|
Name |
Accession |
Description |
Interval |
E-value |
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-251 |
2.69e-178 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 489.63 E-value: 2.69e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDT 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 81 TLPLTVNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAPEVVSMHPEFISMFGPRGAEQLGIYRHHHNHRHDLQG 240
Cdd:PRK09544 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVVSLHPEFISMFGPRGAEQLGIYRHHHNHRHDLQG 240
|
250
....*....|.
gi 446125168 241 RIVLRRGNGHS 251
Cdd:PRK09544 241 RIVLRRGNDRS 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
7.04e-84 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 250.39 E-value: 7.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------LRIGYVPQ 74
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KLYLDTTLPLTV-----------NRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
Cdd:COG1121 83 RAEVDWDFPITVrdvvlmgrygrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAPEVVsMHPEFIS 215
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEV-LTPENLS 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-202 |
2.23e-83 |
|
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: 247.83 E-value: 2.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------LRIGYVPQKLYLD 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 80 TTLPLTVNRFLRLR-----------PGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
Cdd:cd03235 81 RDFPISVRDVVLMGlyghkglfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125168 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSG 202
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-215 |
6.15e-56 |
|
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: 179.47 E-value: 6.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------RIGYV 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLylDTTLPLTV------NRFLRLRPGTQKTD-----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
Cdd:COG1120 81 PQEP--PAPFGLTVrelvalGRYPHLGLFGRPSAedreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVsMHPEFIS 215
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLkDGRIVAQGPPEEV-LTPELLE 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-205 |
9.64e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 178.33 E-value: 9.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LRIGYVPQ 74
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KLYLDTTlpLTVNRFLR-------LRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
Cdd:COG1131 81 EPALYPD--LTVRENLRffarlygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 148 TQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPD 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-196 |
1.09e-54 |
|
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: 173.78 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------RIGYVPQ 74
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkelarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 klyldttlpltvnrflrlrpgtqktdilpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125168 155 GQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-196 |
2.87e-50 |
|
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: 162.18 E-value: 2.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LRIGYVPQ 74
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkepeevkRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KLYLDTTlpLTVNRFLrlrpgtqktdilpalkrvqaghlidapmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
Cdd:cd03230 81 EPSLYEN--LTVRENL-----------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125168 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03230 130 SRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNN 170
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-193 |
3.84e-46 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 152.39 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 13 SFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDTTLPLTV------ 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVrdlvam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 87 NRFLRLRPGTQKT-----DILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
Cdd:NF040873 81 GRWARRGLWRRLTrddraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180 190
....*....|....*....|....*....|..
gi 446125168 162 LIDQLRRElDCAVLMVSHDLHLVMAKTDEVLC 193
Cdd:NF040873 161 LLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-195 |
2.42e-44 |
|
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: 148.20 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------QLRIGYVPQK-- 75
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaaRNRIGYLPEErg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 LYLDTTLPLTVNRFLRLRpGTQKTDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLK-GLKKEEARRRidewLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446125168 152 DVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd03269 160 DPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLN 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-196 |
2.75e-44 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 148.81 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSF----GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL------------ 67
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 --RIGYVPQKLY--LDTTL--------PLTVNRFLRlRPGTQKTDILPALKRVQ--AGHLIDAPMQkLSGGETQRVLLAR 133
Cdd:cd03257 81 rkEIQMVFQDPMssLNPRMtigeqiaePLRIHGKLS-KKEARKEAVLLLLVGVGlpEEVLNRYPHE-LSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125168 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-196 |
5.77e-44 |
|
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: 148.41 E-value: 5.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQ----RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------R 68
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkafrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLY--------LDTTL--PLTVNRFLRlrpgtQKTDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLN 137
Cdd:COG1124 81 VQMVFQDPYaslhprhtVDRILaePLRIHGLPD-----REERIAELLEQVGlPPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-180 |
7.06e-44 |
|
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: 146.86 E-value: 7.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL----------RIGYVP 73
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QKLYLDTTLPLTVN-RFL-RLRPGTQ-KTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
Cdd:COG4133 82 HADGLKPELTVRENlRFWaALYGLRAdREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|
gi 446125168 151 VDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
Cdd:COG4133 162 LDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-214 |
8.92e-44 |
|
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: 147.48 E-value: 8.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------RIGYV 72
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQklYLDTTL--PlTV---------NrfLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
Cdd:COG1122 81 FQ--NPDDQLfaP-TVeedvafgpeN--LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHH-ICCSGAPEVVSMHPEFI 214
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGrIVADGTPREVFSDYELL 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-205 |
5.16e-43 |
|
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: 152.99 E-value: 5.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR-VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGYV 72
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpasWRrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLdttLPLTVNRFLRL-RPGTQKTDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQ 140
Cdd:COG4988 417 PQNPYL---FAGTIRENLRLgRPDASDEELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCLNH-HICCSGAPE 205
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL-LAQADRILVLDDgRIVEQGTHE 556
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-196 |
6.45e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 6.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-------RIGYVPQK-- 75
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPldpedrrRIGYLPEErg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 LYLDTTLPLTVNRFLRLRpGTQKTDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
Cdd:COG4152 82 LYPKMKVGEQLVYLARLK-GLSKAEAKRRadewLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 152 D-VNGQVaLYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4152 161 DpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINK 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-211 |
3.64e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.78 E-value: 3.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------RIGY 71
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLdttLP-LTV--N-----RFLRLRPGTQKTDILPALKRVQAGHLIDA-PMQkLSGGETQRVLLARALLNRPQLL 142
Cdd:COG3842 82 VFQDYAL---FPhLTVaeNvafglRMRGVPKAEIRARVAELLELVGLEGLADRyPHQ-LSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLH--LVMAktDEVLCLNH-HICCSGAPEVVSMHP 211
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLALA--DRIAVMNDgRIEQVGTPEEIYERP 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
4.19e-42 |
|
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: 144.03 E-value: 4.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-------------- 66
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 -------------------LRIGYVPQklyLDTTLPLTVNRFLRLRPGTQKT--DILPALKRVQAGHLIDAPMQKLSGGE 125
Cdd:COG0411 81 iartfqnprlfpeltvlenVLVAAHAR---LGRGLLAALLRLPRARREEREAreRAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAP 204
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFgRVIAEGTP 237
|
250
....*....|
gi 446125168 205 EVVSMHPEFI 214
Cdd:COG0411 238 AEVRADPRVI 247
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-197 |
7.68e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 7.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------RIGYVPQ 74
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 K--LYLDT-----TLPLTvnrfLRLRPGTQKTdILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:COG4619 82 EpaLWGGTvrdnlPFPFQ----LRERKFDRER-ALELLERLGlPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125168 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-215 |
9.52e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 142.95 E-value: 9.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYVPQkl 76
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspwelaRRRAVLPQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 ylDTTL--PLTVNRFLRL------RPGTQKTDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALL-------NRPQ 140
Cdd:COG4559 83 --HSSLafPFTVEEVVALgraphgSSAAQDRQIVReALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVsMHPEFIS 215
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQgRLVAQGTPEEV-LTDELLE 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-212 |
1.46e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.51 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNGQ--------- 66
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 --LRIGYVPQKLylDTTL-PLTVN-------RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
Cdd:COG1123 81 rgRRIGMVFQDP--MTQLnPVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEILAAPQ 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-196 |
1.38e-40 |
|
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: 145.82 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQR-----RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL----------- 67
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 ---RIGYVPQKLY--LDTTL--------PLTVNRflRLRPGTQKTDILPALKRVQ--AGHLIDAPMQkLSGGETQRVLLA 132
Cdd:COG1123 340 lrrRVQMVFQDPYssLNPRMtvgdiiaePLRLHG--LLSRAERRERVAELLERVGlpPDLADRYPHE-LSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-195 |
1.71e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.61 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYVPQ 74
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdiaklpleelrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 klyldttlpltvnrflrlrpgtqktdilpalkrvqaghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446125168 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-183 |
2.78e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 138.25 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQ----RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------- 66
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 --LR---IGYVPQKLYLdttLP-LTV--N-----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLAR 133
Cdd:COG1136 81 arLRrrhIGFVFQFFNL---LPeLTAleNvalplLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125168 134 ALLNRPQLLVLDEPTQGVD-VNGQvALYDLIDQLRRELDCAVLMVSHDLHL 183
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDsKTGE-EVLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-197 |
3.50e-40 |
|
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: 137.60 E-value: 3.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYV 72
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKlyldttlP------LTVN-------RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
Cdd:cd03225 81 FQN-------PddqffgPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-194 |
3.66e-40 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 138.68 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV----------------IKRng 65
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 66 qlRIGYVPQKLYLDTTLPLTVN------------RFLRLRPgTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLAR 133
Cdd:COG1119 79 --RIGLVSPALQLRFPRDETVLdvvlsgffdsigLYREPTD-EQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-196 |
7.00e-40 |
|
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: 137.68 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------QLRIGYVP 73
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkepreaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QKLYLDTTlpLTVNRFLRL---------RPGTQKTDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
Cdd:COG4555 81 DERGLYDR--LTVRENIRYfaelyglfdEELKKRIEEL--IELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125168 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-214 |
1.42e-39 |
|
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: 137.03 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-------------- 66
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 LRIGYVPQK--LYLDttlpLTV--NRFLRLRpgtQKTDILPALKRVQAGHLIDA----------PMQkLSGGETQRVLLA 132
Cdd:COG1127 82 RRIGMLFQGgaLFDS----LTVfeNVAFPLR---EHTDLSEAEIRELVLEKLELvglpgaadkmPSE-LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVV--SM 209
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLaDGKIIAEGTPEELlaSD 233
|
....*...
