFAGKGIHNLSYGQKKRVCIAGLLAMGHEILL 162
Cdd:PRK13646 89 MVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 163 LDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLP 242
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHIGLP 248
|
250 260
....*....|....*....|...
gi 1948769844 243 HIAELIYQLKHEEGFSFSRLPLT 265
Cdd:PRK13646 249 EIVQLQYDFEQKYQTKLKDIALT 271
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-234 |
1.54e-45 |
|
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: 153.43 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY---RKVGLVFQnp 89
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlrRRMGMLFQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 DDQLF-ATTVFEDAAFGPRNMG-CGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPT 167
Cdd:cd03261 85 SGALFdSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 168 AGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDEL 234
Cdd:cd03261 165 AGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
14-251 |
1.99e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 155.78 E-value: 1.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEV----------LLDGENVLKLHPRDI----- 78
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkKNNHELITNPYSKKIknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 79 -YRKVGLVFQNPDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLLAM 156
Cdd:PRK13631 114 lRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 157 GHEILLLDEPTAGLDPMGEYRMMELLTRlNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELAN 236
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINS 272
|
250
....*....|....*
gi 1948769844 237 VKLRLPHIAELIYQL 251
Cdd:PRK13631 273 TSIQVPRVIQVINDL 287
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-252 |
2.96e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 154.10 E-value: 2.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDDQLFATTVFED 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 AAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMEL 181
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 182 LTRLNRDQGVTIVMATHSVDLVPIFlHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHIAELIYQLK 252
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAASS-DRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKDLR 252
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-231 |
7.47e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 154.92 E-value: 7.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVL-KLHPRDiyRKVGLVFQNPDdqLFA 95
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE--RRVGFVFQHYA--LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 -TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMG 174
Cdd:COG1118 89 hMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 175 EYRMMELLTRLNRDQGVTIVMATHSVD--------LVpiflhqlhILSRGRLIRGGAPEEVFTAP 231
Cdd:COG1118 169 RKELRRWLRRLHDELGGTTVFVTHDQEealeladrVV--------VMNQGRIEQVGTPDEVYDRP 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-218 |
1.38e-44 |
|
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: 150.33 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDG---TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDI--YR--KVGL 84
Cdd:cd03255 7 SKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaaFRrrHIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQNPddQLFAT-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:cd03255 87 VFQSF--NLLPDlTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHiLSRGRL 218
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIE-LRDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-231 |
1.98e-44 |
|
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: 150.46 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQNPddQL 93
Cdd:cd03300 8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNY--AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 94 FA-TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP 172
Cdd:cd03300 84 FPhLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 173 MGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:cd03300 164 KLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-227 |
2.06e-44 |
|
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: 150.80 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---RDIYRKVGLVFQNPD- 90
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalRQLRRQIGMIFQQFNl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 -DQLfatTVFED---AAFGPRN-----MGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:cd03256 90 iERL---SVLENvlsGRLGRRStwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 162 LLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-202 |
3.34e-44 |
|
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: 148.94 E-value: 3.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENvlkLHPRDIYRKVGLVFQNPDD 91
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFATTVFEDAAFGPRNMGcgdaEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:cd03226 83 QLFTDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 1948769844 172 pmgeYRMMELLTRLNRD---QGVTIVMATHSVDL 202
Cdd:cd03226 159 ----YKNMERVGELIRElaaQGKAVIVITHDYEF 188
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-231 |
6.28e-43 |
|
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: 146.68 E-value: 6.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDd 91
Cdd:cd03295 7 TKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 qLFA-TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDM--AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:cd03295 86 -LFPhMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 169 GLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-231 |
2.46e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 145.33 E-value: 2.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDdqlfa 95
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPY----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 ttvfedAAFGPR------------NMGCGDAEVktRVEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILL 162
Cdd:COG1124 90 ------ASLHPRhtvdrilaeplrIHGLPDREE--RIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 163 LDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:COG1124 162 LDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-227 |
2.79e-41 |
|
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: 142.69 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYpDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLhPRDIYRKVGLVFQNPDd 91
Cdd:COG4555 8 SKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGVLPDERG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 qLFAT-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:COG4555 85 -LYDRlTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 171 DPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:COG4555 164 DVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-227 |
3.02e-41 |
|
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: 150.75 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYP-DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQnpD 90
Cdd:COG2274 480 SFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQ--D 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEdaafgprNMGCGDAEV-KTRVEAALASVDMAEFAGK---GIH--------NLSYGQKKRVCIAGLLAMGH 158
Cdd:COG2274 558 VFLFSGTIRE-------NITLGDPDAtDEEIIEAARLAGLHDFIEAlpmGYDtvvgeggsNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 159 EILLLDEPTAGLDPMGEYRMMELLTRLnrDQGVTIVMATHSVDLVPIFlHQLHILSRGRLIRGGAPEEV 227
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEEL 696
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
21-233 |
6.11e-41 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 141.66 E-value: 6.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKV---MDGLIKGYK--GEVLLDGENVL--KLHPRDIYRKVGLVFQNPDdqL 93
Cdd:TIGR00972 16 ALKNINLDIPKNQVTALIGPSGCGKSTLLRSlnrMNDLVPGVRieGKVLFDGQDIYdkKIDVVELRRRVGMVFQKPN--P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 94 FATTVFEDAAFGPRNMGCGD-AEVKTRVEAALASVDMAEFAGKGIHN----LSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:TIGR00972 94 FPMSIYDNIAYGPRLHGIKDkKELDEIVEESLKKAALWDEVKDRLHDsalgLSGGQQQRLCIARALAVEPEVLLLDEPTS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 169 GLDPMGEYRMMELLTRLNRDqgVTIVMATHSV-------DLVPIFLhqlhilsRGRLIRGGAPEEVFTAPDE 233
Cdd:TIGR00972 174 ALDPIATGKIEELIQELKKK--YTIVIVTHNMqqaarisDRTAFFY-------DGELVEYGPTEQIFTNPKE 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-226 |
6.91e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 148.37 E-value: 6.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 3 DTRISVDLE--SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYR 80
Cdd:COG4988 332 AGPPSIELEdvSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 81 KVGLVFQNPddQLFATTVFEDAAFGprNMGCGDAEVktrvEAALASVDMAEFA-----------GKGIHNLSYGQKKRVC 149
Cdd:COG4988 412 QIAWVPQNP--YLFAGTIRENLRLG--RPDASDEEL----EAALEAAGLDEFVaalpdgldtplGEGGRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 150 IAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQgvTIVMATHSVDLVPIFLHQLHiLSRGRLIRGGAPEE 226
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILV-LDDGRIVEQGTHEE 557
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-226 |
2.13e-40 |
|
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: 139.81 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYpDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLV 85
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNP--DDQLfatTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:cd03265 79 FQDLsvDDEL---TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEE 226
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-218 |
9.95e-40 |
|
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: 137.54 E-value: 9.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDI---YRKVGLVFQnpDD 91
Cdd:cd03292 10 YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKIGVVFQ--DF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFAT-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:cd03292 88 RLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1948769844 171 DPMGEYRMMELLTRLNrDQGVTIVMATHSVDLVPIFLHQLHILSRGRL 218
Cdd:cd03292 168 DPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-231 |
1.59e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 140.71 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY---RKVGLVFQ 87
Cdd:PRK11153 10 VFPQGGRTIhALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarRQIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 --NpddQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:PRK11153 90 hfN---LLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 166 PTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-231 |
2.29e-39 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 138.55 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 11 ESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY----RKVGLVF 86
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRelrrKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 87 QNpddqlFA----TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILL 162
Cdd:cd03294 109 QS-----FAllphRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 163 LDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-233 |
3.09e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.48 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 3 DTRISVDLESYKYpDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKV---MDGLIKG--YKGEVLLDGENVL--KLHP 75
Cdd:COG1117 9 EPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPGarVEGEILLDGEDIYdpDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 76 RDIYRKVGLVFQ--NPddqlFATTVFEDAAFGPRNMGCGD-AEVKTRVEAALASV-----------DMAefagkgiHNLS 141
Cdd:COG1117 88 VELRRRVGMVFQkpNP----FPKSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAalwdevkdrlkKSA-------LGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 142 YGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDqgVTIVMATHSV-------DLVpIFLHQlhils 214
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMqqaarvsDYT-AFFYL----- 228
|
250
....*....|....*....
gi 1948769844 215 rGRLIRGGAPEEVFTAPDE 233
Cdd:COG1117 229 -GELVEFGPTEQIFTNPKD 246
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
27-218 |
3.85e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.10 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPddQLFATTVFE--DAAF 104
Cdd:COG4619 21 LTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEP--ALWGGTVRDnlPFPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 105 GPRNmgcgDAEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLT 183
Cdd:COG4619 99 QLRE----RKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLR 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 184 RLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRL 218
Cdd:COG4619 175 EYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-217 |
4.54e-39 |
|
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: 134.29 E-value: 4.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQnpdd 91
Cdd:cd00267 6 SFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 qlfattvfedaafgprnmgcgdaevktrveaalasvdmaefagkgihnLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1948769844 172 PMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGR 217
Cdd:cd00267 113 PASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-231 |
6.44e-39 |
|
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: 136.31 E-value: 6.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 20 VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQNPddQLFA-TTV 98
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHY--ALFRhMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 99 FEDAAFG----PRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMG 174
Cdd:cd03296 92 FDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 175 EYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:cd03296 172 RKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-233 |
7.16e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 139.06 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---RDIYRKVGLVFQ 87
Cdd:COG1135 10 TFPTKGGPVtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelRAARRKIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 NpdDQLFAT-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEP 166
Cdd:COG1135 90 H--FNLLSSrTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 167 TAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDE 233
Cdd:COG1135 168 TSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
27-218 |
8.82e-39 |
|
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: 133.68 E-value: 8.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLVFQNPddQLFAT-TVFEdaafg 105
Cdd:cd03230 21 LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEP--SLYENlTVRE----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 prNMgcgdaevktrveaalasvdmaefagkgihNLSYGQKKRVCIAglLAMGH--EILLLDEPTAGLDPMGEYRMMELLT 183
Cdd:cd03230 93 --NL-----------------------------KLSGGMKQRLALA--QALLHdpELLILDEPTSGLDPESRREFWELLR 139
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 184 RLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRL 218
Cdd:cd03230 140 EL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
15-227 |
9.31e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 135.89 E-value: 9.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY---RKVGLVFQ--NP 89
Cdd:TIGR02315 11 YPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRklrRRIGMIFQhyNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 DDQLfatTVFED---AAFGPRN-----MGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:TIGR02315 91 IERL---TVLENvlhGRLGYKPtwrslLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 162 LLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:TIGR02315 168 LADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-231 |
1.39e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 138.28 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 7 SVDLES-YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLV 85
Cdd:COG3839 3 SLELENvSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNPDdqLF-ATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:COG3839 81 FQSYA--LYpHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHsvDLVPIFL--HQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH--DQVEAMTlaDRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-168 |
1.13e-37 |
|
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: 130.46 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 25 MRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQnpDDQLF-ATTVFEDAA 103
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQ--DPQLFpRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 104 FGPRNMGCGDAEVKTRVEAALASVDMAEFA----GKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-233 |
1.82e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.43 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVL--KLHPRDIYRKVGLVFQNPdd 91
Cdd:COG1126 9 KSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQF-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFA-TTVFEDAAFGP---RNMGcgDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPT 167
Cdd:COG1126 87 NLFPhLTVLENVTLAPikvKKMS--KAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 168 AGLDP-M-GEyrMMELLTRLnRDQGVTIVMATH------SV-DLVpIFLHQlhilsrGRLIRGGAPEEVFTAPDE 233
Cdd:COG1126 165 SALDPeLvGE--VLDVMRDL-AKEGMTMVVVTHemgfarEVaDRV-VFMDG------GRIVEEGPPEEFFENPQH 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-203 |
2.59e-37 |
|
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: 130.38 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENV--LKLHPRDIYRKVGLVFQNPddQLFA 95
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIGMVFQDF--ALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 T-TVFEDAAFGprnmgcgdaevktrveaalasvdmaefagkgihnLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMG 174
Cdd:cd03229 90 HlTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180
....*....|....*....|....*....
gi 1948769844 175 EYRMMELLTRLNRDQGVTIVMATHSVDLV 203
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEA 164
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-230 |
3.86e-37 |
|
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: 132.13 E-value: 3.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLI-KGYKGEVLLDGENVLKLHPRDIYRKVGLVfqNPDDQLF- 94
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDVWELRKRIGLV--SPALQLRf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 95 --ATTVFE---DAAFG----PRNmgcGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLaMGH-EILLLD 164
Cdd:COG1119 92 prDETVLDvvlSGFFDsiglYRE---PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL-VKDpELLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSV-DLVPIFLHQLhILSRGRLIRGGAPEEVFTA 230
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVeEIPPGITHVL-LLKDGRVVAAGPKEEVLTS 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-217 |
4.34e-37 |
|
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: 129.43 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGL 84
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQNPddQLFATTVFEdaafgprNMgcgdaevktrveaalasvdmaefagkgihnLSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:cd03228 81 VPQDP--FLFSGTIRE-------NI------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLnrDQGVTIVMATHSVDLVPIFlHQLHILSRGR 217
Cdd:cd03228 122 EATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
15-222 |
4.86e-37 |
|
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: 130.78 E-value: 4.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGtVALAEMRLEIRRGeFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLVFQ--NPDDQ 92
Cdd:cd03264 10 YGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQefGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 93 LfatTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP 172
Cdd:cd03264 87 F---TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1948769844 173 MGEYRMMELLTRLNRDqgVTIVMATHSVDLVPIFLHQLHILSRGRLIRGG 222
Cdd:cd03264 164 EERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-231 |
9.14e-37 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 134.97 E-value: 9.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQnpDDQL-FAT 96
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ--DTSLsFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 TVFEDAAFG-----PRNMGCGDAEvKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PRK09536 93 DVRQVVEMGrtphrSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 172 PMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK09536 172 INHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-198 |
9.46e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.61 E-value: 9.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQNPddQ 92
Cdd:PRK09452 21 SKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQSY--A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 93 LFA-TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PRK09452 97 LFPhMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190
....*....|....*....|....*....|.
gi 1948769844 172 pmgeYRM---MEL-LTRLNRDQGVTIVMATH 198
Cdd:PRK09452 177 ----YKLrkqMQNeLKALQRKLGITFVFVTH 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-201 |
2.48e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 127.67 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 4 TRISVDLESYKYPDG---TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLklHP---Rd 77
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPgadR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 78 iyrkvGLVFQnpDDQLFA-TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAM 156
Cdd:COG4525 79 -----GVVFQ--KDALLPwLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1948769844 157 GHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVD 201
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
27-219 |
2.97e-35 |
|
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: 126.47 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPR---DIYRKVGLVFQNPDDQLFAT-TVFEDA 102
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRRKEIQMVFQDPMSSLNPRmTIGEQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 103 AFGPRNMGCGDAEVKTRVEAALASVDM---AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMM 179
Cdd:cd03257 106 AEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQIL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1948769844 180 ELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:cd03257 186 DLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
27-230 |
5.09e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 5.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPddQL-FATTVFEDAAFG 105
Cdd:PRK13548 23 LTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS--SLsFPFTVEEVVAMG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 PRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHE------ILLLDEPTAGLDPMGEYRMM 179
Cdd:PRK13548 101 RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLAHQHHVL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 180 ELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTA 230
Cdd:PRK13548 181 RLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-201 |
5.25e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 5.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQnpDDQLFA-TTVFEDAAFG 105
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQ--ENNLFPhLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 PRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRL 185
Cdd:COG3840 96 LRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDEL 175
|
170
....*....|....*.