gi 446125168 210 HP---EFI 214
Cdd:COG1127 234 DPwvrQFL 241
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-212 |
1.98e-39 |
|
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: 136.41 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRIGYVP 73
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QKLyldTTLP-LTV-------------NRFLRLRPGTQKTDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
Cdd:cd03219 82 QIP---RLFPeLTVlenvmvaaqartgSGLLLARARREEREAreraEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQgRVIAEGTPDEVRNNPR 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-181 |
2.23e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.14 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF----GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------LRIG 70
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQKlylDTTLP-LTV--N-----RFLRLRPGTQKTDILPALKRVQAGHLIDA-PMQkLSGGETQRVLLARALLNRPQL 141
Cdd:COG1116 84 VVFQE---PALLPwLTVldNvalglELRGVPKAERRERARELLELVGLAGFEDAyPHQ-LSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-184 |
1.09e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.02 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQ-RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR--I 69
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipyLRrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 70 GYVPQ--KLYLDTT------LPLTVnrfLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
Cdd:COG2884 82 GVVFQdfRLLPDRTvyenvaLPLRV---TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLV 184
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELV 200
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-211 |
1.64e-38 |
|
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: 134.17 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ--------------LRIG 70
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQK--LYLDttlpLTV--NRFLRLRPGTQKTD------ILPALKRV---QAGHLIDApmqKLSGGETQRVLLARALLN 137
Cdd:cd03261 81 MLFQSgaLFDS----LTVfeNVAFPLREHTRLSEeeireiVLEKLEAVglrGAEDLYPA---ELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVV--SMHP 211
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEGTPEELraSDDP 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-196 |
6.67e-38 |
|
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: 131.87 E-value: 6.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------RIGYVPQK 75
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 LYLdttLP-LTV--N-----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
Cdd:cd03259 81 YAL---FPhLTVaeNiafglKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125168 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-180 |
8.40e-38 |
|
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: 131.84 E-value: 8.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQ----RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR 68
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 ---IGYVPQKLYLdttLP-LTV--N-----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
Cdd:cd03255 81 rrhIGFVFQSFNL---LPdLTAleNvelplLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446125168 138 RPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSHD 180
Cdd:cd03255 158 DPKIILADEPTGNLDsETGKEVM-ELLRELNKEAGTTIVVVTHD 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-198 |
8.42e-38 |
|
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: 131.83 E-value: 8.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR----VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------LRIGYVPQ 74
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KlylDTTLP-LTVN-------RFLRLRPGTQKTDILPALKRVQAGHLIDA-PMQkLSGGETQRVLLARALLNRPQLLVLD 145
Cdd:cd03293 81 Q---DALLPwLTVLdnvalglELQGVPKAEARERAEELLELVGLSGFENAyPHQ-LSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125168 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHI 198
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI-------DEAVFLADRV 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-196 |
1.87e-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: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFG--QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGY 71
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldlesLRknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLdttlpltvnrFlrlrPGTQKTDIlpalkrvqaghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
Cdd:cd03228 81 VPQDPFL----------F----SGTIRENI-------------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125168 152 DVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03228 128 DPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-205 |
2.17e-37 |
|
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: 137.98 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR--IGY 71
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldedDLRrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYL-DTTLplTVNrfLRL-RPGTQKTDILPALKRVQAGHLI-------DAPM----QKLSGGETQRVLLARALLNR 138
Cdd:COG4987 414 VPQRPHLfDTTL--REN--LRLaRPDATDEELWAALERVGLGDWLaalpdglDTWLgeggRRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCL-NHHICCSGAPE 205
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAG-LERMDRILVLeDGRIVEQGTHE 554
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-196 |
2.65e-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: 129.23 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-------------RIGYVP 73
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplrrRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QKLYLDTTlpLTVNRFLRLRpgtqktdilpalkrvqaghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
Cdd:cd03229 83 QDFALFPH--LTVLENIALG---------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125168 154 NGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03229 134 ITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-192 |
2.88e-37 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 136.73 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKL-YLDTTL 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQeELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 PLtVNRFLRLRPGTQKTDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
Cdd:COG0488 395 TV-LDELRDGAPGGTEQEVRGYLGRFLfSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEE 473
|
170 180 190
....*....|....*....|....*....|.
gi 446125168 162 LIDqlrrELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:COG0488 474 ALD----DFPGTVLLVSHDRYFLDRVATRIL 500
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-166 |
1.51e-36 |
|
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: 128.46 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LRIGYVPQ 74
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KLyldTTLP-LTVNRFL-------RLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:cd03264 80 EF---GVYPnFTVREFLdyiawlkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180
....*....|....*....|
gi 446125168 147 PTQGVDVNGQVALYDLIDQL 166
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSEL 176
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-215 |
2.66e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 129.12 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYVPQKl 76
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelaRRRAVLPQH- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 yldTTL--PLTVNRFLRL-----RPGTQKTDILP--ALKRVQAGHLIDAPMQKLSGGETQRVLLARALL------NRPQL 141
Cdd:PRK13548 85 ---SSLsfPFTVEEVVAMgraphGLSRAEDDALVaaALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVsMHPEFIS 215
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQgRLVADGTPAEV-LTPETLR 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-197 |
4.76e-36 |
|
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: 124.87 E-value: 4.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQklyldttlpl 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 tvnrflrlrpgtqktdilpalkrvqaghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLId 164
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL- 113
|
170 180 190
....*....|....*....|....*....|...
gi 446125168 165 qlrRELDCAVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:cd03221 114 ---KEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-212 |
5.21e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 130.65 E-value: 5.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL----------RIGYVPQ 74
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnlpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KlYLdttL-P-LTV--N-RF-LRLRPGT-----QKTDILpaLKRVQAGHLIDA-PMQkLSGGETQRVLLARALLNRPQLL 142
Cdd:COG1118 83 H-YA---LfPhMTVaeNiAFgLRVRPPSkaeirARVEEL--LELVQLEGLADRyPSQ-LSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 143 VLDEPTQGVDVngQVAlYDLIDQLRR---ELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:COG1118 156 LLDEPFGALDA--KVR-KELRRWLRRlhdELGGTTVFVTHDQEEALELADRVVVMNQgRIEQVGTPDEVYDRPA 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-222 |
9.87e-36 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 131.12 E-value: 9.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYVP 73
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QK--LYLDTTLPLTV--------NRFLRLRPgTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
Cdd:PRK09536 84 QDtsLSFEFDVRQVVemgrtphrSRFDTWTE-TDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHPEFISMFGPRGA 222
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLaDGRVRAAGPPADVLTADTLRAAFDARTA 241
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-196 |
2.10e-35 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 133.04 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR--VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGY 71
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpasLRrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLdttlpltvnrF-------LRL-RPGTQKTDILPALKRVQAGHLIDA-PM----------QKLSGGETQRVLLA 132
Cdd:COG2274 554 VLQDVFL----------FsgtirenITLgDPDATDEEIIEAARLAGLHDFIEAlPMgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDK 684
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-191 |
2.87e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.29 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR 68
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYLdttLP-LTV----------NRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
Cdd:COG1129 81 IAIIHQELNL---VPnLSVaeniflgrepRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRV 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-180 |
4.52e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.96 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDTTLPL-- 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 -----------TVNRFLRLRPGTQKTDILPA-LKRVQA------------------------GHLIDAPMQKLSGGETQR 128
Cdd:COG0488 81 tvldgdaelraLEAELEELEAKLAEPDEDLErLAELQEefealggweaearaeeilsglgfpEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 129 VLLARALLNRPQLLVLDEPTQGVDVNGqvalydlIDQLRREL---DCAVLMVSHD 180
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLES-------IEWLEEFLknyPGTVLVVSHD 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-196 |
1.24e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.40 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR---- 68
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtalrgraLRrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 -IGYVPQKLYLdttlpltVNR--------------------FLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQ 127
Cdd:COG3638 81 rIGMIFQQFNL-------VPRlsvltnvlagrlgrtstwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 128 RVLLARALLNRPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDpKTARQVM-DLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-222 |
1.49e-34 |
|
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: 126.75 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 22 DVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------------RIGYVPQklylDTTLP--L 84
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQ----EARLFphL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 TVNRFL-----RLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
Cdd:COG4148 93 SVRGNLlygrkRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 160 YDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFISMFGPRGA 222
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQgRVVASGPLAEVLSRPDLLPLAGGEEA 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-191 |
3.89e-34 |
|
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: 120.61 E-value: 3.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRIGYV 72