gi 1948769844 186 NRDQGVTIVMATHSVD 201
Cdd:COG3840 176 CRERGLTVLMVTHDPE 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
17-212 |
5.76e-35 |
|
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: 124.90 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENvLKLHPRDIYRKVGLVFqnPDDQLFAT 96
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-IRDAREDYRRRLAYLG--HADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 -TVFEDAAFGPRNMGCGDAEvkTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:COG4133 90 lTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1948769844 176 YRMMELLTRLnRDQGVTIVMATHSVDLVPiFLHQLHI 212
Cdd:COG4133 168 ALLAELIAAH-LARGGAVLLTTHQPLELA-AARVLDL 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-219 |
8.37e-35 |
|
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: 124.92 E-value: 8.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGT-VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLVFQnpDDQ 92
Cdd:cd03263 9 TYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQ--FDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 93 LFAT-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:cd03263 86 LFDElTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1948769844 172 PMGEYRMMELLTRLNRdqGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:cd03263 166 PASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-231 |
9.52e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.80 E-value: 9.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGY-----KGEVLLDGENVLKLHPRDIYRKVGLVFQ--NPDDQLf 94
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQipNPIPNL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 95 atTVFEDAAFGPR--NMGCGDAEVKTRVEAALASVDMAEF--------AGKgihnLSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:PRK14247 98 --SIFENVALGLKlnRLVKSKKELQERVRWALEKAQLWDEvkdrldapAGK----LSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNRDqgVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-226 |
1.13e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 131.43 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPD 90
Cdd:COG4987 340 SFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 dqLFATTVFEDAAFGprNMGCGDAEVktrvEAALASVDMAEFA-----------GKGIHNLSYGQKKRVCIAGLLAMGHE 159
Cdd:COG4987 420 --LFDTTLRENLRLA--RPDATDEEL----WAALERVGLGDWLaalpdgldtwlGEGGRRLSGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 160 ILLLDEPTAGLDPMGEYRMMELLTRLNRDQgvTIVMATHSVDLVPIFlHQLHILSRGRLIRGGAPEE 226
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
17-231 |
1.31e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.41 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQNPddQLFA- 95
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSY--ALFPh 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 176 YRM-MELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK11607 186 DRMqLEVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-231 |
1.43e-34 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 124.76 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPrdIYRKVGLVFQNpdDQLFA-TTVFE 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP--EKRDISYVPQN--YALFPhMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 101 DAAFGPRNMGCGDAEVKTRVEaalasvDMAEFAGKGiH-------NLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPM 173
Cdd:cd03299 91 NIAYGLKKRKVDKKEIERKVL------EIAEMLGID-HllnrkpeTLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 174 GEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-222 |
2.06e-34 |
|
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: 123.85 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 5 RISVDLESYKYPDG-TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVG 83
Cdd:cd03245 2 RIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNPddQLFATTVFEDAAfgprnMGCGDAEVKTRVEAA-LASVDmaEFA-----------GKGIHNLSYGQKKRVCIA 151
Cdd:cd03245 82 YVPQDV--TLFYGTLRDNIT-----LGAPLADDERILRAAeLAGVT--DFVnkhpngldlqiGERGRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 152 GLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQgvTIVMATHS---VDLVpiflHQLHILSRGRLIRGG 222
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRpslLDLV----DRIIVMDSGRIVADG 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-212 |
1.15e-33 |
|
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: 121.87 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIY---RKVGLVFQNPD 90
Cdd:cd03262 8 KSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINelrQKVGMVFQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 dqLFA-TTVFEDAAFGPRNM-GCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:cd03262 87 --LFPhLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 169 GLDP--MGEyrMMELLTRLNRDqGVTIVMATHSV-------DLVpIFLHQLHI 212
Cdd:cd03262 165 ALDPelVGE--VLDVMKDLAEE-GMTMVVVTHEMgfarevaDRV-IFMDDGRI 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-230 |
3.54e-33 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 122.02 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 4 TRISVDLESYKYPDGTVAlAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVG 83
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQN---PDDqlfaTTVFEDAAFG--PRN--MGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAM 156
Cdd:PRK10253 85 LLAQNattPGD----ITVQELVARGryPHQplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 157 GHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTA 230
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
21-232 |
8.92e-33 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 120.09 E-value: 8.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENvLKLHPRDIYRKVGLVFQNP--DDQLfatTV 98
Cdd:TIGR03864 16 ALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHD-LRRAPRAALARLGVVFQQPtlDLDL---SV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 99 FEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRM 178
Cdd:TIGR03864 92 RQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVGLDPASRAAI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 179 MELLTRLNRDQGVTIVMATHSVDLVPIfLHQLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:TIGR03864 172 TAHVRALARDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLADGAAAELRGATG 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-231 |
1.28e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 122.88 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQNPddQL 93
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHY--AL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 94 FA-TTVFEDAAFG----PRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:PRK10851 86 FRhMTVFDNIAFGltvlPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 169 GLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
5-222 |
3.91e-32 |
|
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: 117.78 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 5 RISVDLEsYKYPDGTVALAemrLEIRrGEFTGILGSNGSGKTTLLKVMDGLIKGYKGE------VLLDGENVLKLHPRDi 78
Cdd:cd03297 1 MLCVDIE-KRLPDFTLKID---FDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtVLFDSRKKINLPPQQ- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 79 yRKVGLVFQNpdDQLFA-TTVFEDAAFGPRnmGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMG 157
Cdd:cd03297 75 -RKIGLVFQQ--YALFPhLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 158 HEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGG 222
Cdd:cd03297 150 PELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-227 |
5.39e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 117.92 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK-VGLVFQnpDDQLFAT 96
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPE--GRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 -TVFED---AAFGPRnmgcgDAEVKTRVEAALasvDM----AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:cd03224 90 lTVEENlllGAYARR-----RAKRKARLERVY---ELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 169 GLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:cd03224 162 GLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-245 |
7.47e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.89 E-value: 7.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 19 TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVL--KLHPRDIYRKVGLVFQNPDdqLFA- 95
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFY--LFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVFEDAAFGPRNM-GCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPmg 174
Cdd:PRK09493 92 LTALENVMFGPLRVrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP-- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 175 EYRmMELLTRLNR--DQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPdelANVKLR--LPHIA 245
Cdd:PRK09493 170 ELR-HEVLKVMQDlaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP---PSQRLQefLQHVS 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-198 |
1.09e-31 |
|
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: 116.59 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQNpddq 92
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQN---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 93 lFA----TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:cd03301 81 -YAlyphMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190
....*....|....*....|....*....|
gi 1948769844 169 GLDPMGEYRMMELLTRLNRDQGVTIVMATH 198
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTH 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-199 |
1.53e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 119.77 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPdd 91
Cdd:TIGR02868 341 SAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDA-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFATTVFEDAAFGprNMGCGDAEvktrVEAALASVDMAEFA-----------GKGIHNLSYGQKKRVCIAGLLAMGHEI 160
Cdd:TIGR02868 419 HLFDTTVRENLRLA--RPDATDEE----LWAALERVGLADWLralpdgldtvlGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 1948769844 161 LLLDEPTAGLDPMGEYRMMELLtrLNRDQGVTIVMATHS 199
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
29-219 |
2.96e-30 |
|
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: 112.26 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIKGY--KGEVLLDGENvlkLHPRDIYRKVGLVFQnpDDQLFAT-TVFEdaafg 105
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRP---LDKRSFRKIIGYVPQ--DDILHPTlTVRE----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 prnmgcgdaevktrveaALasvdmaEFAGKgIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRL 185
Cdd:cd03213 102 -----------------TL------MFAAK-LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1948769844 186 nRDQGVTIVMATH--SVDLVPIFlHQLHILSRGRLI 219
Cdd:cd03213 158 -ADTGRTIICSIHqpSSEIFELF-DKLLLLSQGRVI 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-203 |
5.72e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.56 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGEnvlklhprdiyRKVGLVFQNPD-DQLFA 95
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEvPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVFEDAAFG--PRNMGCG--DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:NF040873 72 LTVRDLVAMGrwARRGLWRrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|..
gi 1948769844 172 PMGEYRMMELLTRLnRDQGVTIVMATHSVDLV 203
Cdd:NF040873 152 AESRERIIALLAEE-HARGATVVVVTHDLELV 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-199 |
2.35e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 116.23 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 5 RISVDLESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGL 84
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQNPddQLFATTVFEDAAFgprnmGCGDAEVkTRVEAALASVDMAEF-----------AGKGIHNLSYGQKKRVCIAGL 153
Cdd:TIGR02857 401 VPQHP--FLFAGTIAENIRL-----ARPDASD-AEIREALERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1948769844 154 LAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNrdQGVTIVMATHS 199
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHR 516
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-219 |
3.49e-29 |
|
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: 110.00 E-value: 3.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHprDIYRKVGLVFQNPddQLFAT-TVF 99
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGALIEAP--GFYPNlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 100 EDAAFGPRNMGCGDAevktRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMM 179
Cdd:cd03268 91 ENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1948769844 180 ELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:cd03268 167 ELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-230 |
4.43e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.87 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQN---PDD 91
Cdd:PRK11231 12 YGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHhltPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 qlfaTTVFEDAAFG--PRNMGCG--DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPT 167
Cdd:PRK11231 91 ----ITVRELVAYGrsPWLSLWGrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 168 AGLDPMGEYRMMELLTRLNrDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTA 230
Cdd:PRK11231 167 TYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-198 |
5.99e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.26 E-value: 5.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPdd 91
Cdd:COG1132 346 SFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDT-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFATTVFEDAAFGprNMGCGDAEvktrVEAALASVDMAEFA-----------GKGIHNLSYGQKKRVCIAGLLAMGHEI 160
Cdd:COG1132 424 FLFSGTIRENIRYG--RPDATDEE----VEEAAKAAQAHEFIealpdgydtvvGERGVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 1948769844 161 LLLDEPTAGLDPMGEYRMMELLTRLNRdqGVTIVMATH 198
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMK--GRTTIVIAH 533
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-226 |
7.42e-29 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 111.71 E-value: 7.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLVFQ--NPDD 91
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQyaSVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLfatTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:TIGR01188 80 DL---TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 172 PMGEYRMMELLTRLNrDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEE 226
Cdd:TIGR01188 157 PRTRRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-222 |
1.29e-28 |
|
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: 108.73 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQnpDDQLFA-TTVFEDAAFG 105
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQ--ENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 pRNMGCG-DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTR 184
Cdd:cd03298 95 -LSPGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1948769844 185 LNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGG 222
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-222 |
1.93e-28 |
|
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: 108.22 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 20 VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLVFQNpdDQLFA-TTV 98
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDS--TGLYDrLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 99 FEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRM 178
Cdd:cd03266 96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1948769844 179 MELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGG 222
Cdd:cd03266 176 REFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-227 |
3.16e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.81 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDI---------YRK--V 82
Cdd:COG4152 9 KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgylpeerglYPKmkV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 83 GlvfqnpdDQLfattVFedaaFGPRNmGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAmgH--EI 160
Cdd:COG4152 89 G-------EQL----VY----LARLK-GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL--HdpEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 161 LLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-232 |
4.36e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIK-----GYKGEVLLDGENVL--KLHPRDIYRKVGLVFQ--NPDDQLfatT 97
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYspDVDPIEVRREVGMVFQypNPFPHL---T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 98 VFEDAAFGPR--NMGCGDAEVKTRVEAALASVDMAEFAGKGIH----NLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PRK14267 102 IYDNVAIGVKlnGLVKSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 172 PMGEYRMMELLTRLNRDqgVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:PRK14267 182 PVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-231 |
6.83e-28 |
|
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: 109.37 E-value: 6.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGY---KGEVLLDGENVLKLHPRDI----YRKVG 83
Cdd:COG0444 10 YFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELrkirGREIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNPddqlfattvfeDAAFGPR-------------NMGCGDAEVKTRVEAALASV---DMAEFAGKGIHNLSYGQKKR 147
Cdd:COG0444 90 MIFQDP-----------MTSLNPVmtvgdqiaeplriHGGLSKAEARERAIELLERVglpDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 148 VCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpiflhqLHILSR------GRLIRG 221
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVV------AEIADRvavmyaGRIVEE 232
|
250
....*....|
gi 1948769844 222 GAPEEVFTAP 231
Cdd:COG0444 233 GPVEELFENP 242
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-202 |
1.30e-27 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 106.36 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTRISVDLESYKYPDGT---VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENvlkLHPRD 77
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD---LFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 78 -------IYRKVGLVFQNpdDQLFAT-TVFEdaafgprNMGC-----GDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQ 144
Cdd:COG4181 81 edararlRARHVGFVFQS--FQLLPTlTALE-------NVMLplelaGRRDARARARALLERVGLGHRLDHYPAQLSGGE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 145 KKRVCIAGLLAMGHEILLLDEPTAGLD-PMGEyRMMELLTRLNRDQGVTIVMATHSVDL 202
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDaATGE-QIIDLLFELNRERGTTLVLVTHDPAL 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-198 |
1.32e-27 |
|
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: 104.99 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGT-VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGL 84
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQnpDDQLFATTVFEdaafgprNMgcgdaevktrveaalasvdmaefagkgihnLSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:cd03246 81 LPQ--DDELFSGSIAE-------NI------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190
....*....|....*....|....*....|....
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATH 198
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL-KAAGATRIVIAH 154
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-231 |
1.80e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.18 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 3 DTRISVDLESYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKV 82
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 83 GLVFQnpddQLFAT---TVFEDAAFG--PRNMGCG--DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLA 155
Cdd:PRK10575 88 AYLPQ----QLPAAegmTVRELVAIGryPWHGALGrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 156 MGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
27-232 |
2.24e-27 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 106.42 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENV-------LKLHPRD------IYRKVGLVFQNPDdqL 93
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPADrrqlqrIRTRLGMVFQSFN--L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 94 FA-TTVFEDAAFGPRN-MGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:COG4598 107 WShMTVLENVIEAPVHvLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 172 P--MGE-YRMMELLTrlnrDQGVTIVMATHSVDL-------VpIFLHQlhilsrGRLIRGGAPEEVFTAPD 232
Cdd:COG4598 187 PelVGEvLKVMRDLA----EEGRTMLVVTHEMGFardvsshV-VFLHQ------GRIEEQGPPAEVFGNPK 246
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-219 |
3.34e-27 |
|
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: 103.28 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD-IYRKVGLVFQnpddqlfat 96
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 tvfedaafgprnmgcgdaevktrveaalasvdmaefagkgihnLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEY 176
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1948769844 177 RMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:cd03216 120 RLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-222 |
3.72e-27 |
|
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: 104.67 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 19 TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDI---------YRKVglvfqnp 89
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpeerglYPKM------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 ddqlfatTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAG 169
Cdd:cd03269 86 -------KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 170 LDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGG 222
Cdd:cd03269 159 LDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
27-232 |
1.57e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.52 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK-VGLVFQnpDDQLFAT-TVFEdaaf 104
Cdd:COG0410 24 LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPE--GRRIFPSlTVEE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 105 gprN--MGCGDAEVKTRVEAALASV-----DMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYR 177
Cdd:COG0410 98 ---NllLGAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 178 MMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:COG0410 175 IFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-218 |
2.22e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 103.66 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK-VGLVFQNPddqlfa 95
Cdd:COG4674 21 DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLgIGRKFQKP------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 tTVFED---------AAFGPRN-----MGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:COG4674 95 -TVFEEltvfenlelALKGDRGvfaslFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 162 LLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVmaTHSVDLVPIF------LHQLHILSRGRL 218
Cdd:COG4674 174 LLDEPVAGMTDAETERTAELLKSLAGKHSVVVV--EHDMEFVRQIarkvtvLHQGSVLAEGSL 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-222 |
2.58e-26 |
|
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: 103.18 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 20 VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIyRKVGLVFQNPDDQLFATTVF 99
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-RRIGVVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 100 EDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMM 179
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1948769844 180 ELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGG 222
Cdd:cd03267 194 NFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-230 |
3.60e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 103.81 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTRISVDLESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIyr 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 81 kVGLVFQNPD-DQLFATTVfEDAAFGPR--NMGC---GDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLL 154
Cdd:PRK15056 80 -VAYVPQSEEvDWSFPVLV-EDVVMMGRygHMGWlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 155 AMGHEILLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLhQLHILSRGRLIRGGAPEEVFTA 230
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFC-DYTVMVKGTVLASGPTETTFTA 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-231 |
5.31e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.19 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYpDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKgYKGEVLLDGEnvLKLHPRDIY------ 79
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGR--VEFFNQNIYerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 80 ----RKVGLVFQNPDdqLFATTVFEDAAFGPRNMGC-GDAEVKTRVEAALASVDMAEFAGKGIH----NLSYGQKKRVCI 150
Cdd:PRK14258 84 nrlrRQVSMVHPKPN--LFPMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 151 AGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSvdlvpifLHQLHILSR------------GRL 218
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN-------LHQVSRLSDftaffkgnenriGQL 234
|
250
....*....|...