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfasprdarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQklyldttlpltvnrflrlrpgtqktdilpalkrvqaghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:cd03216 81 YQ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125168 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:cd03216 115 PAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRV 152
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-205 |
4.71e-34 |
|
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: 122.09 E-value: 4.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKRNGQLR--IGYVPQKLY 77
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPREVRrrIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 LDTTLPLTVNRFLRLR----PGTQKTD-ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:cd03265 84 VDDELTGWENLYIHARlygvPGAERRErIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125168 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEGTPE 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-196 |
5.28e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 128.36 E-value: 5.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGYV 72
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltlesLRrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLdttLPLTV--NrfLRL-RPGTQKTDILPALKRVQAGHLIDA-PMQ----------KLSGGETQRVLLARALLNR 138
Cdd:COG1132 420 PQDTFL---FSGTIreN--IRYgRPDATDEEVEEAAKAAQAHEFIEAlPDGydtvvgergvNLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-NADRILVLDD 549
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-194 |
5.34e-34 |
|
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: 128.17 E-value: 5.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------RIGYV 72
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLdttLPLTVNRFLRL-RPGTQKTDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQ 140
Cdd:TIGR02857 402 PQHPFL---FAGTIAENIRLaRPDASDAEIREALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125168 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCL 194
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-205 |
7.42e-34 |
|
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: 121.77 E-value: 7.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRIGYVP 73
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppherarAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QKLYLDTTLP----LTVNRFLRLRPGTQKT-----DILPALK---RVQAGHlidapmqkLSGGETQRVLLARALLNRPQL 141
Cdd:cd03224 82 EGRRIFPELTveenLLLGAYARRRAKRKARlervyELFPRLKerrKQLAGT--------LSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 142 LVLDEPTQG-----VDVngqvaLYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:cd03224 154 LLLDEPSEGlapkiVEE-----IFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERgRVVLEGTAA 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-205 |
1.90e-33 |
|
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: 121.14 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQ-RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------QLR--IGY 71
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrQLRrqIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLdtTLPLTV---------------NRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
Cdd:cd03256 83 IFQQFNL--IERLSVlenvlsgrlgrrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDgRIVFDGPPA 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-148 |
2.78e-33 |
|
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: 118.13 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYVPQKLYLDTTLP----- 83
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrKEIGYVFQDPQLFPRLTvrenl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 84 LTVNRFLRLRPGTQKTDILPALKRVQAGHL----IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-191 |
3.06e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.52 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR 68
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaiaLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQklylDTTL--PLTV--NRFLRLRPGTQ-KTDILPALKRVQAghLI---------DAPMQKLSGGETQRVLLARA 134
Cdd:COG3845 82 IGMVHQ----HFMLvpNLTVaeNIVLGLEPTKGgRLDRKAARARIRE--LSerygldvdpDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 135 LLNRPQLLVLDEPT-----QGVDvngqvALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:COG3845 156 LYRGARILILDEPTavltpQEAD-----ELFEILRRLAAE-GKSIIFITHKLREVMAIADRV 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-196 |
3.61e-33 |
|
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: 120.09 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRI 69
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 70 GYVPQ--KLYLDttlpLTV--N-----RFLRLRPGTQKT-----DILPALK---RVQAGHlidapmqkLSGGETQRVLLA 132
Cdd:COG0410 81 GYVPEgrRIFPS----LTVeeNlllgaYARRDRAEVRADlervyELFPRLKerrRQRAGT--------LSGGEQQMLAIG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 133 RALLNRPQLLVLDEPTQG-----VDvngqvALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLER 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-217 |
4.33e-33 |
|
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: 120.03 E-value: 4.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LRIGYVPQK 75
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 LYLDTTLPLTVN-----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
Cdd:cd03300 81 YALFPHLTVFENiafglRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE--FISMF 217
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKgKIQQIGTPEEIYEEPAnrFVADF 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-217 |
6.39e-33 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 119.75 E-value: 6.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRrVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLRIGYVPQKLY 77
Cdd:cd03299 3 VENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppeKRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 LdttLP-LTVNRF----LRLRPGTQKTD---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:cd03299 82 L---FPhMTVYKNiaygLKKRKVDKKEIerkVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP--EFISMF 217
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNgKLIQVGKPEEVFKKPknEFVAEF 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-196 |
1.37e-32 |
|
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: 118.59 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 18 RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL----------RIGYV-PQKLYLDTTLPLT- 85
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkflrRIGVVfGQKTQLWWDLPVId 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 86 ----VNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
Cdd:cd03267 115 sfylLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190
....*....|....*....|....*....|....*
gi 446125168 162 LIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-196 |
2.29e-32 |
|
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: 117.85 E-value: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------QLRIGYVPQK--LYLDTTLPLTV 86
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaeaRRRLGFVSDStgLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 87 NRFLRLRpGTQKTDILPALK----RVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDL 162
Cdd:cd03266 100 EYFAGLY-GLKGDELTARLEeladRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190
....*....|....*....|....*....|....
gi 446125168 163 IDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03266 179 IRQL-RALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-195 |
2.65e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 116.97 E-value: 2.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFG-QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG--------QLRIGYVPQ-- 74
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerRKSIGYVMQdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 --KLYLDttlplTVNRFLRLR---PGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:cd03226 81 dyQLFTD-----SVREELLLGlkeLDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 150 GVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-182 |
6.63e-32 |
|
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: 116.16 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LRIGYV--P 73
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkniealRRIGALieA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QKLYLDttlpLTVNRFLRLR---PGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
Cdd:cd03268 81 PGFYPN----LTARENLRLLarlLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190
....*....|....*....|....*....|..
gi 446125168 151 VDVNGQVALYDLIDQLRRElDCAVLMVSHDLH 182
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLS 187
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-196 |
1.56e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.89 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVsfgqRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRIGY 71
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VP-----QKLYLD------TTLPL--TVNRFLRLRPGTQKTDILPALKR--VQAGHlIDAPMQKLSGGETQRVLLARALL 136
Cdd:COG1129 332 VPedrkgEGLVLDlsirenITLASldRLSRGGLLDRRRERALAEEYIKRlrIKTPS-PEQPVGNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRE 469
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-231 |
2.04e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 118.28 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKRNGQLR-IGYVP 73
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedVTHRSIQQRdICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QKLYLDTTLPLTVN-----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
Cdd:PRK11432 85 QSYALFPHMSLGENvgyglKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP--EFISMF-------- 217
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKgKIMQIGSPQELYRQPasRFMASFmgdanifp 244
|
250
....*....|....
gi 446125168 218 GPRGAEQLGIYRHH 231
Cdd:PRK11432 245 ATLSGDYVDIYGYR 258
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-152 |
2.35e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 115.51 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLvSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR 68
Cdd:COG1137 1 MMTL-EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQ------KLyldttlplTV--N--RFLRLRPGT-----QKTDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLAR 133
Cdd:COG1137 80 IGYLPQeasifrKL--------TVedNilAVLELRKLSkkereERLEEL--LEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....*....
gi 446125168 134 ALLNRPQLLVLDEPTQGVD 152
Cdd:COG1137 150 ALATNPKFILLDEPFAGVD 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-195 |
2.68e-31 |
|
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: 113.47 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFG--QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR--IGYV 72
Cdd:cd03246 2 EVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnELGdhVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKlyldttlpltvnrfLRLRPGTQKTDIlpalkrvqaghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:cd03246 82 PQD--------------DELFSGSIAENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125168 153 VNGQVALYDLIDQLrRELDCAVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:cd03246 129 VEGERALNQAIAAL-KAAGATRIVIAHRPETL-ASADRILVLE 169
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-212 |
3.01e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.88 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LRIGYVPQK 75
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 LYL--------DTTLPLTV-NRflRLRPGTQ--KTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
Cdd:PRK10851 83 YALfrhmtvfdNIAFGLTVlPR--RERPNAAaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQgNIEQAGTPDQVWREPA 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-182 |
4.01e-31 |
|
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: 114.59 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLV-----APDEGVIKRNGQ------------- 66
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 LRIGYVPQKLYLdttLPLTVNRFLRLRP---GTQKTDILP-----ALKRVqagHLIDAPMQK-----LSGGETQRVLLAR 133
Cdd:cd03260 81 RRVGMVFQKPNP---FPGSIYDNVAYGLrlhGIKLKEELDerveeALRKA---ALWDEVKDRlhalgLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125168 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDLH 182
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQ 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-152 |
4.55e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.24 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGQLRIGYVPQ 74
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KLYLDTTLPLTVN-----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:PRK13536 122 FDNLDLEFTVRENllvfgRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
...
gi 446125168 150 GVD 152
Cdd:PRK13536 202 GLD 204
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-196 |
2.05e-30 |
|
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: 114.79 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 14 FGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKRNGQLR--IGYVPQKLYLDTTLP 83
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGtarvagydVVREPRKVRrsIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 84 LTVN-----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
Cdd:TIGR01188 83 GRENlemmgRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 446125168 159 LYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:TIGR01188 163 IWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDH 199
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-217 |
2.82e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.81 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDTT 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 82 ------LP-LTV--NRFLRLRpgTQKT---DILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
Cdd:PRK09452 92 fqsyalFPhMTVfeNVAFGLR--MQKTpaaEITPrvmeALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE--FISMF 217
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDgRIEQDGTPREIYEEPKnlFVARF 244
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-217 |
3.52e-30 |
|
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: 112.78 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR-VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR--IGYV 72
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvELRrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLdttLP-LTVNRFLRLRPGTQKTDILPALKRV-QAGHLIDAPMQK--------LSGGETQRVLLARALLNRPQLL 142
Cdd:cd03295 81 IQQIGL---FPhMTVEENIALVPKLLKWPKEKIRERAdELLALVGLDPAEfadrypheLSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHICCSGAPEVV----------SMHPE 212
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDI-------DEAFRLADRIAIMKNGEIVqvgtpdeilrSPAND 230
|
....*
gi 446125168 213 FISMF 217
Cdd:cd03295 231 FVAEF 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-220 |
4.48e-30 |
|
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: 117.54 E-value: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QL--RIGY 71
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreELgrHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQklylDTTL-PLTV--N--RFLRLRPgtqkTDILPALKRVQAGHLI-------DAPM----QKLSGGETQRVLLARAL 135
Cdd:COG4618 411 LPQ----DVELfDGTIaeNiaRFGDADP----EKVVAAAKLAGVHEMIlrlpdgyDTRIgeggARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLvMAKTDEVLCLNHhiccsGApevvsmhpefIS 215
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSL-LAAVDKLLVLRD-----GR----------VQ 545
|
....*
gi 446125168 216 MFGPR 220
Cdd:COG4618 546 AFGPR 550
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-196 |
4.51e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 4.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSlVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------RIGY 71
Cdd:COG3839 1 MAS-LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQK--LYldttlP-LTV--N-RF-LRLRpGTQKTDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
Cdd:COG3839 80 VFQSyaLY-----PhMTVyeNiAFpLKLR-KVPKAEIdrrvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-184 |
5.95e-30 |
|
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: 113.99 E-value: 5.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQR----RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAP---DEGVIKRNGQ---------- 66
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdllklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 --LR---IGYVPQklylD--TTL-P-LTVNRFL--------RLRPGTQKTDILPALKRV---QAGHLIDA-PMQkLSGGE 125
Cdd:COG0444 81 rkIRgreIQMIFQ----DpmTSLnPvMTVGDQIaeplrihgGLSKAEARERAIELLERVglpDPERRLDRyPHE-LSGGM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVV 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-211 |
6.64e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 111.66 E-value: 6.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LRIGYVPQK 75
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqeRNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 --LYLDTTLPLTVNRFLRLRPGTQKTD-------ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:cd03296 83 yaLFRHMTVFDNVAFGLRVKPRSERPPeaeirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP 211
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKgRIEQVGTPDEVYDHP 228
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-152 |
8.58e-30 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 111.60 E-value: 8.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRIGYVPQ- 74
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlpmherarLGIGYLPQe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 -----KLYLDTTLPLTVNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:TIGR04406 85 asifrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
...
gi 446125168 150 GVD 152
Cdd:TIGR04406 165 GVD 167
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-196 |
1.33e-29 |
|
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: 110.42 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQlRIGYVPQK--------- 75
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-DVTDLPPKdrdiamvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 ---LYLDTT------LPLTVNRFlrlRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:cd03301 80 nyaLYPHMTvydniaFGLKLRKV---PKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125168 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-179 |
1.48e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.06 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVL-SDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLdttlP 83
Cdd:COG4178 363 LALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYL----P 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 84 L-TvnrfLR---LRPGTQKT----DILPALKRVQAGHLIDAP------MQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:COG4178 439 LgT----LRealLYPATAEAfsdaELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|.
gi 446125168 150 GVDVNGQVALYDLidqLRREL-DCAVLMVSH 179
Cdd:COG4178 515 ALDEENEAALYQL---LREELpGTTVISVGH 542
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-196 |
1.63e-29 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 110.75 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRR----VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNG 65
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 66 QLRIGYVPQ--------KLYLDTTLPLtvnRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
Cdd:cd03258 81 RRRIGMIFQhfnllssrTVFENVALPL---EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-192 |
1.98e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 110.08 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELS---PGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------------RIGYVPQKLYLDTT 81
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 82 LPLTVN-----RFLRLRPGTQKTDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
Cdd:cd03297 90 LNVRENlafglKRKRNREDRISVDEL--LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 446125168 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-214 |
2.25e-29 |
|
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: 110.98 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL------------RIG 70
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtldeenlweirkKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQKlyldttlP------LTV---------NrfLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
Cdd:TIGR04520 81 MVFQN-------PdnqfvgATVeddvafgleN--LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL-HLVMAktDEVLCLNH-HICCSGAPEVVSMHPEF 213
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeEAVLA--DRVIVMNKgKIVAEGTPREIFSQVEL 229
|
.
gi 446125168 214 I 214
Cdd:TIGR04520 230 L 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-202 |
2.36e-29 |
|
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: 109.90 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR--VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------QLRIGYV 72
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLDTTlpLTVNR----FLRLR--PGTQKTDILPALKR-VQAGHLIDAPMQKLSGGeTQRVL-LARALLNRPQLLVL 144
Cdd:cd03263 81 PQFDALFDE--LTVREhlrfYARLKglPKSEIKEEVELLLRvLGLTDKANKRARTLSGG-MKRKLsLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 145 DEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDLHLVmaktdEVLCLNHHICCSG 202
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEA-----EALCDRIAIMSDG 208
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-194 |
2.77e-29 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 109.24 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------------RIGY 71
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtpplnskkaskfrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYL-DTtlpLTVNRFLRL------RPGTQK-TDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
Cdd:TIGR03608 81 LFQNFALiEN---ETVEENLDLglkykkLSKKEKrEKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125168 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLhLVMAKTDEVLCL 194
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-195 |
5.03e-29 |
|
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: 109.24 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR-VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGYV 72
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldsLRraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQklylDTTL-PLTVNRFLRL-RPGTQKTDILPALKrvqAGHLIDAPMQ--------------KLSGGETQRVLLARALL 136
Cdd:cd03253 81 PQ----DTVLfNDTIGYNIRYgRPDATDEEVIEAAK---AAQIHDKIMRfpdgydtivgerglKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLK 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-214 |
5.46e-29 |
|
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: 110.23 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFG-----QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------QL 67
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrditakkkkklkDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 R--IGYVPQ----KLYLDTTL------PltvnRFLRLRPGTQKTDILPALKRVQaghlIDAPMQK-----LSGGETQRVL 130
Cdd:TIGR04521 81 RkkVGLVFQfpehQLFEETVYkdiafgP----KNLGLSEEEAEERVKEALELVG----LDEEYLErspfeLSGGQMRRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSM 209
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDGTPREVFS 232
|
....*
gi 446125168 210 HPEFI 214
Cdd:TIGR04521 233 DVDEL 237
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-250 |
5.66e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 112.13 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 22 DVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------------RIGYVPQKLYLDTTLPLTV 86
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 87 NrflrLRPGTQKTDilPALKRVQ---------AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
Cdd:TIGR02142 95 N----LRYGMKRAR--PSERRISferviellgIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 158 ALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHPEFISM-FGPRGAEQLGIYRHHHNHR 235
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAGPIAEVWASPDLPWLaREDQGSLIEGVVAEHDQHY 248
|
250
....*....|....*
gi 446125168 236 HDLQgrivLRRGNGH 250
Cdd:TIGR02142 249 GLTA----LRLGGGH 259
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-152 |
7.46e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 110.67 E-value: 7.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGQLRIG 70
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQKLYLDTTLPLTVN-----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENllvfgRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
....*..
gi 446125168 146 EPTQGVD 152
Cdd:PRK13537 164 EPTTGLD 170
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-181 |
9.71e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.69 E-value: 9.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVlsDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQK-----LYLDTT 81
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvsmLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 82 L--PLTV--NRFLRLRPG-----TQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL-NRPQLLvLDEPTQGV 151
Cdd:COG3840 82 LfpHLTVaqNIGLGLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRPILL-LDEPFSAL 160
|
170 180 190
....*....|....*....|....*....|
gi 446125168 152 DVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDP 190
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-196 |
1.17e-28 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 107.72 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL--------------R 68
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvnrlrgrqlpllrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQ--KLYLDTTLPLTVNRFLRLRpGTQKTDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
Cdd:TIGR02673 81 IGVVFQdfRLLPDRTVYENVALPLEVR-GKKEREIqrrvGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125168 143 VLDEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-152 |
2.12e-28 |
|
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: 107.63 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRIGYV 72
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQklylDTTL--PLTVNRFLRL------RPGTQKTDILPA-LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
Cdd:cd03218 81 PQ----EASIfrKLTVEENILAvleirgLSKKEREEKLEElLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
....*....