gi 1948769844 219 IRGGAPEEVFTAP 231
Cdd:PRK14258 235 VEFGLTKKIFNSP 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
27-234 |
6.21e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.80 E-value: 6.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLK--LHPRDIYrkvgLVFQNPddQLFA-TTVFEDAA 103
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsIQQRDIC----MVFQSY--ALFPhMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 104 FGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLT 183
Cdd:PRK11432 101 YGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 184 RLNRDQGVTIVMATHsvDLVPIFL--HQLHILSRGRLIRGGAPEEVFTAPDEL 234
Cdd:PRK11432 181 ELQQQFNITSLYVTH--DQSEAFAvsDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-231 |
6.30e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 6.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGY------KGEVLLDGENVLKLHPRDIYRKVGLVF 86
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskikvDGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 87 QNPdDQLFATTVFEDAAFGPRNMGCGDA-EVKTRVEAALASVDMaefaGKGIHN--------LSYGQKKRVCIAGLLAMG 157
Cdd:PRK14246 97 QQP-NPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGL----WKEVYDrlnspasqLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 158 HEILLLDEPTAGLDPMGEYRMMELLTRLNRDqgVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-235 |
7.46e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.55 E-value: 7.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 20 VALAEMRLEIRRGEFTGILGSNGSGKTTLLKV---MDGLIKGYK--GEVLLDGENVL--KLHPRDIYRKVGLVFQNPDDq 92
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRveGKVTFHGKNLYapDVDPVEVRRRIGMVFQKPNP- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 93 lFATTVFEDAAFGPRNMGC-GDA-EVKTRV--EAALASVDMAEFAGKGIhNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:PRK14243 103 -FPKSIYDNIAYGARINGYkGDMdELVERSlrQAALWDEVKDKLKQSGL-SLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 169 GLDPMGEYRMMELLTRLNRDqgVTIVMATHSV-------DLVPIFLHQLHILSR--GRLIRGGAPEEVFTAPDELA 235
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQ--YTIIIVTHNMqqaarvsDMTAFFNVELTEGGGryGYLVEFDRTEKIFNSPQQQA 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-231 |
1.35e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKV---MDGLIK--GYKGEVLLDGENVLKlhPR----DIYRKVGLVFQNPDD 91
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPevTITGSIVYNGHNIYS--PRtdtvDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 qlFATTVFEDAAFGPRNMGCGDAEV-KTRVEAALASVDMAEFAGKGIHN----LSYGQKKRVCIAGLLAMGHEILLLDEP 166
Cdd:PRK14239 98 --FPMSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 167 TAGLDPMGEYRMMELLTRLNRDqgVTIVMATHSV-------DLVPIFLHqlhilsrGRLIRGGAPEEVFTAP 231
Cdd:PRK14239 176 TSALDPISAGKIEETLLGLKDD--YTMLLVTRSMqqasrisDRTGFFLD-------GDLIEYNDTKQMFMNP 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-201 |
1.48e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.94 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPrDIYRK-VGLVFQNPddQLFA 95
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQqVSYCAQTP--TLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVFEDAAFgPRNMGcGDAEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMG 174
Cdd:PRK10247 95 DTVYDNLIF-PWQIR-NQQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180
....*....|....*....|....*..
gi 1948769844 175 EYRMMELLTRLNRDQGVTIVMATHSVD 201
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-201 |
1.56e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.70 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 4 TRISVDlesykYPdGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVlklhpRDIYRKVG 83
Cdd:PRK11248 5 SHLYAD-----YG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNpDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:PRK11248 74 VVFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVD 201
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-232 |
1.82e-25 |
|
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: 103.26 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 24 EMRLEIRRGEF-------------TGILGSNGSGKTTLLKVMDGLIK---GY---KGEVLLDGENVLKLHPRDiyRKVGL 84
Cdd:COG4148 4 EVDFRLRRGGFtldvdftlpgrgvTALFGPSGSGKTTLLRAIAGLERpdsGRirlGGEVLQDSARGIFLPPHR--RRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQnpDDQLFAT-TVFEDAAFGPRNmgCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:COG4148 82 VFQ--EARLFPHlSVRGNLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVpifLH---QLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEV---ARladHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-226 |
3.52e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.86 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYK---GEVLLDGENVLKLH--PRDIYR---KVGLVFQ--NPD 90
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGrlARDIRKsraNTGYIFQqfNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLfatTVFEDAAFGPrnMGCG----------DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEI 160
Cdd:PRK09984 99 NRL---SVLENVLIGA--LGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 161 LLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEE 226
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-222 |
4.26e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 98.54 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPD-GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHpRDIYRKVGLVFQNPd 90
Cdd:cd03247 7 SFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 dQLFATTVFEdaafgprNMGcgdaevktrveaalasvdmAEFAGkgihnlsyGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:cd03247 85 -YLFDTTLRN-------NLG-------------------RRFSG--------GERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 171 DPMGEYRMMELLTRLNRDQgvTIVMATHSVDLVPIFlHQLHILSRGRLIRGG 222
Cdd:cd03247 130 DPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-236 |
6.33e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.57 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD-IYRKVGLVFQNPddQLFAT 96
Cdd:COG3845 17 GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHF--MLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 -TVFEDAAFG--PRNMGCGD-AEVKTRVEAALA----SVDMAEFagkgIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:COG3845 95 lTVAENIVLGlePTKGGRLDrKAARARIRELSEryglDVDPDAK----VEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 169 GLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEvfTAPDELAN 236
Cdd:COG3845 171 VLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE--TSEEELAE 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-236 |
7.42e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 9 DLESYKyPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKgYKGEVLLDGENVLKLHPRDIYRKVGLVFQN 88
Cdd:PRK11174 354 DLEILS-PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKHLSWVGQN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 PddQLFATTVFEDAAFGPRNMGcgdaevKTRVEAALASVDMAEFA-----------GKGIHNLSYGQKKRVCIAGLLAMG 157
Cdd:PRK11174 432 P--QLPHGTLRDNVLLGNPDAS------DEQLQQALENAWVSEFLpllpqgldtpiGDQAAGLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 158 HEILLLDEPTAGLDPMGEYRMMELLTRLNRDQgvTIVMATHSVDlvpiFLHQL-HIL--SRGRLIRGGAPEEVFTAPDEL 234
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLE----DLAQWdQIWvmQDGQIVQQGDYAELSQAGGLF 577
|
..
gi 1948769844 235 AN 236
Cdd:PRK11174 578 AT 579
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-231 |
7.55e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 103.61 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKgYKGEVLLDGENVLKLHPRD---IYRKVGLVFQNPddqlfattvFedAA 103
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP---------F--GS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 104 FGPR--------------NMGCGDAEVKTRVEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:COG4172 375 LSPRmtvgqiiaeglrvhGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 169 GLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:COG4172 455 ALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-232 |
1.53e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.91 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKvGLV--FQNPddQLFA 95
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVrtFQHV--RLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 T-TVFEDAAFGP-RNMGCG--------------DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHE 159
Cdd:PRK11300 94 EmTVIENLLVAQhQQLKTGlfsgllktpafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 160 ILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-231 |
1.58e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.89 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTRISVDLESYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYR 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEV-LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 81 KVG-------------LVFQNPDDQLFaTTVFEDAAFGP-RNMGCGDAEVKTRVEAALASVDMAEFA-GKGIHNLSYGQK 145
Cdd:PRK10619 80 KVAdknqlrllrtrltMVFQHFNLWSH-MTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 146 KRVCIAGLLAMGHEILLLDEPTAGLDP--MGE-YRMMELLTrlnrDQGVTIVMATHSVDLVP------IFLHQlhilsrG 216
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPelVGEvLRIMQQLA----EEGKTMVVVTHEMGFARhvsshvIFLHQ------G 228
|
250
....*....|....*
gi 1948769844 217 RLIRGGAPEEVFTAP 231
Cdd:PRK10619 229 KIEEEGAPEQLFGNP 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-198 |
2.11e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK-VGLVFQNPDdqLFAT 96
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELN--LVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 -TVFEDAAFG--PRNMGCGD-AEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP 172
Cdd:COG1129 94 lSVAENIFLGrePRRGGLIDwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180
....*....|....*....|....*.
gi 1948769844 173 MGEYRMMELLTRLnRDQGVTIVMATH 198
Cdd:COG1129 174 REVERLFRIIRRL-KAQGVAIIYISH 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-237 |
6.45e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.22 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGyKGEVLLDGENVLKLHPRDIYRKVGLVFQNpDDQLFATTVFEDAAFG- 105
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQ-QSPPFAMPVFQYLALHq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 PRnmGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGH-------EILLLDEPTAGLDPMGEYRM 178
Cdd:COG4138 95 PA--GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWptinpegQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 179 MELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTaPDELANV 237
Cdd:COG4138 173 DRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PENLSEV 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-231 |
1.04e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.34 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 19 TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---RDIYRK-VGLVFQNpddqlF 94
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKkIAMVFQS-----F 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 95 A----TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:PRK10070 116 AlmphMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 171 DPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-221 |
1.75e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.33 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDI---YRKVGLVFQN 88
Cdd:PRK10908 8 SKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 pDDQLFATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:PRK10908 88 -HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 169 GLDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRG 221
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-228 |
2.35e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 94.98 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLhPRDIYRK-VGLVFQnpD 90
Cdd:cd03254 9 NFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSmIGVVLQ--D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFGpRNmgcgDAEvKTRVEAALASVDMAEF-----------AGKGIHNLSYGQKKRVCIAGLLAMGHE 159
Cdd:cd03254 86 TFLFSGTIMENIRLG-RP----NAT-DEEVIEAAKEAGAHDFimklpngydtvLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 160 ILLLDEPTAGLDPMGEYRMMELLTRLNrdQGVTIVMATH------SVDLVpIFLHQlhilsrGRLIRGGAPEEVF 228
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHrlstikNADKI-LVLDD------GKIIEEGTHDELL 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-199 |
3.77e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.17 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 32 GEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGlvfqnPDDQLFAT-TVFEDAAFGPRNMG 110
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG-----HRNAMKPAlTVAENLEFWAAFLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 111 CGDaevkTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRlNRDQG 190
Cdd:PRK13539 103 GEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-HLAQG 177
|
....*....
gi 1948769844 191 VTIVMATHS 199
Cdd:PRK13539 178 GIVIAATHI 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-219 |
6.44e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.75 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKL---HPRDIYRKVGLVFQNPD 90
Cdd:PRK10419 21 KHQHQTV-LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 dqlfattvfedAAFGPRN-------------MGCGDAEVKTRVEAALASVDMA-EFAGKGIHNLSYGQKKRVCIAGLLAM 156
Cdd:PRK10419 100 -----------SAVNPRKtvreiireplrhlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 157 GHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-219 |
6.76e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 94.87 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---RDIYRKVGLVFQNPDDQLFATTV 98
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 99 FEDAAFGP-RNMGCGD-AEVKTRVEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:TIGR02769 107 VRQIIGEPlRHLTSLDeSEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1948769844 176 YRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-228 |
1.06e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 97.51 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 5 RISVDLESYKYPDGTVA-LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVG 83
Cdd:COG4618 330 RLSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNPddQLFATTVFEDAAfgpRnMGCGDAE-VktrVEAA-LASV-DM-AEFA-------GKGIHNLSYGQKKRVCIAg 152
Cdd:COG4618 410 YLPQDV--ELFDGTIAENIA---R-FGDADPEkV---VAAAkLAGVhEMiLRLPdgydtriGEGGARLSGGQRQRIGLA- 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 153 lLAM-GH-EILLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIfLHQLHILSRGRLIRGGAPEEVF 228
Cdd:COG4618 480 -RALyGDpRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
21-219 |
1.41e-22 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 92.85 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGenvlklHP--RDIYRKVGLVFQNPddQLFAT-T 97
Cdd:TIGR03740 15 AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG------HPwtRKDLHKIGSLIESP--PLYENlT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 98 VFEDAAFGPRNMGCGDaevkTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYR 177
Cdd:TIGR03740 87 ARENLKVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1948769844 178 MMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:TIGR03740 163 LRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-230 |
2.22e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.10 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLV--FQNPDD 91
Cdd:PRK13537 16 RYGDKLV-VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVpqFDNLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLfatTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PRK13537 94 DF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 172 PMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTA 230
Cdd:PRK13537 171 PQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-198 |
2.79e-22 |
|
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: 91.65 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLhpRDIYRKVGLVFQNPDDQLFAT 96
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ--RDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 TVFEDAAFGPRNmgCGDAEVKtrVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEY 176
Cdd:TIGR01189 89 SALENLHFWAAI--HGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|..
gi 1948769844 177 RMMELLtRLNRDQGVTIVMATH 198
Cdd:TIGR01189 165 LLAGLL-RAHLARGGIVLLTTH 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-222 |
4.56e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 91.56 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYK---GEVLLDGEnvlKLHPRDIYRKVGLVFQnpDDQLFAT-TVFEDA 102
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPDQFQKCVAYVRQ--DDILLPGlTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 103 AFGP--RNMGCGDAEVKTRVEAALASVDMA--EFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRM 178
Cdd:cd03234 103 TYTAilRLPRKSSDAIRKKRVEDVLLRDLAltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1948769844 179 MELLTRLNRdQGVTIVMATHS--VDLVPIFLHQLhILSRGRLIRGG 222
Cdd:cd03234 183 VSTLSQLAR-RNRIVILTIHQprSDLFRLFDRIL-LLSSGEIVYSG 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
27-232 |
4.83e-22 |
|
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: 91.84 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHprdIYRK--VGLVFQNPDDQLFAT-TVFEDAA 103
Cdd:cd03218 21 LSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP---MHKRarLGIGYLPQEASIFRKlTVEENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 104 FGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLT 183
Cdd:cd03218 98 AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1948769844 184 RLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:cd03218 178 IL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-230 |
6.48e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 91.39 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKY-PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGL 84
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQnpDDQLFATTVFEDAAFGPRNMGcgdaevKTRVEAALASVDMAEF-----------AGKGIHNLSYGQKKRVCIAGL 153
Cdd:cd03252 81 VLQ--ENVLFNRSIRDNIALADPGMS------MERVIEAAKLAGAHDFiselpegydtiVGEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 154 LAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNrdQGVTIVMATHSVDLVPIfLHQLHILSRGRLIRGGAPEEVFTA 230
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-196 |
1.04e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 91.06 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPD--GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKvmdgLIKGY----KGEVLLDGENVLKLHPRDIYRKVGLV 85
Cdd:cd03249 7 SFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVS----LLERFydptSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNPddQLFATTVFEDAAFGpRNmgcgDAEVKTRVEAA-LASVDmaEF-----------AGKGIHNLSYGQKKRVCIAGL 153
Cdd:cd03249 83 SQEP--VLFDGTIAENIRYG-KP----DATDEEVEEAAkKANIH--DFimslpdgydtlVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1948769844 154 LAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQgVTIVMA 196
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR-TTIVIA 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-216 |
1.32e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENV-LKLHP-----RDIYRKVGLVFQN----PD 90
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdFSKTPsdkaiRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 dqlfaTTVFEDAAFGP-RNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAG 169
Cdd:PRK11124 97 -----LTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 170 LDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVP------IFLHQLHILSRG 216
Cdd:PRK11124 172 LDPEITAQIVSIIREL-AETGITQVIVTHEVEVARktasrvVYMENGHIVEQG 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-232 |
2.00e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.98 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 23 AEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY---RKVGLVFQNpdDQLFA-TTV 98
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvrKRMSMLFQS--GALFTdMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 99 FEDAAFGPR-NMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYR 177
Cdd:PRK11831 102 FDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 178 MMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPD 232
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-198 |
2.40e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.65 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVlklHPRDI--YRKVGL------------VFQNPD-- 90
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIatRRRVGYmsqafslygeltVRQNLElh 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFattvfedaafgprnmGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAglLAMGH--EILLLDEPTA 168
Cdd:NF033858 364 ARLF---------------HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA--VAVIHkpELLILDEPTS 426
|
170 180 190
....*....|....*....|....*....|
gi 1948769844 169 GLDPMGEYRMMELLTRLNRDQGVTIVMATH 198
Cdd:NF033858 427 GVDPVARDMFWRLLIELSREDGVTIFISTH 456
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-231 |
2.63e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.07 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENV---LKLHPRDIY---RKVGLVFQN----PD 90
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRllrQKVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 dqlfaTTVFEDAAFGP-RNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAG 169
Cdd:COG4161 97 -----LTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 170 LDPMGEYRMMELLTRLNrDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGApEEVFTAP 231
Cdd:COG4161 172 LDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQP 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-198 |
3.43e-21 |
|
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: 88.70 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlhPRDIYRKVGLVFQNPDDQLFAT 96
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--QRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 TVFEDAAFGPRNmgCGDAEVktrvEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEY 176
Cdd:cd03231 89 SVLENLRFWHAD--HSDEQV----EEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|..
gi 1948769844 177 RMMELLtRLNRDQGVTIVMATH 198
Cdd:cd03231 163 RFAEAM-AGHCARGGMVVLTTH 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-231 |
5.04e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 89.22 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGyKGEVLLDGENVLKLHPRDIYRKVGLVFQNpDDQLFATTVFED 101
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQ-QTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 -AAFGPRnmGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGH-------EILLLDEPTAGLDPM 173
Cdd:PRK03695 90 lTLHQPD--KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWpdinpagQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 174 GEYRMMELLTRLNRdQGVTIVMATHSVDLVpifLHQLH---ILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK03695 168 QQAALDRLLSELCQ-QGIAVVMSSHDLNHT---LRHADrvwLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-198 |
5.70e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 92.34 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiYRkvglvfqnpdd 91
Cdd:PRK10522 329 TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED-YR----------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFAtTVFEDAAFGPRNMGC-GDAEVKTRVEAALASVDMA---EFAGKGIHN--LSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:PRK10522 397 KLFS-AVFTDFHLFDQLLGPeGKPANPALVEKWLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190
....*....|....*....|....*....|....*.
gi 1948769844 166 PTAGLDPMGE---YRmmELLTRLnRDQGVTIVMATH 198
Cdd:PRK10522 476 WAADQDPHFRrefYQ--VLLPLL-QEMGKTIFAISH 508
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-201 |
6.65e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 25 MR--LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQnpDDQLFATTVFEda 102
Cdd:PRK10771 16 MRfdLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQ--ENNLFSHLTVA-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 103 afgpRNMGCG-------DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:PRK10771 90 ----QNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180
....*....|....*....|....*.
gi 1948769844 176 YRMMELLTRLNRDQGVTIVMATHSVD 201
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLE 191
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-218 |
8.26e-21 |
|
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: 88.30 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPD--GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNP 89
Cdd:cd03248 18 TFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 ddQLFATTVFEDAAFGPRnmGCGDAEVKTRVEAALASVDMAEF-------AGKGIHNLSYGQKKRVCIAGLLAMGHEILL 162
Cdd:cd03248 98 --VLFARSLQDNIAYGLQ--SCSFECVKEAAQKAHAHSFISELasgydteVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 163 LDEPTAGLDPMGEYRMMELLTRLNRDQgvTIVMATHSVDLVPiFLHQLHILSRGRL 218
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-231 |
9.09e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 9.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGL---IKGYK--GEVLLDGENVLKLhpRDIY---RKVGLVFQNP 89
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkVSGYRysGDVLLGGRSIFNY--RDVLefrRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 DDqlFATTVFEDAAFGPR-NMGCGDAEVKTRVEAALASVDMAEFAGKGIHN----LSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:PRK14271 111 NP--FPMSIMDNVLAGVRaHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNrdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-224 |
2.53e-20 |
|
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: 90.84 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVlKLHPRDIYRKVGLVFQNpdDQLF- 94
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQH--NILFh 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 95 ATTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMG 174
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1948769844 175 EYRMMELLtrLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAP 224
Cdd:TIGR01257 1097 RRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-235 |
2.61e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.96 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKG--------YKGEVLLDGENVLKLHPRDIYRKVGLVFQn 88
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 PDDQLFATTVFEDAAFG--PRNMGCGDAEVKTR--VEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAM-------- 156
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGryPHARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 157 -GHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTaPDELA 235
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAHIA 249
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-219 |
3.07e-20 |
|
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: 86.43 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLhprdiyrKVGLVFQNpddqlfATTVFEDAAFGP 106
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-------GLGGGFNP------ELTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 107 RNMGCGDAEVKTRVEaalasvDMAEFAGKG------IHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMME 180
Cdd:cd03220 110 RLLGLSRKEIDEKID------EIIEFSELGdfidlpVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1948769844 181 LLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:cd03220 184 RLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-238 |
4.08e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.17 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYP---DGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQN 88
Cdd:TIGR00958 485 SFSYPnrpDVPV-LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 PddQLFATTVFEDAAFGPRNmgCGDAEVKTRVEAALASVDMAEFAgKGIHN--------LSYGQKKRVCIAGLLAMGHEI 160
Cdd:TIGR00958 564 P--VLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHDFIMEFP-NGYDTevgekgsqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 161 LLLDEPTAGLDPMGEYrmmeLLTRLNRDQGVTIVMATHSVDLVPIfLHQLHILSRGRLIRGGAPEEVFTAPDELANVK 238
Cdd:TIGR00958 639 LILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-198 |
4.99e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.84 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLVFqnpddqlfattvfe 100
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVF-------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 101 daafGPRNM------------------GCGDAEVKTRVEAaLASV-DMAEFAGKGIHNLSYGQKKRvC--IAGLLamgH- 158
Cdd:COG4586 102 ----GQRSQlwwdlpaidsfrllkaiyRIPDAEYKKRLDE-LVELlDLGELLDTPVRQLSLGQRMR-CelAAALL---Hr 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1948769844 159 -EILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATH 198
Cdd:COG4586 173 pKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSH 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-196 |
5.24e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 86.13 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYP-DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQnpD 90
Cdd:cd03251 7 TFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ--D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLFATTVFEDAAFGPRnmGCGDAEVKTRVEAALASvdmaEFAGK---GIH--------NLSYGQKKRVCIAGLLAMGHE 159
Cdd:cd03251 85 VFLFNDTVAENIAYGRP--GATREEVEEAARAANAH----EFIMElpeGYDtvigergvKLSGGQRQRIAIARALLKDPP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1948769844 160 ILLLDEPTAGLDPMGEYRMMELLTRLNRDQgVTIVMA 196
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNR-TTFVIA 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-198 |
6.08e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLhpRDIYRkvglvfqnpDDQLF---------ATT 97
Cdd:PRK13538 22 FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ--RDEYH---------QDLLYlghqpgiktELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 98 VFEDAAFGPRNMGCGDAEvktRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGeyr 177
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG--- 164
|
170 180
....*....|....*....|....
gi 1948769844 178 mMELLTRL---NRDQGVTIVMATH 198
Cdd:PRK13538 165 -VARLEALlaqHAEQGGMVILTTH 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-231 |
8.30e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.78 E-value: 8.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 7 SVDLES-YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLV 85
Cdd:PRK11000 3 SVTLRNvTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNpddqlFA----TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:PRK11000 81 FQS-----YAlyphLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 162 LLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
27-225 |
9.29e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.89 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGlIKGYK---GEVLLDGENVLKLHPRDIYRK-VGLVFQNPDD-------QLFA 95
Cdd:COG0396 21 LTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKYEvtsGSILLDGEDILELSPDERARAgIFLAFQYPVEipgvsvsNFLR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TtvfedAAFGPRNMGCGDAEVKTRVEAALASVDMAE-FAGKGIH-NLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPM 173
Cdd:COG0396 100 T-----ALNARRGEELSAREFLKLLKEKMKELGLDEdFLDRYVNeGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDID 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 174 GEYRMMELLTRLnRDQGVTIVMATHS---VDLVPIflHQLHILSRGRLIRGGAPE 225
Cdd:COG0396 175 ALRIVAEGVNKL-RSPDRGILIITHYqriLDYIKP--DFVHVLVDGRIVKSGGKE 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-199 |
1.38e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPddqLFA 95
Cdd:COG1101 16 VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDP---MMG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 T----TVFEDAAF-----GPRNMGCG-DAEVKTRVEAALASVDMaefagkGIHN--------LSYGQkkRVCIAGLLA-M 156
Cdd:COG1101 93 TapsmTIEENLALayrrgKRRGLRRGlTKKRRELFRELLATLGL------GLENrldtkvglLSGGQ--RQALSLLMAtL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1948769844 157 GH-EILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHS 199
Cdd:COG1101 165 TKpKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-233 |
1.76e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.19 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVM-------DGLIKgyKGEVLLDGENVLKLHP---RDIYRKVGLVFQ 87
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIR--VGDITIDTARSLSQQKgliRQLRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 NPDdqLFA-TTVFEDAAFGPRNM-GCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:PRK11264 93 NFN--LFPhRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 166 PTAGLDP--MGE-YRMMELLTRLNRdqgvTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDE 233
Cdd:PRK11264 171 PTSALDPelVGEvLNTIRQLAQEKR----TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-224 |
2.94e-19 |
|
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: 83.70 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 5 RISVDLESYKY-PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVG 83
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNPddQLFATTVFEDAAfgPRNMgCGDAEvktrVEAALASVDMAEF----AGKGIH-------NLSYGQKKRVCIAG 152
Cdd:cd03244 82 IIPQDP--VLFSGTIRSNLD--PFGE-YSDEE----LWQALERVGLKEFveslPGGLDTvveeggeNLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 153 LLAMGHEILLLDEPTAGLDPMGEYRMMELLTrlNRDQGVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAP 224
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDSP 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-202 |
3.32e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.10 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDG---TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIY----RKVGLVF 86
Cdd:PRK11629 14 RYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 87 QN----PDdqlfaTTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILL 162
Cdd:PRK11629 94 QFhhllPD-----FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1948769844 163 LDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDL 202
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-200 |
4.35e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.34 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEvLLDGENVLKlHPRDIYRkvgLVFQnpDDQL 93
Cdd:PRK11247 21 RYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLA-EAREDTR---LMFQ--DARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 94 FA-TTVFEDAAFGPRnmgcGDAevKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP 172
Cdd:PRK11247 93 LPwKKVIDNVGLGLK----GQW--RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180
....*....|....*....|....*...
gi 1948769844 173 MGEYRMMELLTRLNRDQGVTIVMATHSV 200
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDV 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
27-227 |
9.12e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 9.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLhPrdIYR--KVGL--------VFQNpddqLfat 96
Cdd:COG1137 24 LEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-P--MHKraRLGIgylpqeasIFRK----L--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 TVFED--AAFGPRNMgcGDAEVKTRVEAALASVDMAEFAG-KGIHnLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPM 173
Cdd:COG1137 94 TVEDNilAVLELRKL--SKKEREERLEELLEEFGITHLRKsKAYS-LSGGERRRVEIARALATNPKFILLDEPFAGVDPI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 174 GEYRMMELLTRLnRDQGVTIVMATHSV----DLVpiflHQLHILSRGRLIRGGAPEEV 227
Cdd:COG1137 171 AVADIQKIIRHL-KERGIGVLITDHNVretlGIC----DRAYIISEGKVLAEGTPEEI 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-231 |
1.17e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.51 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDiyRKVGLVFQNpddqlF 94
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQN-----Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 95 A----TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVciagllAMGHEI------LLLD 164
Cdd:PRK11650 86 AlyphMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRV------AMGRAIvrepavFLFD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHsvDLVP--IFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTH--DQVEamTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-231 |
1.78e-18 |
|
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: 84.74 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKT-TLLKVM----DGLIKgYKGEVLLDGENVLKLHPRDIYR----KVGLVFQ------NP-- 89
Cdd:COG4172 31 FDIAAGETLALVGESGSGKSvTALSILrllpDPAAH-PSGSILFDGQDLLGLSERELRRirgnRIAMIFQepmtslNPlh 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 --DDQLFATTVfedaafgpRNMGCGDAEVKTRVEAALASVdmaefagkGI-----------HNLSYGQKKRVCIAGLLAM 156
Cdd:COG4172 110 tiGKQIAEVLR--------LHRGLSGAAARARALELLERV--------GIpdperrldaypHQLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 157 GHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-228 |
2.47e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 11 ESYKypdGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENV--LKLHPRdIYRKVGLVFQN 88
Cdd:PRK10895 11 KAYK---GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIslLPLHAR-ARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 PD--------DQLFATTVFEDaafgprnmGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEI 160
Cdd:PRK10895 87 ASifrrlsvyDNLMAVLQIRD--------DLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 161 LLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVF 228
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-231 |
2.82e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.24 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKT-TLLKVM-----DGLIKGykgEVLLDGENVLKLHPRDIYR---- 80
Cdd:PRK09473 21 TFSTPDGDVtAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMgllaaNGRIGG---SATFNGREILNLPEKELNKlrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 81 KVGLVFQNP----------DDQLFATTVFEdaafgpRNMGCGDA-EVKTRVeaaLASVDMAEfAGKGI----HNLSYGQK 145
Cdd:PRK09473 98 QISMIFQDPmtslnpymrvGEQLMEVLMLH------KGMSKAEAfEESVRM---LDAVKMPE-ARKRMkmypHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 146 KRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPE 225
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
....*.
gi 1948769844 226 EVFTAP 231
Cdd:PRK09473 248 DVFYQP 253
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-245 |
3.16e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.67 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKT-TLLKVMDGLIKGYK---GEVLLDGENVlklHPRDIY-RKVGLVFQNPDdqlfattvfed 101
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSlTCAAALGILPAGVRqtaGRVLLDGKPV---APCALRgRKIATIMQNPR----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 AAFGP-RNMGCGDAEV-----KTRVEAALASV-------DMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:PRK10418 90 SAFNPlHTMHTHARETclalgKPADDATLTAAleavgleNAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 169 GLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDELANVKLRLPHIA 245
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLA 246
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-198 |
3.36e-18 |
|
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: 84.08 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGEnVLKLHPRDIYRkvglvfqnpddQLFAtTVFEDAAFGP 106
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ-PVTADNREAYR-----------QLFS-AVFSDFHLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 107 RNMGCGDAEVKTRVEAALASVDMAE---FAGKGIHN--LSYGQKKRVciAGLLAM--GHEILLLDEPTAGLDPmgEYRMM 179
Cdd:COG4615 420 RLLGLDGEADPARARELLERLELDHkvsVEDGRFSTtdLSQGQRKRL--ALLVALleDRPILVFDEWAADQDP--EFRRV 495
|
170 180
....*....|....*....|..