gi 446125168 144 LDEPTQGVD 152
Cdd:cd03218 157 LDEPFAGVD 165
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-216 |
3.26e-28 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 107.62 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSfgqRRvLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIKRNGQLRIGYVPQKL-----YL-- 78
Cdd:COG4138 2 QLNDVAVA---GR-LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELarhraYLsq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 --DTTLPLTVNRFLRL-RPGTQKTDILPAL-----KRVQAGHLIDAPMQKLSGGETQRVLLARALLN-------RPQLLV 143
Cdd:COG4138 77 qqSPPFAMPVFQYLALhQPAGASSEAVEQLlaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 144 LDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVsMHPEFISM 216
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEV-MTPENLSE 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-212 |
3.86e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.79 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYVPQK 75
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlaRRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 LyldtTLP--LTVNRFL------------RLRPGTQKTdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
Cdd:PRK11231 85 H----LTPegITVRELVaygrspwlslwgRLSAEDNAR-VNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL--------HLVMAKTDEVLclnhhicCSGAPEVVsMHPE 212
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLnqasrycdHLVVLANGHVM-------AQGTPEEV-MTPG 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-181 |
5.52e-28 |
|
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: 111.30 E-value: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------QLRIGYVPQ 74
Cdd:TIGR02868 337 LRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KLYLDTTlplTVNRFLRL-RPGTQKTDILPALKRVQAGHLIDA-------PMQ----KLSGGETQRVLLARALLNRPQLL 142
Cdd:TIGR02868 417 DAHLFDT---TVRENLRLaRPDATDEELWAALERVGLADWLRAlpdgldtVLGeggaRLSGGERQRLALARALLADAPIL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125168 143 VLDEPTQGVDVNGQVALY-DLIDQLRREldcAVLMVSHDL 181
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLeDLLAALSGR---TVVLITHHL 530
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-196 |
5.65e-28 |
|
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: 106.54 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGYV 72
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrksLRsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLdttLPLTVNRFLRL-RPGTQKTDILPALKRVQAGHLI-------DAPM----QKLSGGETQRVLLARALLNRPQ 140
Cdd:cd03254 83 LQDTFL---FSGTIMENIRLgRPNATDEEVIEAAKEAGAHDFImklpngyDTVLgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIK-NADKILVLDD 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-183 |
1.14e-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: 105.59 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQRR----VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------- 66
Cdd:COG4181 6 APIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 -LR---IGYVPQKLYLDTTL--------PLTvnrfLRLRPGTQKTdILPALKRVQAGHLIDA-PMQkLSGGETQRVLLAR 133
Cdd:COG4181 86 rLRarhVGFVFQSFQLLPTLtalenvmlPLE----LAGRRDARAR-ARALLERVGLGHRLDHyPAQ-LSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125168 134 ALLNRPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSHDLHL 183
Cdd:COG4181 160 AFATEPAILFADEPTGNLDaATGEQII-DLLFELNRERGTTLVLVTHDPAL 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-196 |
1.25e-27 |
|
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: 104.05 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVsfgqRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRIGY 71
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VP---QKLYLDTTLPLTVNRFLRLRpgtqktdilpalkrvqaghlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPT 148
Cdd:cd03215 80 VPedrKREGLVLDLSVAENIALSSL---------------------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446125168 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYE 179
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-179 |
2.13e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.19 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ--------LRIGYVPQKLYLD 79
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaEACHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 80 TTLPLTVN-RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL-NRPqLLVLDEPTQGVDVNGQV 157
Cdd:PRK13539 86 PALTVAENlEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRP-IWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 446125168 158 ALYDLIdQLRRELDCAVLMVSH 179
Cdd:PRK13539 165 LFAELI-RAHLAQGGIVIAATH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-196 |
7.50e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.55 E-value: 7.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 18 RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGqlrigYVPQKLYldttlpltvNRFLRlRPGT- 96
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPFKRR---------KEFAR-RIGVv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 97 --QKT----DiLPA------LKRV-------------------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
Cdd:COG4586 101 fgQRSqlwwD-LPAidsfrlLKAIyripdaeykkrldelvellDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125168 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-210 |
9.10e-27 |
|
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: 103.53 E-value: 9.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFG-QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ--------------LRIGYV 72
Cdd:TIGR02315 5 ENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklrRRIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLDTTLPL-------------TVNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
Cdd:TIGR02315 85 FQHYNLIERLTVlenvlhgrlgykpTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMH 210
Cdd:TIGR02315 165 DLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAgEIVFDGAPSELDDE 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-195 |
9.77e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.33 E-value: 9.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL----------- 67
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 RIGYV---PQKLYLDTTLPLTVNRFLRLRpGTQKTDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
Cdd:PRK13635 82 QVGMVfqnPDNQFVGATVQDDVAFGLENI-GVPREEMVErvdqALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMN 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-184 |
1.03e-26 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 107.97 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGqrrvlsDVSLELSPGKI-----LTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrNGQLRIGYVPQklYL 78
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQ--YI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 DTTLPLTVNRFLRLRPGT-----QKTDILpalKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
Cdd:PRK13409 410 KPDYDGTVEDLLRSITDDlgssyYKSEII---KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180 190
....*....|....*....|....*....|.
gi 446125168 154 NGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:PRK13409 487 EQRLAVAKAIRRIAEEREATALVVDHDIYMI 517
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-180 |
3.04e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.40 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNGQL---------RIGYVP 73
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRltalpaeqrRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 Q------------KLYLDttLPLTVNRFLRlrpgtqKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
Cdd:COG4136 83 QddllfphlsvgeNLAFA--LPPTIGRAQR------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 142 LVLDEPTQGVDVngqvalyDLIDQLR-------RELDCAVLMVSHD 180
Cdd:COG4136 155 LLLDEPFSKLDA-------ALRAQFRefvfeqiRQRGIPALLVTHD 193
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-181 |
1.85e-25 |
|
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: 99.53 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LR--IGY 71
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkknineLRqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYL--------DTTLPLTVnrfLRLRPGTQKTDI-LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
Cdd:cd03262 81 VFQQFNLfphltvleNITLAPIK---VKGMSKAEAEERaLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446125168 143 VLDEPTQGVD--VNGQValYDLIDQLRRElDCAVLMVSHDL 181
Cdd:cd03262 158 LFDEPTSALDpeLVGEV--LDVMKDLAEE-GMTMVVVTHEM 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-165 |
2.00e-25 |
|
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: 98.97 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----QLRIGYVPQKLYL--- 78
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaEQRDEPHENILYLghl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 ---DTTLPLTVN-RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
Cdd:TIGR01189 82 pglKPELSALENlHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170
....*....|.
gi 446125168 155 GQVALYDLIDQ 165
Cdd:TIGR01189 162 GVALLAGLLRA 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-191 |
3.43e-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: 103.23 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQ----RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD----EGVIKRNGQ------ 66
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQdllgls 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 ---LR------IGYV---PQklyldTTL-PL-TVNRFL--------RLRPGTQKTDILPALKRVQaghlIDAPMQK---- 120
Cdd:COG4172 83 ereLRrirgnrIAMIfqePM-----TSLnPLhTIGKQIaevlrlhrGLSGAAARARALELLERVG----IPDPERRlday 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 121 ---LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV--MAktDEV 191
Cdd:COG4172 154 phqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVrrFA--DRV 227
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-191 |
3.50e-25 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 103.71 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQK----LYLD 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqlefLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 80 TTlPLtvNRFLRLRPGT---QKTDILPALKRvqAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
Cdd:PRK10636 392 ES-PL--QHLARLAPQEleqKLRDYLGGFGF--QGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180 190
....*....|....*....|....*....|....*.
gi 446125168 157 VALYD-LIDqlrreLDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK10636 467 QALTEaLID-----FEGALVVVSHDRHLLRSTTDDL 497
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-197 |
3.83e-25 |
|
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: 99.05 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF-----GQRR--VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--VIKRNGQ----- 66
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsiLVRHDGGwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 ---------LR---IGYVPQklyldttlpltvnrFLRLRPGTQKTDIL--PALK--------RVQAGHLI---------- 114
Cdd:COG4778 81 qaspreilaLRrrtIGYVSQ--------------FLRVIPRVSALDVVaePLLErgvdreeaRARARELLarlnlperlw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 115 DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLC 193
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDaANRAVVV-ELIEEAKAR-GTAIIGIFHDEEVREAVADRVVD 224
|
....
gi 446125168 194 LNHH 197
Cdd:COG4778 225 VTPF 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-184 |
4.08e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 101.31 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQR----RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--- 68
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalsereLRaar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 --IGYVPQKLYLDTT--------LPLTVNrflrlrpGTQKTDI----LPALKRVQAGHLIDA-PMQkLSGGETQRVLLAR 133
Cdd:COG1135 82 rkIGMIFQHFNLLSSrtvaenvaLPLEIA-------GVPKAEIrkrvAELLELVGLSDKADAyPSQ-LSGGQKQRVGIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125168 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVV 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-184 |
4.19e-25 |
|
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: 103.33 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGqrrvlsDVSLELSPGKI-----LTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrNGQLRIGYVPQklYL 78
Cdd:COG1245 341 LVEYPDLTKSYG------GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQ--YI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 DTTLPLTVNRFLRLRPGTQ------KTDILpalKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:COG1245 411 SPDYDGTVEEFLRSANTDDfgssyyKTEII---KPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190
....*....|....*....|....*....|..