gi 1948769844 180 ---ELLTRLnRDQGVTIVMATH 198
Cdd:COG4615 496 fytELLPEL-KARGKTVIAISH 516
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-230 |
5.31e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.61 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 5 RISVDLESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGL 84
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQNPddQLFATTVFEDAAFGpRNMGcgdaevKTRVEAALASVDMAEFAGK---GIH--------NLSYGQKKRVCIAGL 153
Cdd:PRK10790 420 VQQDP--VVLADTFLANVTLG-RDIS------EEQVWQALETVQLAELARSlpdGLYtplgeqgnNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 154 LAMGHEILLLDEPTAGLDPMGEYRMMELLtRLNRDQGVTIVMAtHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFTA 230
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIA-HRLSTI-VEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
27-227 |
5.45e-18 |
|
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: 79.88 E-value: 5.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGlIKGYK---GEVLLDGENVLKLHPRDIYRK-VGLVFQNPddqlfattvfeda 102
Cdd:cd03217 21 LTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEvteGEILFKGEDITDLPPEERARLgIFLAFQYP------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 103 afgprnmgcgdaevktrveAALASVDMAEF---AGKGihnLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMM 179
Cdd:cd03217 87 -------------------PEIPGVKNADFlryVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 180 ELLTRLnRDQGVTIVMATHSVDL----VPIFlhqLHILSRGRLIRGGAPEEV 227
Cdd:cd03217 145 EVINKL-REEGKSVLIITHYQRLldyiKPDR---VHVLYDGRIVKSGDKELA 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-231 |
5.52e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 20 VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGyKGEVLLDGENVLKLHPRD---IYRKVGLVFQNPDDQLFAT 96
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 -TVFEDAAFGPR--NMGCGDAEVKTRVEAALASVDM---------AEFAGkgihnlsyGQKKRVCIAGLLAMGHEILLLD 164
Cdd:PRK15134 379 lNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLdpetrhrypAEFSG--------GQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-222 |
2.84e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 81.71 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLV 85
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNPddQLFATTVFEDAAFGPRNmGCGDAEVKTRVEAALASVDMAEFAgKGIH--------NLSYGQKKRVCIAGLLAMG 157
Cdd:TIGR01193 554 PQEP--YIFSGSILENLLLGAKE-NVSQDEIWAACEIAEIKDDIENMP-LGYQtelseegsSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 158 HEILLLDEPTAGLDPMGEYRMMELLTRLNRDqgvTIVMATHSVDlVPIFLHQLHILSRGRLIRGG 222
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQG 690
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-217 |
4.42e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.08 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 32 GEFTGILGSNGSGKTTLLKVMDGLIKG--YKGEVLLDGENVLKlhprDIYRKVGLVFQnpDDQLFA-TTVFEDAAFG--- 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKPTK----QILKRTGFVTQ--DDILYPhLTVRETLVFCsll 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 --PRNMgcgDAEVKTRV------EAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYR 177
Cdd:PLN03211 168 rlPKSL---TKQEKILVaesvisELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1948769844 178 MMELLTRLNRdQGVTIVMATH--SVDLVPIFlHQLHILSRGR 217
Cdd:PLN03211 245 LVLTLGSLAQ-KGKTIVTSMHqpSSRVYQMF-DSVLVLSEGR 284
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-230 |
4.66e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.20 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDG------EnvlklhprdiyrkVGLVFqNPDdqlfaTTVFE 100
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsallE-------------LGAGF-HPE-----LTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 101 DAAFGPRNMGCGDAEVKTRVEaalasvDMAEFAGKG------IHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP-- 172
Cdd:COG1134 108 NIYLNGRLLGLSRKEIDEKFD------EIVEFAELGdfidqpVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAaf 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 173 ----MGeyRMMELltrlnRDQGVTIVMATHSVDLVP------IFLHQlhilsrGRLIRGGAPEEVFTA 230
Cdd:COG1134 182 qkkcLA--RIREL-----RESGRTVIFVSHSMGAVRrlcdraIWLEK------GRLVMDGDPEEVIAA 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-204 |
8.12e-17 |
|
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: 76.74 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGenvlklhprdiyrKVGLVFQNPddQLFATTVFEDAAFG- 105
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEP--WIQNGTIRENILFGk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 PRNMgcgdAEVKTRVEAALASVDMAEFAG--------KGIhNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYR 177
Cdd:cd03250 91 PFDE----ERYEKVIKACALEPDLEILPDgdlteigeKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180
....*....|....*....|....*..
gi 1948769844 178 MMELLTRLNRDQGVTIVMATHSVDLVP 204
Cdd:cd03250 166 IFENCILGLLLNNKTRILVTHQLQLLP 192
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-198 |
1.37e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVA-LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYR----KVGLVF 86
Cdd:PRK10535 13 SYPSGEEQVEvLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 87 QNPD--DQLFATTVFEDAAFgprNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:PRK10535 93 QRYHllSHLTAAQNVEVPAV---YAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190
....*....|....*....|....*....|....
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATH 198
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTH 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-242 |
1.39e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 28 EIRRGEFTGILGSNGSGKTTLLKVMDGLIKG---YKGEVLLDGEnvlKLHPRDIYRKVGLVFQnpDDQLFAT-TVFEDAA 103
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM---PIDAKEMRAISAYVQQ--DDLFIPTlTVREHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 104 FG-----PRNMgcGDAEVKTRVEAALASVDMAEFA------GKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP 172
Cdd:TIGR00955 122 FQahlrmPRRV--TKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 173 MGEYRMMELLTRLNrDQGVTIVMATH--SVDLVPIFlHQLHILSRGRLIRGGAPEEvftAPDELANVKLRLP 242
Cdd:TIGR00955 200 FMAYSVVQVLKGLA-QKGKTIICTIHqpSSELFELF-DKIILMAEGRVAYLGSPDQ---AVPFFSDLGHPCP 266
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-202 |
1.98e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.36 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP--RDIYR--KVGLVFQNpdDQLFAT- 96
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEeaRAKLRakHVGFVFQS--FMLIPTl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEY 176
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|....*.
gi 1948769844 177 RMMELLTRLNRDQGVTIVMATHSVDL 202
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-230 |
2.77e-16 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 76.11 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVmdgLIKGY---KGEVLLDGENVLKLHPRDIYRKVGLVFQn 88
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL---LFRFYdvsSGSILIDGQDIREVTLDSLRRAIGVVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 pDDQLFATTVFEDAAFGprNMGCGDAEVktrVEAALASvdmaefagkGIHN-------------------LSYGQKKRVC 149
Cdd:cd03253 83 -DTVLFNDTIGYNIRYG--RPDATDEEV---IEAAKAA---------QIHDkimrfpdgydtivgerglkLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 150 IAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRdqGVTIVMATHSV------DLVpIFLHQLHILSRGR----LI 219
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLstivnaDKI-IVLKDGRIVERGTheelLA 224
|
250
....*....|.
gi 1948769844 220 RGGAPEEVFTA 230
Cdd:cd03253 225 KGGLYAEMWKA 235
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-231 |
3.51e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.25 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 1 MVDTR-ISVDLESykyPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGyKGEV-----LLDGENVLKL 73
Cdd:COG4170 3 LLDIRnLTIEIDT---PQGRVkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVtadrfRWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 74 HPRD----IYRKVGLVFQNP----------DDQL---FATTVFED---AAFGPRnmgcgdaevKTRVEAALASVD----- 128
Cdd:COG4170 79 SPRErrkiIGREIAMIFQEPsscldpsakiGDQLieaIPSWTFKGkwwQRFKWR---------KKRAIELLHRVGikdhk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 129 --MAEFAgkgiHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIF 206
Cdd:COG4170 150 diMNSYP----HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQW 225
|
250 260
....*....|....*....|....*
gi 1948769844 207 LHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:COG4170 226 ADTITVLYCGQTVESGPTEQILKSP 250
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
14-233 |
3.63e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLklhPRDIYR------------K 81
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ---LRDLYAlseaerrrllrtE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 82 VGLVFQNPDDQLfATTVFEDAAFGPRNMGCGD----------AEVKTRVEAALASVD--MAEFAGkgihnlsyGQKKRVC 149
Cdd:PRK11701 91 WGFVHQHPRDGL-RMQVSAGGNIGERLMAVGArhygdirataGDWLERVEIDAARIDdlPTTFSG--------GMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 150 IAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFT 229
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLD 241
|
....
gi 1948769844 230 APDE 233
Cdd:PRK11701 242 DPQH 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-231 |
3.80e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---RDIYRKVGLVFQNPDd 91
Cdd:PRK11308 24 PERLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPY- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 qlfattvfedAAFGPR-------------NMGCGDAEVKTRVEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMG 157
Cdd:PRK11308 103 ----------GSLNPRkkvgqileeplliNTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 158 HEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-218 |
7.22e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 73.62 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD-IYRKVGLVfqnPDDQLfattvfEDAAFG 105
Cdd:cd03215 21 FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYV---PEDRK------REGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 PRNmgcgdaevkTRVEAALASVdmaefagkgihnLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRL 185
Cdd:cd03215 92 DLS---------VAENIALSSL------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 186 nRDQGVTIVMatHSVDLVPIFL--HQLHILSRGRL 218
Cdd:cd03215 151 -ADAGKAVLL--ISSELDELLGlcDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-227 |
9.08e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLV--FQNPDDQLfa 95
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVpqFDNLDLEF-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 tTVFEDAAFGPRNMGcgdaeVKTR-VEAALASV-DMAEFAGKG---IHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:PRK13536 130 -TVRENLLVFGRYFG-----MSTReIEAVIPSLlEFARLESKAdarVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 171 DPMGEY----RMMELLTRlnrdqGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:PRK13536 204 DPHARHliweRLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-216 |
1.07e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 73.43 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVM-----DGLIKGykgEVLLDGenvlKLHPRDIYRKVGLVFQNPDDQLFATtvfedaa 103
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLagrktAGVITG---EILING----RPLDKNFQRSTGYVEQQDVHSPNLT------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 104 fgprnmgcgdaevktrVEAALasvdmaEFAGKgIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLT 183
Cdd:cd03232 96 ----------------VREAL------RFSAL-LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 184 RLNrDQGVTIVMATH--SVDLVPIFlHQLHILSRG 216
Cdd:cd03232 153 KLA-DSGQAILCTIHqpSASIFEKF-DRLLLLKRG 185
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-226 |
1.09e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVmdgLIKGY---KGEVLLDGENVLKLHPRDIYRKVGLVFQ 87
Cdd:PRK11160 345 SFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL---LTRAWdpqQGEILLNGQPIADYSEAALRQAISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 NPDdqLFATTVFEDAAfgprnMGCGDA------EVKTRVE-AALASVD--MAEFAGKGIHNLSYGQKKRVCIAGLLAMGH 158
Cdd:PRK11160 422 RVH--LFSATLRDNLL-----LAAPNAsdealiEVLQQVGlEKLLEDDkgLNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 159 EILLLDEPTAGLDPMGEYRMMELLTRLNRDQgvTIVMATHSVDLVPIFlHQLHILSRGRLIRGGAPEE 226
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
27-220 |
2.79e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLdgenvlklhPRDIyrKVGLVFQNPDdqLFAT-TVFE--DAA 103
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGL--RIGYLPQEPP--LDDDlTVLDtvLDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 104 FGPR------------NMGCGDAEVK------------------TRVEAALAS--VDMAEFAGKgIHNLSYGQKKRVCIA 151
Cdd:COG0488 86 DAELraleaeleeleaKLAEPDEDLErlaelqeefealggweaeARAEEILSGlgFPEEDLDRP-VSELSGGWRRRVALA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 152 GLLAMGHEILLLDEPTAGLDpmgeYRMMELLTR-LNRDQGvTIVMATHSVDlvpiFLHQL--HI--LSRGRLIR 220
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLD----LESIEWLEEfLKNYPG-TVLVVSHDRY----FLDRVatRIleLDRGKLTL 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-231 |
3.00e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 74.36 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHP---RDIYRKVGLVFQNPddqlfattvfeDAA 103
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewRAVRSDIQMIFQDP-----------LAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 104 FGPRnMGCGD---------------AEVKTRVEAALASVDMAE-FAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPT 167
Cdd:PRK15079 111 LNPR-MTIGEiiaeplrtyhpklsrQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 168 AGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPiflhqlHILSR------GRLIRGGAPEEVFTAP 231
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVK------HISDRvlvmylGHAVELGTYDEVYHNP 253
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-224 |
3.82e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 72.44 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 3 DTRISVDLESYKY-PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK 81
Cdd:cd03369 4 HGEIEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 82 VGLVFQNPddQLFATTVfeDAAFGPRNMgCGDAEVKTRVEAAlasvdmaefagKGIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:cd03369 84 LTIIPQDP--TLFSGTI--RSNLDPFDE-YSDEEIYGALRVS-----------EGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 162 LLDEPTAGLDpmgeYRMMELLTRLNRD--QGVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAP 224
Cdd:cd03369 148 VLDEATASID----YATDALIQKTIREefTNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-171 |
5.77e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.59 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 31 RGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLdGENVlklhprdiyrKVGLVFQNPDDQLFATTVFEDAAFGPRNMG 110
Cdd:TIGR03719 347 PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQSRDALDPNKTVWEEISGGLDIIK 415
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 111 CGDAEVKTRveaalASVDMAEFAG----KGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:TIGR03719 416 LGKREIPSR-----AYVGRFNFKGsdqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-217 |
7.45e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.07 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLL-DGENVLKLhPRDIYRKVG-----LVFQNP 89
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFL-PQRPYLPLGtlreaLLYPAT 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 DDQlfattvFEDAAfgprnmgcgdaevktrVEAALASVDMAEFAGK------GIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:COG4178 452 AEA------FSDAE----------------LREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 164 DEPTAGLDPMGEYRMMELLtrLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGR 217
Cdd:COG4178 510 DEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGDGS 561
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-204 |
8.05e-15 |
|
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: 71.59 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEV-----LLDGENVLKLHPRDIYrKVGLVFQ 87
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRY-SVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 NPddQLFATTVFEDAAFG-PRNmgcgDAEVKTRVEAA--------LASVDMAEFAGKGIhNLSYGQKKRVCIAGLLAMGH 158
Cdd:cd03290 87 KP--WLLNATVEENITFGsPFN----KQRYKAVTDACslqpdidlLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1948769844 159 EILLLDEPTAGLD-PMGEYRMMELLTRLNRDQGVTIVMATHSVDLVP 204
Cdd:cd03290 160 NIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLP 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-217 |
1.17e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.88 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEV-LLDGENVLKLhPRDIYrkvgl 84
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFL-PQRPY----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 vfqnpddqlFATTVFEDAAFGPRNMgcgdaevktrveaalasvdmaefagkgihNLSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:cd03223 75 ---------LPLGTLREQLIYPWDD-----------------------------VLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 165 EPTAGLDPMGEYRMMELLtrlnRDQGVTIVMATHSVDLVPIFLHQLHILSRGR 217
Cdd:cd03223 117 EATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
27-203 |
1.35e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEvlldgeNVLKLHPRDIYRKVGLVfqnpdDQLFATTVFEDAAFGP 106
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA------GCVDVPDNQFGREASLI-----DAIGRKGDFKDAVELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 107 RNMGCGDAEvktrveAALASVDmaefagkgihNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLN 186
Cdd:COG2401 120 NAVGLSDAV------LWLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLA 183
|
170
....*....|....*..
gi 1948769844 187 RDQGVTIVMATHSVDLV 203
Cdd:COG2401 184 RRAGITLVVATHHYDVI 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-231 |
1.72e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 32 GEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD---IYRKVGLVFQNPDDQLFATTVFEDAAFGP-- 106
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqaLRRDIQFIFQDPYASLDPRQTVGDSIMEPlr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 107 -RNMGCGDAEVKtRVEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTR 184
Cdd:PRK10261 430 vHGLLPGKAAAA-RVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1948769844 185 LNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK10261 509 LQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-198 |
2.05e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 8 VDLE--SYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLdGENVlklhprdiyrKVGLV 85
Cdd:COG0488 316 LELEglSKSYGDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQ-----NPDDqlfatTVFEdaAFGPRNMGCGDAEVKTRVEAALASVDMAEfagKGIHNLSYGQKKRVCIAGLLAMGHEI 160
Cdd:COG0488 384 DQhqeelDPDK-----TVLD--ELRDGAPGGTEQEVRGYLGRFLFSGDDAF---KPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190
....*....|....*....|....*....|....*....