gi 446125168 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:COG1245 488 VEQRLAVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
6.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.29 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFG--QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR-- 68
Cdd:PRK13632 5 SVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkEIRkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKlyldttlP------LTV---------NRflRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLAR 133
Cdd:PRK13632 85 IGIIFQN-------PdnqfigATVeddiafgleNK--KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMaKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgKLIAQGKPKEILNNKE 234
|
..
gi 446125168 213 FI 214
Cdd:PRK13632 235 IL 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-192 |
8.26e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.98 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGvikrngQLRIGYVP-QKLYLDTTLPLT 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------ELLAGTAPlAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 86 VNRFLR-----------LRpGTQKTDILPALKRVQ-AGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
Cdd:PRK11247 89 DARLLPwkkvidnvglgLK-GQWRDAALQALAAVGlADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125168 154 NGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-148 |
1.28e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.76 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-------------RIG 70
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdskkdinklrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQKLYLdttLP-LTV--N-----RFLRLRPGTQKTDI-LPALKRVQAGHLIDA-PMQkLSGGETQRVLLARALLNRPQ 140
Cdd:COG1126 81 MVFQQFNL---FPhLTVleNvtlapIKVKKMSKAEAEERaMELLERVGLADKADAyPAQ-LSGGQQQRVAIARALAMEPK 156
|
....*...
gi 446125168 141 LLVLDEPT 148
Cdd:COG1126 157 VMLFDEPT 164
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-207 |
1.54e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 97.66 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSlENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------------KRNG 65
Cdd:PRK10895 1 MATLTA-KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplharARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 66 qlrIGYVPQKLYLDTTLPLTVNRF--LRLR---PGTQKTDILPAL-KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
Cdd:PRK10895 80 ---IGYLPQEASIFRRLSVYDNLMavLQIRddlSAEQREDRANELmEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVV 207
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEI 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-199 |
1.87e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.32 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQ----RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGL-----VAPDEGVIKRNGQL----- 67
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESllhas 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 ----------RIGYVPQK----LYLDTTLPLTVNRFLRLRPGTQK----TDILPALKRV----QAGHLIDAPMQkLSGGE 125
Cdd:PRK15134 83 eqtlrgvrgnKIAMIFQEpmvsLNPLHTLEKQLYEVLSLHRGMRReaarGEILNCLDRVgirqAAKRLTDYPHQ-LSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHIC 199
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
7-215 |
2.10e-24 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 97.70 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVsfGQRrvLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIKRNGQLRIGYVPQKL-----YL--D 79
Cdd:PRK03695 3 LNDVAV--STR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELarhraYLsqQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 80 TTLPLTVNRF----LRLRPGTQKTDILPAL----KRVQAGHLIDAPMQKLSGGETQRVLLARALL-----NRP--QLLVL 144
Cdd:PRK03695 78 QTPPFAMPVFqyltLHQPDKTRTEAVASALnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 145 DEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLNHHIC-CSGAPEVVsMHPEFIS 215
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLlASGRRDEV-LTPENLA 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-179 |
2.16e-24 |
|
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: 95.30 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVL-SDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDttlp 83
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 84 ltvnrflrlrPGTqktdilpaLKRVqaghLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
Cdd:cd03223 77 ----------LGT--------LREQ----LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170
....*....|....*.
gi 446125168 164 dqlrRELDCAVLMVSH 179
Cdd:cd03223 135 ----KELGITVISVGH 146
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-184 |
2.50e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.84 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSF---------GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------- 65
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplakln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 66 ---------------QLRIGYV-PQKlyldttlplTVNRFLRlRPGTQKTDILPALKRVQAGHLIDA-----------PM 118
Cdd:PRK10419 81 raqrkafrrdiqmvfQDSISAVnPRK---------TVREIIR-EPLRHLLSLDKAERLARASEMLRAvdlddsvldkrPP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 119 QkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:PRK10419 151 Q-LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLV 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-207 |
2.61e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.07 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF----------------------GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDE 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 59 GVIKRNGqlRI--------GYVPQklyldttlpLTV--NRFLRLRP-GTQKTDILPALKRVQA----GHLIDAPMQKLSG 123
Cdd:COG1134 81 GRVEVNG--RVsallelgaGFHPE---------LTGreNIYLNGRLlGLSRKEIDEKFDEIVEfaelGDFIDQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSG 202
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKgRLVMDG 228
|
....*
gi 446125168 203 APEVV 207
Cdd:COG1134 229 DPEEV 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-148 |
3.42e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 100.66 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR-VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGYV 72
Cdd:COG5265 358 VRFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdvtqasLRaaIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQklylDTTLpltVNRFLRL-----RPGTQKTDILPALKRVQAGHLIDA-PMQ----------KLSGGETQRVLLARALL 136
Cdd:COG5265 438 PQ----DTVL---FNDTIAYniaygRPDASEEEVEAAARAAQIHDFIESlPDGydtrvgerglKLSGGEKQRVAIARTLL 510
|
170
....*....|..
gi 446125168 137 NRPQLLVLDEPT 148
Cdd:COG5265 511 KNPPILIFDEAT 522
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-214 |
3.86e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.98 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LRIG 70
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpghqiARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQ----KLYLDTTL--PLTVNRFLRLR----PGTQKTdilPA---------------LKRVQAGHLIDAPMQKLSGGE 125
Cdd:PRK11300 82 VVRTfqhvRLFREMTVieNLLVAQHQQLKtglfSGLLKT---PAfrraesealdraatwLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHI-CCSGAP 204
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTpLANGTP 238
|
250
....*....|
gi 446125168 205 EVVSMHPEFI 214
Cdd:PRK11300 239 EEIRNNPDVI 248
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-180 |
6.19e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.47 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLvSLENVSVSFG----QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQlRI------- 69
Cdd:COG4525 1 MSML-TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-PVtgpgadr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 70 GYVPQKlylDTTLP-LTV--N-RF-LRLR--PGTQKTDI-LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
Cdd:COG4525 79 GVVFQK---DALLPwLNVldNvAFgLRLRgvPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-181 |
1.97e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.99 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGQLRigyvpqKLY 77
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLR------DLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 ldtTLPLTVNRFLR--------------LRP--------------------GTQKTDILPALKRVQ--AGHLIDAPMQkL 121
Cdd:PRK11701 77 ---ALSEAERRRLLrtewgfvhqhprdgLRMqvsaggnigerlmavgarhyGDIRATAGDWLERVEidAARIDDLPTT-F 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 122 SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDL 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-166 |
2.01e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 94.69 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDegvikrNGQLRIGyvPQKLYLDTTLPL 84
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPD------SGQLNIA--GHQFDFSQKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 TVNRFLRLRPGT--QKTDILPALKRVQagHLIDAPMQ-------------------------------KLSGGETQRVLL 131
Cdd:COG4161 75 KAIRLLRQKVGMvfQQYNLWPHLTVME--NLIEAPCKvlglskeqarekamkllarlrltdkadrfplHLSGGQQQRVAI 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 446125168 132 ARALLNRPQLLVLDEPTQGVD--VNGQVAlyDLIDQL 166
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDpeITAQVV--EIIREL 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-192 |
2.15e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.20 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 21 SDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LRIG--YVPQK-----LYLDTTL- 82
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKeinalstaqrLARGlvYLPEDrqssgLYLDAPLa 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 ----PLTVNRF-LRLRPGtQKTDILPALKR---VQAGHlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
Cdd:PRK15439 360 wnvcALTHNRRgFWIKPA-RENAVLERYRRalnIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190
....*....|....*....|....*....|....*...
gi 446125168 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK15439 438 ARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVL 474
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-197 |
2.16e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVP-----QKL 76
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 YLDTTLPL---TVNRFLRLrPgTQKTDILPALKRVQAG--------HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
Cdd:PRK10247 85 YCAQTPTLfgdTVYDNLIF-P-WQIRNQQPDPAIFLDDlerfalpdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125168 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLNHH 197
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQPH 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-152 |
2.87e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------------KRNGQLR- 68
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsktpsdKAIRELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 -IGYVPQKLYLDTTLPLTVN------RFLRLRPGTQKTDILPALKRVQAGHLIDA-PMQkLSGGETQRVLLARALLNRPQ 140
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTVQQNlieapcRVLGLSKDQALARAEKLLERLRLKPYADRfPLH-LSGGQQQRVAIARALMMEPQ 161
|
170
....*....|..
gi 446125168 141 LLVLDEPTQGVD 152
Cdd:PRK11124 162 VLLFDEPTAALD 173
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-191 |
4.78e-23 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 92.94 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----QLRIGYVPQKLYL----- 78
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldFQRDSIARGLLYLghapg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 -DTTLPLTVN-RFLRLRPGTQKtdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
Cdd:cd03231 84 iKTTLSVLENlRFWHADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 446125168 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-196 |
6.10e-23 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 93.45 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFG--QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR--IGY 71
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaSLRrqIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLDTTlplTVNRFLRL-RPGTQKTDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRP 139
Cdd:cd03251 81 VSQDVFLFND---TVAENIAYgRPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIE-NADRIVVLED 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-194 |
7.30e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.63 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSV-SFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LRIG 70
Cdd:COG3845 257 VLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVP---QKLYLDTTLPLTVNRFLRL--RPGTQKTDIL--PALKRvQAGHLI----------DAPMQKLSGGETQRVLLAR 133
Cdd:COG3845 337 YIPedrLGRGLVPDMSVAENLILGRyrRPPFSRGGFLdrKAIRA-FAEELIeefdvrtpgpDTPARSLSGGNQQKVILAR 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLhlvmaktDEVLCL 194
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDL-------DEILAL 468
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-152 |
7.68e-23 |
|
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: 91.84 E-value: 7.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 11 SVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAP--DEGVIKRNGQ--------LRIGYVPQKlylDT 80
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrKIIGYVPQD---DI 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125168 81 TLP-LTVNRFLRlrpgtqktdilpalkrvqaghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:cd03213 93 LHPtLTVRETLM----------------------FAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-194 |
1.03e-22 |
|
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: 91.22 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR--VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG--------QLR--IGYV 72
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekALSslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYL-DTTLPLTVNRflrlrpgtqktdilpalkrvqaghlidapmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
Cdd:cd03247 81 NQRPYLfDTTLRNNLGR-------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125168 152 DVNGQVALYDLI-DQLRrelDCAVLMVSHdlHLV-MAKTDEVLCL 194
Cdd:cd03247 130 DPITERQLLSLIfEVLK---DKTLIWITH--HLTgIEHMDKILFL 169
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-195 |
1.24e-22 |
|
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: 93.33 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGQLRIGYVPQKLYLDTtlPL 84
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyqlDRKQRRAFRRDVQLVFQDS--PS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 TVN--------------RFLRLRPGTQKTDILPALKRV--QAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPT 148
Cdd:TIGR02769 100 AVNprmtvrqiigeplrHLTSLDESEQKARIAELLDMVglRSEDADKLPRQ-LSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446125168 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMD 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-179 |
1.43e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.67 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLV-----APDEGVIKRNGQ---------LR 68
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQdifkmdvieLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 -----IGYVPQ-----KLYLDTTLPLTVNRFLRLRPGTQKTdILPALKRVQ----AGHLIDAPMQKLSGGETQRVLLARA 134
Cdd:PRK14247 82 rrvqmVFQIPNpipnlSIFENVALGLKLNRLVKSKKELQER-VRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125168 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSH 179
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-212 |
2.00e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.91 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLY--- 77
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 -----------LDTTLPLTVNRFLRLRPGTQ------KTDILPALKRV---QAGHLIDApmqKLSGGETQRVLLARALLN 137
Cdd:PRK11831 84 krmsmlfqsgaLFTDMNVFDNVAYPLREHTQlpapllHSTVMMKLEAVglrGAAKLMPS---ELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHPE 212
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVaDKKIVAHGSAQALQANPD 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-179 |
2.36e-22 |
|
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: 91.50 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----QL-------RIGY 71
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirQLdpadlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQklylDTTL---PLTVNRFLRLRPGTQKtDILPALKRVQAGHLI-DAPM----------QKLSGGETQRVLLARALLN 137
Cdd:cd03245 83 VPQ----DVTLfygTLRDNITLGAPLADDE-RILRAAELAGVTDFVnKHPNgldlqigergRGLSGGQRQAVALARALLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVAlydLIDQLRREL-DCAVLMVSH 179
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEER---LKERLRQLLgDKTLIIITH 197
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-168 |
2.77e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.41 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGY 71
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtrasLRrnIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKlyldttlPLTVNRF----LRL-RPGTQKTDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARAL 135
Cdd:PRK13657 414 VFQD-------AGLFNRSiednIRVgRPDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrqLSGGERQRLAIARAL 486
|
170 180 190
....*....|....*....|....*....|...
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK 519
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-169 |
3.84e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.19 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLvrvvLGLVApdeGVIK-RNGQL---------------- 67
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIA---GARKiQQGRVevlggdmadarhrrav 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 --RIGYVPQ----KLYLDttlpLTV--N--------------RFLRLRPGTQKTDILPALKRvqaghlidaPMQKLSGGE 125
Cdd:NF033858 75 cpRIAYMPQglgkNLYPT----LSVfeNldffgrlfgqdaaeRRRRIDELLRATGLAPFADR---------PAGKLSGGM 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446125168 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-192 |
3.88e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.87 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF----GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNGQlRIGYVP 73
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGR-EILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QK------------LYLDttlPLT-VNRFLR----------LRPGTQKTD-------ILPALKRVQAGHLIDAPMQKLSG 123
Cdd:PRK09473 88 EKelnklraeqismIFQD---PMTsLNPYMRvgeqlmevlmLHKGMSKAEafeesvrMLDAVKMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 233
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-194 |
5.27e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 91.43 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGQLRI----------- 69
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimRSGAELElyqlseaerrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 70 ------GYVPQK----LYLDTT---------LPLTVNRFLRLRPGTQKTdilpaLKRVQ--AGHLIDAPMQkLSGGETQR 128
Cdd:TIGR02323 83 lmrtewGFVHQNprdgLRMRVSaganigerlMAIGARHYGNIRATAQDW-----LEEVEidPTRIDDLPRA-FSGGMQQR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-194 |
8.34e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.22 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYL---DTTLP---------LTVN 87
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVfqnYSLLPwltvreniaLAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 88 RFLRLRPGTQKTDILPA-LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEhIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180
....*....|....*....|....*...
gi 446125168 167 RRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVML 188
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-196 |
9.57e-22 |
|
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: 89.86 E-value: 9.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGY 71
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiglhdLRsrISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYL-DTTLpltvnRFlRLRPGTQKTD--ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLN 137
Cdd:cd03244 83 IPQDPVLfSGTI-----RS-NLDPFGEYSDeeLWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIdqlRREL-DCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTI---REAFkDCTVLTIAHRLDTII-DSDRILVLDK 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-192 |
1.56e-21 |
|
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: 89.77 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPG-----KILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQlRIGYVPQKLYLDTtlPLTVNRFLR--- 91
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADY--EGTVRDLLSsit 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 92 LRPGTQ---KTDILPALKRVQaghLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
Cdd:cd03237 87 KDFYTHpyfKTEIAKPLQIEQ---ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....
gi 446125168 169 ELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-183 |
1.76e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.49 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR---IGYVPQKLYL----- 78
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaeLRnqkLGFIYQFHHLlpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 ---DTTLPLTVNRflrLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
Cdd:PRK11629 104 aleNVAMPLLIGK---KKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180
....*....|....*....|....*...
gi 446125168 156 QVALYDLIDQLRRELDCAVLMVSHDLHL 183
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-196 |
2.66e-21 |
|
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: 88.62 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR--IGYVPQKLYLDTTLPLT 85
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipyLRrkIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 86 VNRFLRLR-----PGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
Cdd:cd03292 97 ENVAFALEvtgvpPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 446125168 161 DLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03292 177 NLLKKINKA-GTTVVVATHAKELVDTTRHRVIALER 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-215 |
2.75e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.37 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGqLRIGYVPQKLY------- 77
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG-LDVATTPSRELakrlail 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 ---LDTTLPLTVN------RF--LRLRPGTQKTDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
Cdd:COG4604 81 rqeNHINSRLTVRelvafgRFpySKGRLTAEDREIIDeAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVsMHPEFIS 215
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEI-ITPEVLS 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-192 |
2.87e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.37 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------LRIGYVPQKly 77
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgAERGVVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 lDTTLPL-----TVNRFLRLR--PGTQKTDI-LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:PRK11248 79 -EGLLPWrnvqdNVAFGLQLAgvEKMQRLEIaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446125168 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDL-HLVMAKTDEVL 192
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIeEAVFMATELVL 201
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-196 |
2.92e-21 |
|
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: 92.50 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFG-QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR--IGYV 72
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhTLRqfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLDTTLPLTvNRFLRLRPGTQKTDILPALKRVQaghlIDAPMQK---------------LSGGETQRVLLARALLN 137
Cdd:TIGR01193 554 PQEPYIFSGSILE-NLLLGAKENVSQDEIWAACEIAE----IKDDIENmplgyqtelseegssISGGQKQRIALARALLT 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 138 RPQLLVLDEPTQGVDVngqVALYDLIDQLRRELDCAVLMVSHDLHlVMAKTDEVLCLNH 196
Cdd:TIGR01193 629 DSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLDH 683
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-181 |
3.31e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.00 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVR-------------VVLGLVAPDEGVIKRNGQLRIG 70
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQKLYLDTTLPLTVN-RF--LRLRpGTQKTDI----LPALKRV----QAGHLidaPMQkLSGGETQRVLLARALLNRP 139
Cdd:PRK09493 81 MVFQQFYLFPHLTALENvMFgpLRVR-GASKEEAekqaRELLAKVglaeRAHHY---PSE-LSGGQQQRVAIARALAVKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125168 140 QLLVLDEPTQGVDvngqvalydliDQLRREldcaVLMVSHDL 181
Cdd:PRK09493 156 KLMLFDEPTSALD-----------PELRHE----VLKVMQDL 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-183 |
3.46e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.94 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----LRIGYVPQKLYL- 78
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrQRDEYHQDLLYLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 -----DTTLPLTVN-RFL-RLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
Cdd:PRK13538 81 hqpgiKTELTALENlRFYqRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 446125168 152 DVNGqVAlyDLIDQLRRELD---CAVLMVSHDLHL 183
Cdd:PRK13538 161 DKQG-VA--RLEALLAQHAEqggMVILTTHQDLPV 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-180 |
3.78e-21 |
|
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: 91.92 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDTTLPLTVNRFLRLRP 94
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 95 GTQKTDILPALK------------------RVQA------GHLI----------------DAPMQKLSGGETQRVLLARA 134
Cdd:TIGR03719 96 IKDALDRFNEISakyaepdadfdklaaeqaELQEiidaadAWDLdsqleiamdalrcppwDADVTKLSGGERRRVALCRL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 135 LLNRPQLLVLDEPTQGVDVNgQVAlydLIDQLRRELDCAVLMVSHD 180
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAE-SVA---WLERHLQEYPGTVVAVTHD 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-180 |
4.99e-21 |
|
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: 91.54 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKlylDTTLPLTVN 87
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS---RDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 88 RFLRLRPGTQKTDI----LPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
Cdd:TIGR03719 403 VWEEISGGLDIIKLgkreIPSRAYVGRFNFKGSDQQKkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
170 180
....*....|....*....|.