gi 1948769844 161 LLLDEPTAGLDPmgeyRMMELLTR-LNRDQGvTIVMATH 198
Cdd:COG0488 454 LLLDEPTNHLDI----ETLEALEEaLDDFPG-TVLLVSH 487
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-231 |
2.14e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.08 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 28 EIRRGEFTGILGSNGSGKT-TLLKVMdGLIKgYKGEVL-----LDGENVLKLHPRDIYRKVG----LVFQNPDDQLFA-- 95
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSvSSLAIM-GLID-YPGRVMaekleFNGQDLQRISEKERRNLVGaevaMIFQDPMTSLNPcy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGK---GIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP 172
Cdd:PRK11022 107 TVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 173 MGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK11022 187 TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-206 |
2.39e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 70.90 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFT-----GILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVlKLHPRDIyrkvglvfq 87
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYI--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 NPDdqlFATTVfEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEfagKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPT 167
Cdd:cd03237 71 KAD---YEGTV-RDLLSSITKDFYTHPYFKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1948769844 168 AGLDpmGEYRMM--ELLTR--LNRDQGVTIV-----MATHSVDLVPIF 206
Cdd:cd03237 144 AYLD--VEQRLMasKVIRRfaENNEKTAFVVehdiiMIDYLADRLIVF 189
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-198 |
4.96e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYR-KVGLVFQNPD-- 90
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQELSvi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLfatTVFEDAAFG--PRNMGCGD-----AEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:PRK09700 93 DEL---TVLENLYIGrhLTKKVCGVniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 164 DEPTAGLDPmGEYRMMELLTRLNRDQGVTIVMATH 198
Cdd:PRK09700 170 DEPTSSLTN-KEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-227 |
6.31e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.37 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLiKGYK---GEVL----------------LDGE--------- 68
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM-DQYEptsGRIIyhvalcekcgyverpsKVGEpcpvcggtl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 69 --------NVLKLHPRDIYRKVGLVFQnpddQLFA----TTVFEDAAFGPRNMGcgdAEVKTRVEAALASVDMAEFAGKG 136
Cdd:TIGR03269 90 epeevdfwNLSDKLRRRIRKRIAIMLQ----RTFAlygdDTVLDNVLEALEEIG---YEGKEAVGRAVDLIEMVQLSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 137 IH---NLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHIL 213
Cdd:TIGR03269 163 THiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
250
....*....|....
gi 1948769844 214 SRGRLIRGGAPEEV 227
Cdd:TIGR03269 243 ENGEIKEEGTPDEV 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-227 |
9.32e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.99 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGtvalaeMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGE--VLLDGENVLKLHPRDIYRK-- 81
Cdd:TIGR03269 290 ISVDRGVVKAVDN------VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRGra 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 82 ---VGLVFQNPDdqLFA-TTVFED--AAFG---PRNMGCGDAeVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAG 152
Cdd:TIGR03269 364 kryIGILHQEYD--LYPhRTVLDNltEAIGlelPDELARMKA-VITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 153 LLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-198 |
1.19e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD-----IYrkvgLVFQ 87
Cdd:PRK15439 18 SKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKahqlgIY----LVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 NPddQLFAT-TVFEDAAFG-PRNmgcgdAEVKTRVEAALA----SVDMAEFAGkgihNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:PRK15439 94 EP--LLFPNlSVKENILFGlPKR-----QASMQKMKQLLAalgcQLDLDSSAG----SLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1948769844 162 LLDEPTAGLDPmGEYRmmELLTRLN--RDQGVTIVMATH 198
Cdd:PRK15439 163 ILDEPTASLTP-AETE--RLFSRIRelLAQGVGIVFISH 198
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-231 |
1.32e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 35 TGILGSNGSGKTTLLKVMDGLIKGYKGEVLLdGENVLKLHPRDIY-----RKVGLVFQnpDDQLFattvfedaafgPRnm 109
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKGIClppekRRIGYVFQ--DARLF-----------PH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 110 gcgdaevkTRVEAAL----ASVDMAEFAG----KGI--------HNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD-P 172
Cdd:PRK11144 91 --------YKVRGNLrygmAKSMVAQFDKivalLGIeplldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 173 mgeyRMMELLT---RLNRDQGVTIVMATHSVDLVpifLH---QLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK11144 163 ----RKRELLPyleRLAREINIPILYVSHSLDEI---LRladRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-220 |
2.47e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPdGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD--------IYRKVGLVf 86
Cdd:PRK11288 14 FP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagvaiIYQELHLV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 87 qnPDdqlfaTTVFEDAAFG--PRNMGCGD-AEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:PRK11288 92 --PE-----MTVAENLYLGqlPHKGGIVNrRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIR 220
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-231 |
4.02e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGEnvlKLHPRDI-YR--KVGLVFQNPDDQLfatt 97
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDYsYRsqRIRMIFQDPSTSL---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 98 vfedaafGPR-------------NMGCGDAEVKTRVEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:PRK15112 101 -------NPRqrisqildfplrlNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-253 |
4.13e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.08 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIK--GYKGEVLLDGENVLKLHPRDIYRKvGLVFQNPDDQLF 94
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERA-GIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 95 AT-TVFEDAAFGPRNMGCG----DAEVKTRVEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:TIGR02633 91 PElSVAENIFLGNEITLPGgrmaYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 169 GLDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIrGGAPEEVFTAPD--------ELANVKLR 240
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV-ATKDMSTMSEDDiitmmvgrEITSLYPH 248
|
250
....*....|....
gi 1948769844 241 LPH-IAELIYQLKH 253
Cdd:TIGR02633 249 EPHeIGDVILEARN 262
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-230 |
4.23e-13 |
|
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: 69.20 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPddQLFA 95
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDP--VLFS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVFEDA-AFGPRN-----MGCGDAEVKTRVEAALASVDMAefAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAG 169
Cdd:TIGR00957 1374 GSLRMNLdPFSQYSdeevwWALELAHLKTFVSALPDKLDHE--CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 170 LDpmgeYRMMELLTRLNRDQ--GVTIVMATHSVDLVPIFLHQLhILSRGRLIRGGAPEEVFTA 230
Cdd:TIGR00957 1452 VD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVI-VLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-253 |
6.80e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIK--GYKGEVLLDGENVLKLHPRD--------IYRKVGLVF 86
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDteragiaiIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 87 QnpddqlfaTTVFEDAAFGPRNMGCG---DAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:PRK13549 96 E--------LSVLENIFLGNEITPGGimdYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIrGGAPEEVFTAPD--------ELA 235
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHI-GTRPAAGMTEDDiitmmvgrELT 245
|
250
....*....|....*....
gi 1948769844 236 NVKLRLPH-IAELIYQLKH 253
Cdd:PRK13549 246 ALYPREPHtIGEVILEVRN 264
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
6-217 |
6.82e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGL 84
Cdd:PRK10789 314 LDVNIRQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQNPddQLFATTVFEDAAfgprnMGCGDAEVKTRVEAA-LASV--DM--------AEFAGKGIHnLSYGQKKRVCIAGL 153
Cdd:PRK10789 394 VSQTP--FLFSDTVANNIA-----LGRPDATQQEIEHVArLASVhdDIlrlpqgydTEVGERGVM-LSGGQKQRISIARA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 154 LAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNrdQGVTIVMATHSVDLVP-----IFLHQLHILSRGR 217
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWG--EGRTVIISAHRLSALTeaseiLVMQHGHIAQRGN 532
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-216 |
6.94e-13 |
|
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: 68.89 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPdGTVALAEMRL--EIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlHPRDIYRKVGLV--FQNPD 90
Cdd:TIGR01257 1947 YS-GTSSPAVDRLcvGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCpqFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQLfatTVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:TIGR01257 2025 DLL---TGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1948769844 171 DPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRG 216
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-218 |
1.36e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.88 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 20 VALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDgenvlklhprdiyRKVGLVFQNP--------DD 91
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAwimnatvrGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFATTvfEDAAfgprnmGCGDAEVKTRVEAALASVDMA---EFAGKGIhNLSYGQKKRVCIAGLLAMGHEILLLDEPTA 168
Cdd:PTZ00243 741 ILFFDE--EDAA------RLADAVRVSQLEADLAQLGGGletEIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 169 GLDP-MGEYRMMELLtrLNRDQGVTIVMATHSVDLVPiflHQLHI--LSRGRL 218
Cdd:PTZ00243 812 ALDAhVGERVVEECF--LGALAGKTRVLATHQVHVVP---RADYVvaLGDGRV 859
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-217 |
2.75e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.52 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPdd 91
Cdd:PRK13657 341 SFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFATTVFEDAAFGPRNmgCGDAEVKTRVEAALASvDMAE--------FAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:PRK13657 419 GLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAH-DFIErkpdgydtVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLNRDQgVTIVMAtH------SVDLVpIFLHQLHILSRGR 217
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGR-TTFIIA-HrlstvrNADRI-LVFDNGRVVESGS 552
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-216 |
3.05e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.67 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIkgyKGEVLLDGENVLKLHPRD--IYRKVGLVFQNpDDQLFATTVFED---AA 103
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERV---TTGVITGGDRLVNGRPLDssFQRSIGYVQQQ-DLHLPTSTVRESlrfSA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 104 FGPRNMGCGDAEVKTRVEAALASVDMAEFA-------GKGihnLSYGQKKRVCIA-GLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:TIGR00956 862 YLRQPKSVSKSEKMEYVEEVIKLLEMESYAdavvgvpGEG---LNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1948769844 176 YRMMELLTRLNrDQGVTIVMATH--SVDLVPIFlHQLHILSRG 216
Cdd:TIGR00956 939 WSICKLMRKLA-DHGQAILCTIHqpSAILFEEF-DRLLLLQKG 979
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-203 |
3.10e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 64.38 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 20 VALAEMRLEIRRGEFTGILGSNGSGKTTLLKvmdGLIKGY---KGEVLLDGE----NVLKLHPRDIY--RK--VGLVFQn 88
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLK---CIYGNYlpdSGSILVRHDggwvDLAQASPREILalRRrtIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 pddqlFATTVfedaafgPR------------NMGCGDAEVKTRVEAALASVDMAE---------FAGkgihnlsyGQKKR 147
Cdd:COG4778 101 -----FLRVI-------PRvsaldvvaepllERGVDREEARARARELLARLNLPErlwdlppatFSG--------GEQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 148 VCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLV 203
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVR 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-229 |
4.70e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 33 EFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPddQLFATTV-FEDAAFGPRNmgc 111
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP--VLFSGTVrFNIDPFSEHN--- 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 112 gDAEVKTRVEAALAS--VDMAEFA-----GKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDpmgeYRMMELLTR 184
Cdd:PLN03232 1338 -DADLWEALERAHIKdvIDRNPFGldaevSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIQR 1412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1948769844 185 LNRDQ--GVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFT 229
Cdd:PLN03232 1413 TIREEfkSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
29-222 |
7.09e-12 |
|
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: 63.05 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIKGY---KGEVLLDGENVLKL---HPRDIyrkvglVFQNPDDQLFAT-TVFED 101
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFaekYPGEI------IYVSEEDVHFPTlTVRET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 AAFGPRnmGCGDAEVKtrveaalasvdmaefagkGIhnlSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMEL 181
Cdd:cd03233 104 LDFALR--CKGNEFVR------------------GI---SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1948769844 182 LTRLNRDQGVTIVMATH--SVDLVPIFlHQLHILSRGRLIRGG 222
Cdd:cd03233 161 IRTMADVLKTTTFVSLYqaSDEIYDLF-DKVLVLYEGRQIYYG 202
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-231 |
7.88e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 13 YKYPDGTV-ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKG----YKGEVLLDGENVLKLHPRDIYRKVG---- 83
Cdd:PRK15093 13 FKTSDGWVkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGhnvs 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 84 LVFQNPDDQLFATTVFEDA----------------AFGPRnmgcgdaevKTRVEAALASV---DMAEFAGKGIHNLSYGQ 144
Cdd:PRK15093 93 MIFQEPQSCLDPSERVGRQlmqnipgwtykgrwwqRFGWR---------KRRAIELLHRVgikDHKDAMRSFPYELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 145 KKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAP 224
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
....*..
gi 1948769844 225 EEVFTAP 231
Cdd:PRK15093 244 KELVTTP 250
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-171 |
1.17e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 31 RGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLdGENVlklhprdiyrKVGLVFQNPDDQLFATTVFEDAAFGPRNMG 110
Cdd:PRK11819 349 PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQSRDALDPNKTVWEEISGGLDIIK 417
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 111 CGDAEVKTRveaalASVDMAEFAG----KGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PRK11819 418 VGNREIPSR-----AYVGRFNFKGgdqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
27-222 |
1.18e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLiKGYK---GEVLLDGENVLKLHPRDIYRK-VGLVFQNPDDQLFATTV-FED 101
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAYKileGDILFKGESILDLEPEERAHLgIFLAFQYPIEIPGVSNAdFLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 AAFGPRNMGCGDAEVK-----TRVEAALASVDMAE-FAGKGIHN-LSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMG 174
Cdd:CHL00131 107 LAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 175 EYRMMELLTRLnRDQGVTIVMATHSVDL----VPIFlhqLHILSRGRLIRGG 222
Cdd:CHL00131 187 LKIIAEGINKL-MTSENSIILITHYQRLldyiKPDY---VHVMQNGKIIKTG 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-212 |
1.87e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKL-HPRDIYRKVGLVFQNPDDQLFA 95
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdRSRFMAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVFEDAAFGPRnmgcgdaeVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:PRK13543 102 NLHFLCGLHGRR--------AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1948769844 176 YRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHI 212
Cdd:PRK13543 174 TLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-247 |
2.87e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.22 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 107 RNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLN 186
Cdd:NF000106 112 R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 187 RDqGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAPDElANVKLRLPHIAEL 247
Cdd:NF000106 192 RD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGG-RTLQIRPAHAAEL 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-197 |
3.10e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD-IYRKVGLVfqnPDDQ----LFAT-TVFE 100
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYV---PEDRkgegLVLDlSIRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 101 DAAFGPRNMGCGDAEVKTRVEAALA------------SVDMAefagkgIHNLSYG--QKkrVCIAGLLAMGHEILLLDEP 166
Cdd:COG1129 350 NITLASLDRLSRGGLLDRRRERALAeeyikrlriktpSPEQP------VGNLSGGnqQK--VVLAKWLATDPKVLILDEP 421
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 167 TAGLDpMG---E-YRMMELLTrlnrDQGVTIVMAT 197
Cdd:COG1129 422 TRGID-VGakaEiYRLIRELA----AEGKAVIVIS 451
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-203 |
3.39e-11 |
|
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: 59.77 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENvlklhprdiyrKVGLVFQnpdd 91
Cdd:cd03221 7 SKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFEQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 qlfattvfedaafgprnmgcgdaevktrveaalasvdmaefagkgihnLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190
....*....|....*....|....*....|...
gi 1948769844 172 pmgeYRMMELLTR-LNRDQGvTIVMATHSVDLV 203
Cdd:cd03221 103 ----LESIEALEEaLKEYPG-TVILVSHDRYFL 130
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-196 |
4.94e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.73 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDG-TVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGL 84
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 85 VFQNPddQLFATTVFEDAAFgPRNMGCGDAEVKTRVEAALASvdmaEFAGK---GIH--------NLSYGQKKRVCIAGL 153
Cdd:PRK11176 422 VSQNV--HLFNDTIANNIAY-ARTEQYSREQIEEAARMAYAM----DFINKmdnGLDtvigengvLLSGGQRQRIAIARA 494
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1948769844 154 LAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVtIVMA 196
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIA 536
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-231 |
1.00e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKT-TLLKVMDgLIKGYKGEVLLDG-------ENVLKLHP------RDIY-RKVGLV 85
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMR-LLEQAGGLVQCDKmllrrrsRQVIELSEqsaaqmRHVRgADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNPDDQLFAT-TVFEDAAFGPR-NMGCGDAEVKTRVEAALASVDMAE---FAGKGIHNLSYGQKKRVCIAGLLAMGHEI 160
Cdd:PRK10261 110 FQEPMTSLNPVfTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 161 LLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-235 |
1.04e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLldgenvlklhpRDIYRKVGLVFQNPD-DQLFATTVfe 100
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQKLYlDTTLPLTV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 101 daafgPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMME 180
Cdd:PRK09544 87 -----NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 181 LLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRgRLIRGGAPEEVFTAPDELA 235
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPEFIS 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-171 |
1.27e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLldgenvlklhPRDIYrKVGLVFQNPdd 91
Cdd:TIGR03719 11 SKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR----------PQPGI-KVGYLPQEP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 QLFAT-TVFEDAAFGPR------------NMGCGD------------AEVKTRVEAALA-----SVDMAEFAGK------ 135
Cdd:TIGR03719 78 QLDPTkTVRENVEEGVAeikdaldrfneiSAKYAEpdadfdklaaeqAELQEIIDAADAwdldsQLEIAMDALRcppwda 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1948769844 136 GIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-198 |
1.80e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKlhPRDIYRKvGLVFQ------NPDDQLFA 95
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--DLCTYQK-QLCFVghrsgiNPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVFeDAAFGPRNMGcgdaevktrVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDpmgE 175
Cdd:PRK13540 94 NCLY-DIHFSPGAVG---------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---E 160
|
170 180
....*....|....*....|....*
gi 1948769844 176 YRMMELLTRL--NRDQGVTIVMATH 198
Cdd:PRK13540 161 LSLLTIITKIqeHRAKGGAVLLTSH 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-198 |
2.13e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGL--IKGYKGEVLLDGENVLKLHPRD--------IYRKVGLVfq 87
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRFKDIRDsealgiviIHQELALI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 88 nPddQL-FATTVF---EDAAFGPRNMgcgdAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLL 163
Cdd:NF040905 91 -P--YLsIAENIFlgnERAKRGVIDW----NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 164 DEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATH 198
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-195 |
3.19e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIKG-YKGEVLLDGENVLKLHPRD-IYRKVGLVfqnPDD--------------- 91
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPGkFEGNVFINGKPVDIRNPAQaIRAGIAMV---PEDrkrhgivpilgvgkn 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 92 ------QLFATTVFEDAAfgpRNMGCGDAEVKtRVEAALASVDMAefagkgIHNLSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:TIGR02633 360 itlsvlKSFCFKMRIDAA---AELQIIGSAIQ-RLKVKTASPFLP------IGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190
....*....|....*....|....*....|
gi 1948769844 166 PTAGLDPMGEYRMMELLTRLNRdQGVTIVM 195
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQ-EGVAIIV 458
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-173 |
3.66e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.10 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPD-GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKgYKGEVLLDGENVLKLhPRDIYRKV-GLVFQNp 89
Cdd:cd03289 9 TAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSV-PLQKWRKAfGVIPQK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 ddqlfattVFEDAAFGPRNM---GC-GDAEV-KTRVEAALASVdMAEFAGK-------GIHNLSYGQKKRVCIAGLLAMG 157
Cdd:cd03289 86 --------VFIFSGTFRKNLdpyGKwSDEEIwKVAEEVGLKSV-IEQFPGQldfvlvdGGCVLSHGHKQLMCLARSVLSK 156
|
170
....*....|....*.
gi 1948769844 158 HEILLLDEPTAGLDPM 173
Cdd:cd03289 157 AKILLLDEPSAHLDPI 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-263 |
4.38e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQ-NPDDQLFAttvfedaafG 105
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQrNNTDMLSP---------G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 PRNMGCGDAEV-------KTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRM 178
Cdd:PRK10938 95 EDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 179 MELLTRLNRdQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVftapdeLANVklrlphiaeLIYQLKHEEGFS 258
Cdd:PRK10938 175 AELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI------LQQA---------LVAQLAHSEQLE 238
|
....*
gi 1948769844 259 FSRLP 263
Cdd:PRK10938 239 GVQLP 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-197 |
5.20e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 19 TVALAEMRLEIRRGEFTGILGSNGSGKTTLLkvmdGLIKGYK----GEV-LLDGENVLKLHPRDIYRKVGLVFQNPDDQL 93
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLL----SLIAGARkiqqGRVeVLGGDMADARHRRAVCPRIAYMPQGLGKNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 94 FAT-TVFEDAAFGPRNMGCGDAEVKTRVEAALASVDMAEF----AGKgihnLSYG--QKKRVCIAgLLamgH--EILLLD 164
Cdd:NF033858 90 YPTlSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFadrpAGK----LSGGmkQKLGLCCA-LI---HdpDLLILD 161
|
170 180 190
....*....|....*....|....*....|....
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNRDQ-GVTIVMAT 197
Cdd:NF033858 162 EPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT 195
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-234 |
5.49e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 58.38 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPddQLFATTVFED 101
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP--ILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 aaFGPRNMgCGD---------AEVKTRVEAALASVDmaEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP 172
Cdd:cd03288 115 --LDPECK-CTDdrlwealeiAQLKNMVKSLPGGLD--AVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 173 MGEYRMMELLTRLNRDQgvTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFTAPDEL 234
Cdd:cd03288 190 ATENILQKVVMTAFADR--TVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENLLAQEDGV 248
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-231 |
7.15e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 24 EMRLEIRRGEFTGILGSNGSGKT-TLLKVMDGL----IKGYKGEVLLDGENVLKLHPRDIYR----KVGLVFQNP----- 89
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLpsppVVYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPmvsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 -----DDQLFATTVF-----EDAAFGpRNMGCGDaevktRVEAALASVDMAEFAgkgiHNLSYGQKKRVCIAGLLAMGHE 159
Cdd:PRK15134 107 plhtlEKQLYEVLSLhrgmrREAARG-EILNCLD-----RVGIRQAAKRLTDYP----HQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 160 ILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEVFTAP 231
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-229 |
8.65e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 28 EIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPddQLFATTV-FEDAAFGP 106
Cdd:PLN03130 1261 EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAP--VLFSGTVrFNLDPFNE 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 107 RNmgcgDAEVKTRVEAA-LASV--------DmAEFAGKGiHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDpmgeYR 177
Cdd:PLN03130 1339 HN----DADLWESLERAhLKDVirrnslglD-AEVSEAG-ENFSVGQRQLLSLARALLRRSKILVLDEATAAVD----VR 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 178 MMELLTRLNRDQ--GVTIVMATHSVDLVpIFLHQLHILSRGRLIRGGAPEEVFT 229
Cdd:PLN03130 1409 TDALIQKTIREEfkSCTMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-202 |
8.95e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKvGLVFqNPDDQLF-----ATTVFED 101
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRA-GIML-CPEDRKAegiipVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 AAFGPR----NMGCgdaEVKTRVEAALASVDMAEFAGKG------IHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PRK11288 352 INISARrhhlRAGC---LINNRWEAENADRFIRSLNIKTpsreqlIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190
....*....|....*....|....*....|.
gi 1948769844 172 PMGEYRMMELLTRLnRDQGVTIVMAthSVDL 202
Cdd:PRK11288 429 VGAKHEIYNVIYEL-AAQGVAVLFV--SSDL 456
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-179 |
9.39e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRL-----EIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDgenvLKL--HPRDIYRKV-GLV 85
Cdd:PRK13409 342 EYPDLTKKLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKIsyKPQYIKPDYdGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 fqnpDDQLFATTVFEDAAFgprnmgcgdaeVKTRVEAALASVDMAEfagKGIHNLSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:PRK13409 418 ----EDLLRSITDDLGSSY-----------YKSEIIKPLQLERLLD---KNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170
....*....|....
gi 1948769844 166 PTAGLDPmgEYRMM 179
Cdd:PRK13409 480 PSAHLDV--EQRLA 491
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-171 |
1.75e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 36 GILGSNGSGKTTLLKVMDGLIKGYKGE-VLLDGenvlklhprdiyRKVGLVFQNPddQLFAT-TVFE--DAAFGPR---- 107
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG------------IKVGYLPQEP--QLDPEkTVREnvEEGVAEVkaal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 108 --------NMGCGDAEV------KTRVEAALAS---------VDMAEFA------GKGIHNLSYGQKKRVCIAGLLAMGH 158
Cdd:PRK11819 103 drfneiyaAYAEPDADFdalaaeQGELQEIIDAadawdldsqLEIAMDAlrcppwDAKVTKLSGGERRRVALCRLLLEKP 182
|
170
....*....|...
gi 1948769844 159 EILLLDEPTAGLD 171
Cdd:PRK11819 183 DMLLLDEPTNHLD 195
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-219 |
2.01e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDDQLFATTVFE 100
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 101 DAAFGprnmgcGDAEVKTRVEAALASV-----DMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:PRK11614 100 NLAMG------GFFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1948769844 176 YRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:PRK11614 174 QQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-227 |
2.29e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 12 SYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK-VGLVfqnPD 90
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYI---PE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 DQL-------------FATTVFEDAAFGPRNMgcgdaeVKTRVEAALASVDMAEFA--GKGIH----NLSYG--QKkrVC 149
Cdd:COG3845 341 DRLgrglvpdmsvaenLILGRYRRPPFSRGGF------LDRKAIRAFAEELIEEFDvrTPGPDtparSLSGGnqQK--VI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 150 IAGLLAMGHEILLLDEPTAGLDPMG-EY---RMMELltrlnRDQGVTIVMAthSVDLVPIFL--HQLHILSRGRLIRGGA 223
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAiEFihqRLLEL-----RDAGAAVLLI--SEDLDEILAlsDRIAVMYEGRIVGEVP 485
|
....
gi 1948769844 224 PEEV 227
Cdd:COG3845 486 AAEA 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-195 |
2.50e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIKG-YKGEVLLDGENVLKLHPRDIYR-----------KVGLVfqnPD------ 90
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAYPGrWEGEIFIDGKPVKIRNPQQAIAqgiamvpedrkRDGIV---PVmgvgkn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 91 ------DQLFATTVFEDAAfgprNMGCGDAEVKtRVEAALASVDMAefagkgIHNLSYGQKKRVCIAGLLAMGHEILLLD 164
Cdd:PRK13549 362 itlaalDRFTGGSRIDDAA----ELKTILESIQ-RLKVKTASPELA------IARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190
....*....|....*....|....*....|.
gi 1948769844 165 EPTAGLDPMGEYRMMELLTRLNRdQGVTIVM 195
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQ-QGVAIIV 460
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-222 |
3.46e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 17 DGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLiKGYK---GEVLLDGENVLKLHPRDIYRK-VGLVFQNP--- 89
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEvtgGTVEFKGKDLLELSPEDRAGEgIFMAFQYPvei 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 ---DDQLFATTVFedaafgprnmgcgDAEVKTRVEAALASVDMAEFAGKGIHNL---------------SYGQKKRVCIA 151
Cdd:PRK09580 91 pgvSNQFFLQTAL-------------NAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 152 GLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHS---VDLV-PIFlhqLHILSRGRLIRGG 222
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYqriLDYIkPDY---VHVLYQGRIVKSG 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-198 |
3.56e-09 |
|
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: 57.10 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KYPDGTVALAEMRL-----EIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDgenvLKLhprdiyrkvglvfqn 88
Cdd:COG1245 343 EYPDLTKSYGGFSLeveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKI--------------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 89 pddqlfattvfedaAFGPRNMGcGDAEVktRVEAALASVDMAEFAGK----------GIH--------NLSYGQKKRVCI 150
Cdd:COG1245 404 --------------SYKPQYIS-PDYDG--TVEEFLRSANTDDFGSSyykteiikplGLEklldknvkDLSGGELQRVAI 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1948769844 151 AGLLAMGHEILLLDEPTAGLDPmgEYRMM--ELLTRLNRDQGVTIVMATH 198
Cdd:COG1245 467 AACLSRDADLYLLDEPSAHLDV--EQRLAvaKAIRRFAENRGKTAMVVDH 514
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
61-200 |
3.62e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 61 GEVLLDGENVLKLHPRDIYRKVGLVFQNPddQLFATTVFEDAAFGPRNM-------GCGDAEVKTRVEAALASVDMAefA 133
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEDAtredvkrACKFAAIDEFIESLPNKYDTN--V 1352
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 134 GKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIVMATHSV 200
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-173 |
9.31e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.07 E-value: 9.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 14 KY-PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGyKGEVLLDGE--NVLKLHPrdiYRKV-GLVFQnp 89
Cdd:TIGR01271 1226 KYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVswNSVTLQT---WRKAfGVIPQ-- 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 ddQLFATTVFEDAAFGPRNMgCGDAEV-KTRVEAALASVdMAEFAGK-------GIHNLSYGQKKRVCIAGLLAMGHEIL 161
Cdd:TIGR01271 1300 --KVFIFSGTFRKNLDPYEQ-WSDEEIwKVAEEVGLKSV-IEQFPDKldfvlvdGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170
....*....|..
gi 1948769844 162 LLDEPTAGLDPM 173
Cdd:TIGR01271 1376 LLDEPSAHLDPV 1387
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-171 |
1.13e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIKGYK----GEVLLDGenvlkLHPRDIYR--KVGLVFQNPDDQLFAT-TVFED 101
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDG-----ITPEEIKKhyRGDVVYNAETDVHFPHlTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 AAF-----GPRNMGCGDAEvKTRVEaALASVDMAEF----------AGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEP 166
Cdd:TIGR00956 159 LDFaarckTPQNRPDGVSR-EEYAK-HIADVYMATYglshtrntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
....*
gi 1948769844 167 TAGLD 171
Cdd:TIGR00956 237 TRGLD 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-243 |
1.59e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRK-VGLVFQNPDDQLFAT--TVFEDAAFG 105
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITESRRDNGFFPnfSIAQNMAIS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 106 P--RNMGCGDAE--VKTRVEAALASVDMAEFAGK------GIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGE 175
Cdd:PRK09700 366 RslKDGGYKGAMglFHEVDEQRTAENQRELLALKchsvnqNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948769844 176 YRMMELLTRLNrDQGVTIVMAthSVDLVPIflhqLHILSRGRLIRGGAPEEVFTAPDELAN---VKLRLPH 243
Cdd:PRK09700 446 AEIYKVMRQLA-DDGKVILMV--SSELPEI----ITVCDRIAVFCEGRLTQILTNRDDMSEeeiMAWALPQ 509
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-228 |
2.78e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLldgenvlklhprDIYRKVGLVFQNPddQLFATTVFED 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSV------------VIRGSVAYVPQVS--WIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 102 AAFGP-----RNMGCGDAEVKTRVEAALASVDMAEFAGKGIhNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEY 176
Cdd:PLN03232 699 ILFGSdfeseRYWRAIDVTALQHDLDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 177 RMMELLTRlNRDQGVTIVMATHSVDLVPIfLHQLHILSRGRLIRGGAPEEVF 228
Cdd:PLN03232 778 QVFDSCMK-DELKGKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFAELS 827
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-216 |
8.89e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 30 RRGEFTGILGSNGSGKTTLLKVMDGL-IKGY-KGEVLLDGenvlklHPRD---IYRKVGLVFQNpDDQLFATTVFEDAAF 104
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRkTGGYiEGDIRISG------FPKKqetFARISGYCEQN-DIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 105 G-----PRNMGCGDA-----EVKTRVEaaLASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMG 174
Cdd:PLN03140 977 SaflrlPKEVSKEEKmmfvdEVMELVE--LDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1948769844 175 EYRMMELLtRLNRDQGVTIVMATH--SVDLVPIFlHQLHILSRG 216
Cdd:PLN03140 1055 AAIVMRTV-RNTVDTGRTVVCTIHqpSIDIFEAF-DELLLMKRG 1096
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-206 |
1.09e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLklhprdIYRKVGLvfqnpDDQLfatTVFE 100
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL------IAISSGL-----NGQL---TGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 101 DAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEP-TAG--------LD 171
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVGdqtftkkcLD 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 172 PMGEYrmmelltrlnRDQGVTIVMATHSVDLVPIF 206
Cdd:PRK13545 185 KMNEF----------KEQGKTIFFISHSLSQVKSF 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-204 |
1.28e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 23 AEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKvGLVFQNPDDQlfATTVFEDA 102
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-GLVYLPEDRQ--SSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 103 -------AFGPRNMG-----CGDAEVKTRVEAALaSVDMAEfAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:PRK15439 357 plawnvcALTHNRRGfwikpARENAVLERYRRAL-NIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190
....*....|....*....|....*....|....
gi 1948769844 171 DPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVP 204
Cdd:PRK15439 435 DVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIE 467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-234 |
1.60e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPddQLFATTV------FEDA 102
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP--VLFDGTVrqnvdpFLEA 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 103 AfgprnmgcgDAEvktrVEAALASVDM-----AEFAG------KGIHNLSYGQKKRVCIA-GLLAMGHEILLLDEPTAGL 170
Cdd:PTZ00243 1411 S---------SAE----VWAALELVGLrervaSESEGidsrvlEGGSNYSVGQRQLMCMArALLKKGSGFILMDEATANI 1477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1948769844 171 DPMgeyrmmelltrLNRDQGVTiVMATHSVDLVPIFLHQLH---------ILSRGRLIRGGAPEEVFTAPDEL 234
Cdd:PTZ00243 1478 DPA-----------LDRQIQAT-VMSAFSAYTVITIAHRLHtvaqydkiiVMDHGAVAEMGSPRELVMNRQSI 1538
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-209 |
2.97e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 35 TGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLH-PRDIY--RKVGLVFQnpddqlfaTTVFEDAAFGprnmgc 111
Cdd:PRK13541 29 TYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPYCTYigHNLGLKLE--------MTVFENLKFW------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 112 gdAEVKTRVE---AALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPmgEYRmmELLTRLnrd 188
Cdd:PRK13541 95 --SEIYNSAEtlyAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK--ENR--DLLNNL--- 165
|
170 180
....*....|....*....|.
gi 1948769844 189 qgvtIVMATHSVDLVPIFLHQ 209
Cdd:PRK13541 166 ----IVMKANSGGIVLLSSHL 182
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-171 |
3.55e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 15 YPDGTVALAEMRLEI---------------RRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD-- 77
Cdd:PRK10762 246 YPRLDKAPGEVRLKVdnlsgpgvndvsftlRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgl 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 78 ----IY----RKV-GLVF-----QNPddQLFATTVFEDAAFGPR----NMGCGDA----EVKTrveaalASVDMAefagk 135
Cdd:PRK10762 326 angiVYisedRKRdGLVLgmsvkENM--SLTALRYFSRAGGSLKhadeQQAVSDFirlfNIKT------PSMEQA----- 392
|
170 180 190
....*....|....*....|....*....|....*.
gi 1948769844 136 gIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PRK10762 393 -IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-202 |
3.61e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 27 LEIRRGEFTGILGSNGSGKTTLLKvmDGLIKgyKGEVLLdgENVLKLHPRDIyrkvgLVFQnpdDQLFATTvfedaafgp 106
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKSTLVN--EGLYA--SGKARL--ISFLPKFSRNK-----LIFI---DQLQFLI--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 107 rNMGCGdaevKTRVEAALASvdmaefagkgihnLSYGQKKRVCIAGLLA--MGHEILLLDEPTAGLDPMGEYRMMELLTR 184
Cdd:cd03238 73 -DVGLG----YLTLGQKLST-------------LSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKG 134
|
170
....*....|....*...
gi 1948769844 185 LnRDQGVTIVMATHSVDL 202
Cdd:cd03238 135 L-IDLGNTVILIEHNLDV 151
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-204 |
1.61e-06 |
|
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: 49.17 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGEnvLKLHPRDIY-----RKVGLVFQNPDDQLFAT 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQAWiqndsLRENILFGKALNEKYYQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 TVFEDAAFGPrnmgcgDAEVktrveaaLASVDMAEFAGKGIhNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDP-MGE 175
Cdd:TIGR00957 732 QVLEACALLP------DLEI-------LPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGK 797
|
170 180
....*....|....*....|....*....
gi 1948769844 176 YRMMELLTRLNRDQGVTIVMATHSVDLVP 204
Cdd:TIGR00957 798 HIFEHVIGPEGVLKNKTRILVTHGISYLP 826
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
26-216 |
2.43e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.07 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 26 RLEIR-RGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDDQLFATTVFEDAaf 104
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSLLSRLLRLLLKEED-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 105 gPRNMGCGDAEVKTRVEAALASV--DMAEFAGKG---------------------------------IHNLSYGQKKRVC 149
Cdd:COG3593 94 -KEELEEALEELNEELKEALKALneLLSEYLKELldgldlelelsldeledllkslslriedgkelpLDRLGSGFQRLIL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948769844 150 IAGLLAM-------GHEILLLDEPTAGLDPMGEYRMMELLTRLNRdQGVTIVMATHSVDLVPIF-LHQLHILSRG 216
Cdd:COG3593 173 LALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSE-KPNQVIITTHSPHLLSEVpLENIRRLRRD 246
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-216 |
2.49e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.59 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 16 PDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVfqnpDDQLfa 95
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTL----RDQI-- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 ttVFEDAAFGPRNMGCGDAEvktrVEAALASVDMAEFAGKG-----IHN----LSYGQKKRVCIAGLLAMGHEILLLDEP 166
Cdd:TIGR00954 536 --IYPDSSEDMKRRGLSDKD----LEQILDNVQLTHILEREggwsaVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1948769844 167 TAGLDPMGEYRMMELLtrlnRDQGVTIVMATHSVDLVPIFLHQLHILSRG 216
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLC----REFGITLFSVSHRKSLWKYHEYLLYMDGRG 655
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
137-203 |
3.11e-06 |
|
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: 47.77 E-value: 3.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 137 IHNLSYGQKKRVCIAGLL---AMGHEILLLDEPTAGLDPMGEYRMMELLtRLNRDQGVTIVMATHSVDLV 203
Cdd:pfam13304 234 AFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELL-KELSRNGAQLILTTHSPLLL 302
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-219 |
3.25e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENV-LKLHPRDIYRKVGLVFQNPdDQLFAT 96
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQEL-NLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 97 TVFEDAAFG--PRNMGCGDAEVKTR-VEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPM 173
Cdd:PRK10982 89 SVMDNMWLGryPTKGMFVDQDKMYRdTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1948769844 174 GEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLI 219
Cdd:PRK10982 169 EVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-196 |
4.55e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 3 DTRisVDLESYKypdgtvalaEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLL-DGENVLKLHPRDIYRK 81
Cdd:PTZ00265 393 DTR--KDVEIYK---------DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 82 VGLVFQNP----------------------------DDQLFATTVFEDAAFGPRNMGCGD-------------AEVKTRV 120
Cdd:PTZ00265 462 IGVVSQDPllfsnsiknnikyslyslkdlealsnyyNEDGNDSQENKNKRNSCRAKCAGDlndmsnttdsnelIEMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 121 EAALAS--VDMAE-----------------FAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMEL 181
Cdd:PTZ00265 542 QTIKDSevVDVSKkvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250
....*....|....*.
gi 1948769844 182 LTRLNRDQG-VTIVMA 196
Cdd:PTZ00265 622 INNLKGNENrITIIIA 637
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-213 |
5.97e-06 |
|
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: 45.43 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 31 RGEFTGILGSNGSGKTTLLkvmdglikgykgevlldgenvlklhprdiyRKVGLVfqnpddqlfattVFEDAAFGPRNMG 110
Cdd:cd03227 20 EGSLTIITGPNGSGKSTIL------------------------------DAIGLA------------LGGAQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 111 CGDAEVKTRVEAALASVdmaefagkgIHNLSYGQKKRVCIAGLLAMGHE----ILLLDEPTAGLDPMGEYRMMELLtRLN 186
Cdd:cd03227 58 VKAGCIVAAVSAELIFT---------RLQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAI-LEH 127
|
170 180
....*....|....*....|....*..
gi 1948769844 187 RDQGVTIVMATHSVDLVPIFLHQLHIL 213
Cdd:cd03227 128 LVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-218 |
7.25e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 6 ISVDLESYKYPDGTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLldgenvlklhpRDIYRKVGLV 85
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 86 FQNPDDQLfattvfeDAAFGP--RNMGCGDAEVKTRVEAALASVDMA-EFAGKGIHNLSYGQKKRVCIAGLLAMGHEILL 162
Cdd:PLN03073 578 SQHHVDGL-------DLSSNPllYMMRCFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 163 LDEPTAGLDPMGEYRMMELLTRLnrdQGvTIVMATHSVDLVPIFLHQLHILSRGRL 218
Cdd:PLN03073 651 LDEPSNHLDLDAVEALIQGLVLF---QG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-180 |
9.91e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.00 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGEnvlklhprdiyrkvgLVFQNPDDQLFATT 97
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---------------ISFSSQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 98 VFEDAAFGprnMGCGDAEVKTRVEAALASVDMAEFA-------GKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGL 170
Cdd:cd03291 114 IKENIIFG---VSYDEYRYKSVVKACQLEEDITKFPekdntvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170
....*....|
gi 1948769844 171 DPMGEYRMME 180
Cdd:cd03291 191 DVFTEKEIFE 200
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-240 |
1.49e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 135 KGIHNLSYGQKKRVCIAGLLamGHEIL----LLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQL 210
Cdd:PRK00635 472 RALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISLADRII 548
|
90 100 110
....*....|....*....|....*....|....*
gi 1948769844 211 HILSR-----GRLIRGGAPEEVFTAPDELANVKLR 240
Cdd:PRK00635 549 DIGPGagifgGEVLFNGSPREFLAKSDSLTAKYLR 583
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-194 |
1.98e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 29 IRRGEFTGILGSNGSGKTTLLKVMDGLIK----GYKGEVllDGENVLKLhprdiYRkvGLVFQNpddqlfattVFEDAAF 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEP--SWDEVLKR-----FR--GTELQN---------YFKKLYN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 105 G--------------PRnmgcgdaEVKTRVEAALASVD-------------MAEFAGKGIHNLSYGQKKRVCIAGLLAMG 157
Cdd:PRK13409 158 GeikvvhkpqyvdliPK-------VFKGKVRELLKKVDergkldevverlgLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 1948769844 158 HEILLLDEPTAGLDPMGEYRMMELLTRLNRDQGVTIV 194
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVV 267
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
140-203 |
2.90e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 2.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 140 LSYGQKKRVCIAGLLAM---GHEILLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLV 203
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVI 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-173 |
3.22e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 28 EIRRGEFTGILGSNGSGKTTLLKVMDG-LIKGYKGEVLL------DGENVLklhprDIYRKVGLVfqnpDDQL-----FA 95
Cdd:PRK10938 282 QVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLfgrrrgSGETIW-----DIKKHIGYV----SSSLhldyrVS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 96 TTVfedaafgpRNM---GCGDA-----EVKTR----VEAALASVDM-AEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILL 162
Cdd:PRK10938 353 TSV--------RNVilsGFFDSigiyqAVSDRqqklAQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
170
....*....|.
gi 1948769844 163 LDEPTAGLDPM 173
Cdd:PRK10938 425 LDEPLQGLDPL 435
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-227 |
3.34e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 21 ALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGE-NVLKLHprdiyrkVGLvfqnpDDQLfatTVF 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAIS-------AGL-----SGQL---TGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 100 EDAAFGPRNMGCGDAEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDEPTA---------GL 170
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSvgdqtfaqkCL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1948769844 171 DPMGEYrmmelltrlnRDQGVTIVMATHSVDLVPIFLHQLHILSRGRLIRGGAPEEV 227
Cdd:PRK13546 184 DKIYEF----------KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-186 |
4.29e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 5 RISVDLE--SYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLdGENVlklhprdiyrKV 82
Cdd:PRK15064 317 RNALEVEnlTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-SENA----------NI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 83 GLVFQNPDDQlFAT--TVFEDAAfGPRNMGCGDAEVKTRVEAALASVDMaefAGKGIHNLSYGQKKRVCIAGLLAMGHEI 160
Cdd:PRK15064 385 GYYAQDHAYD-FENdlTLFDWMS-QWRQEGDDEQAVRGTLGRLLFSQDD---IKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180
....*....|....*....|....*.
gi 1948769844 161 LLLDEPTAGLDpmgeyrmMELLTRLN 186
Cdd:PRK15064 460 LVMDEPTNHMD-------MESIESLN 478
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-171 |
6.01e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 22 LAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDG-LIKGYKGEVLLDGenvlklhprdiyrKVGLVFQNpdDQLFATTVFE 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG-------------TVAYVPQV--SWIFNATVRD 697
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 101 DAAFG-----PRNMGCGDAEVKTRVEAALASVDMAEFAGKGIhNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLD 171
Cdd:PLN03130 698 NILFGspfdpERYERAIDVTALQHDLDLLPGGDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-194 |
7.99e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 7.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1948769844 137 IHNLSYGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMELLTRL-NRDQGVTIV 194
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIII 447
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-198 |
1.03e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 18 GTVALAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENVLKLHPRD--------IYRKVGLVfqnp 89
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagigiIHQELNLI---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 90 dDQLfatTVFEDAAFG--PRN-MGCGD-AEVKTRVEAALASVDMAEFAGKGIHNLSYGQKKRVCIAGLLAMGHEILLLDE 165
Cdd:PRK10762 92 -PQL---TIAENIFLGreFVNrFGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190
....*....|....*....|....*....|...
gi 1948769844 166 PTAGLDPMGEYRMMELLTRLnRDQGVTIVMATH 198
Cdd:PRK10762 168 PTDALTDTETESLFRVIREL-KSQGRGIVYISH 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
14-70 |
2.38e-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: 41.02 E-value: 2.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1948769844 14 KYPDGTVALAEMRLEIRRGEFT-----GILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGENV 70
Cdd:cd03222 2 LYPDCVKRYGVFFLLVELGVVKegeviGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP 63
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
140-203 |
2.75e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 2.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948769844 140 LSYGQKKRVCIAGLLAMGHE--ILLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLV 203
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTI 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-213 |
5.89e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.28 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 31 RGEFTGILGSNGSGKTTLLK-VMDGLIKGYKGEVLLDGENVLKLHPRDIYRKVGLVFQNPDDQlfattvfedaafgprnm 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 110 gcgdaevktrveaalasvdmaefagkgihnlsyGQKKRVCIAGLLAMGHEILLLDEPTAGLDPMGEYRMMEL-----LTR 184
Cdd:smart00382 64 ---------------------------------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLL 110
|
170 180 190
....*....|....*....|....*....|....*
gi 1948769844 185 LNRDQGVTIVMATHSVD------LVPIFLHQLHIL 213
Cdd:smart00382 111 LKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLL 145
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-57 |
1.33e-03 |
|
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: 40.15 E-value: 1.33e-03
10 20
....*....|....*....|....*...
gi 1948769844 30 RRGEFTGILGSNGSGKTTLLKVMDGLIK 57
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELK 124
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-227 |
1.98e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 140 LSYGQKKRVCIAGLL---AMGHEILLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVPIFLHQLHI---- 212
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIKTADYIIDLgpeg 908
|
90
....*....|....*.
gi 1948769844 213 -LSRGRLIRGGAPEEV 227
Cdd:TIGR00630 909 gDGGGTVVASGTPEEV 924
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-240 |
2.76e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 140 LSYGQKKRVCIA-----GLLAMgheILLLDEPTAGLDPMGEYRMMELLTRLnRDQGVTIVMATHSVDLVpifLHQLHILS 214
Cdd:TIGR00630 489 LSGGEAQRIRLAtqigsGLTGV---LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTI---RAADYVID 561
|
90 100 110
....*....|....*....|....*....|....
gi 1948769844 215 --------RGRLIRGGAPEEVFTAPDELANVKLR 240
Cdd:TIGR00630 562 igpgagehGGEVVASGTPEEILANPDSLTGQYLS 595
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-198 |
4.81e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.39 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 5 RISVDLE--SYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLLDGEnvLKLHPRDIYRKV 82
Cdd:PRK11147 317 KIVFEMEnvNYQIDGKQL-VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK--LEVAYFDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948769844 83 glvfQNPDdqlfaTTVFEDAAFGPRnmgcgDAEVKTRVEAALASVDMAEFAGK----GIHNLSYGQKKRVCIAGLLAMGH 158
Cdd:PRK11147 394 ----LDPE-----KTVMDNLAEGKQ-----EVMVNGRPRHVLGYLQDFLFHPKramtPVKALSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1948769844 159 EILLLDEPTAGLDpmgeYRMMELLTRLNRD-QGvTIVMATH 198
Cdd:PRK11147 460 NLLILDEPTNDLD----VETLELLEELLDSyQG-TVLLVSH 495
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-65 |
9.91e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 9.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1948769844 12 SYKYPDGTVaLAEMRLEIRRGEFTGILGSNGSGKTTLLKVMDGLIKGYKGEVLL 65
Cdd:PRK10636 319 SAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| |