gi 446125168 160 YDLIDQLRrelDCAVLmVSHD 180
Cdd:TIGR03719 483 EEALLNFA---GCAVV-ISHD 499
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-218 |
6.38e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.09 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDE---GVIKRNG-----------Q 66
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGitltaktvwdiR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 LRIGYV---PQKLYLDTTLPLTV-----NRFLRlRPGTQKTdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNR 138
Cdd:PRK13640 84 EKVGIVfqnPDNQFVGATVGDDVafgleNRAVP-RPEMIKI-VRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL-HLVMAktDEVLCLNH-HICCSGAPEVVSMHPEFISM 216
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIdEANMA--DQVLVLDDgKLLAQGSPVEIFSKVEMLKE 239
|
..
gi 446125168 217 FG 218
Cdd:PRK13640 240 IG 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-207 |
7.85e-21 |
|
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: 86.81 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGL--VAPDEGVIKRNGQL----------RIGyvp 73
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlppeeraRLG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 qkLYLDTTLP-----LTVNRFLRlrpgtqktdilpalkRVQAGhlidapmqkLSGGETQRVLLARALLNRPQLLVLDEPT 148
Cdd:cd03217 79 --IFLAFQYPpeipgVKNADFLR---------------YVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHD---LHLVMAKTDEVLClNHHICCSGAPEVV 207
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREE-GKSVLIITHYqrlLDYIKPDRVHVLY-DGRIVKSGDKELA 192
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-196 |
8.15e-21 |
|
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: 87.20 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF----------------------GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK 62
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 63 RNGQLR------IGYVPQklyldttlpLTV--NRFLRLR-PGTQKTDILPALKRVQA----GHLIDAPMQKLSGGETQRV 129
Cdd:cd03220 81 VRGRVSsllglgGGFNPE---------LTGreNIYLNGRlLGLSRKEIDEKIDEIIEfselGDFIDLPVKTYSSGMKARL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEK 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-179 |
9.57e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 87.33 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSF----GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDE---GVIKRNG--------QL 67
Cdd:cd03234 2 RVLPWWDVGLKAknwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGqprkpdqfQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 RIGYVPQklyLDTTLP-LTVNRFL---------RLRPGTQKTDILP--ALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
Cdd:cd03234 82 CVAYVRQ---DDILLPgLTVRETLtytailrlpRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 136 LNRPQLLVLDEPTQGVDvngQVALYDLIDQLRR--ELDCAVLMVSH 179
Cdd:cd03234 159 LWDPKVLILDEPTSGLD---SFTALNLVSTLSQlaRRNRIVILTIH 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-220 |
9.68e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 9.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYVPQKL 76
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 YL--DTTLPLTVNR--------FLRLRPGTQKTdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:PRK10253 91 TTpgDITVQELVARgryphqplFTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAP-EVVSmhPEFIS-MFGPR 220
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREgKIVAQGAPkEIVT--AELIErIYGLR 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-182 |
1.03e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.83 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFG-----QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LR 68
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeykraKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYLDTTLPLTV----------NRFLRLRPGTQKTDI---LPALKRVQAG--HLIDAPMQKLSGGETQRVLLAR 133
Cdd:COG1101 82 IGRVFQDPMMGTAPSMTIeenlalayrrGKRRGLRRGLTKKRRelfRELLATLGLGleNRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125168 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLH 182
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-196 |
1.22e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.32 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSlVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLR---------IGY 71
Cdd:PRK11000 1 MAS-VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndvppaergVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLDTTLPLTVNRFLRLR-PGTQKTDILpalKRV-------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKlAGAKKEEIN---QRVnqvaevlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125168 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-205 |
1.27e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----LR---IGY 71
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqaLQknlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLDTTLPLTVNR-----------FLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDvvmmgryghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAPE 205
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-179 |
1.47e-20 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 90.07 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLG-----------LVAPDEGV------IKRN 64
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGSgetiwdIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 65 gqlrIGYVPQKLYLDTTLPLTV-NRFL---------------RLRPGTQK-TDILPALKRvqaghLIDAPMQKLSGGETQ 127
Cdd:PRK10938 338 ----IGYVSSSLHLDYRVSTSVrNVILsgffdsigiyqavsdRQQKLAQQwLDILGIDKR-----TADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125168 128 RVLLARALLNRPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSH 179
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDpLNRQLVR-RFVDVLISEGETQLLFVSH 460
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-217 |
1.70e-20 |
|
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: 87.31 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 13 SFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR---IGYVPQKLY 77
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelreLRrkkISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 L--------DTTLPLT---VNRFLRLRPGTQktdilpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:cd03294 113 LlphrtvleNVAFGLEvqgVPRAEREERAAE------ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHICC--------SGAPEVVSMHP--EFISM 216
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFITHDL-------DEALRLGDRIAImkdgrlvqVGTPEEILTNPanDYVRE 259
|
.
gi 446125168 217 F 217
Cdd:cd03294 260 F 260
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-180 |
2.11e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.62 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYV--------PQKLYL 78
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFdqhraeldPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 DTtlpltvnrflrLRPGTQKTDIlPALKRVQAGHLID---------APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:PRK11147 402 DN-----------LAEGKQEVMV-NGRPRHVLGYLQDflfhpkramTPVKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|.
gi 446125168 150 GVDVNGQVALYDLIDqlrrELDCAVLMVSHD 180
Cdd:PRK11147 470 DLDVETLELLEELLD----SYQGTVLLVSHD 496
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-180 |
2.20e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 89.57 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDTTLPL 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 TVNRFLRL--RPGTQKTDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
Cdd:PRK15064 400 TLFDWMSQwrQEGDDEQAVRGTLGRLLfSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNM 479
|
170
....*....|....*....
gi 446125168 162 LIDQLRRELdcavLMVSHD 180
Cdd:PRK15064 480 ALEKYEGTL----IFVSHD 494
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-191 |
3.61e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.93 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRR----VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR----- 68
Cdd:PRK11153 4 LKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekeLRkarrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYL--------DTTLPLTVNrflrlrpGTQKTDI----LPALKRVQAGHLIDA-PMQkLSGGETQRVLLARAL 135
Cdd:PRK11153 84 IGMIFQHFNLlssrtvfdNVALPLELA-------GTPKAEIkarvTELLELVGLSDKADRyPAQ-LSGGQKQRVAIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRV 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-205 |
4.16e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV----------IKRNGQL--- 67
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshiellgrtVQREGRLard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 ------RIGYVPQKLYLDTTLPLTVNRF-------------LRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQR 128
Cdd:PRK09984 81 irksraNTGYIFQQFNLVNRLSVLENVLigalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQgHVFYDGSSQ 238
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-194 |
4.78e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 85.60 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQR---RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----QLRIGYVPQKL 76
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 YLDTTLPLTVNRFLRLR-----PGTQKTDILPALKRVQAGHLIdAPMQK------------LSGGETQRVLLARALLNRP 139
Cdd:cd03248 91 SLVGQEPVLFARSLQDNiayglQSCSFECVKEAAQKAHAHSFI-SELASgydtevgekgsqLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCL 194
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTV-ERADQILVL 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-184 |
5.25e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 87.09 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQR-----------RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------ 66
Cdd:COG4608 7 LLEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQditgls 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 --------LRIGYVPQKLY--LDTTL--------PLTVNRflrLRPGTQKTD-ILPALKRV--QAGHLIDAPMQkLSGGE 125
Cdd:COG4608 87 grelrplrRRMQMVFQDPYasLNPRMtvgdiiaePLRIHG---LASKAERRErVAELLELVglRPEHADRYPHE-FSGGQ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVV 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-192 |
5.62e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 17 RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGlVAPD--EGVIKRNGQ------------LRIGYVPQKLYLDTTL 82
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGrwEGEIFIDGKpvkirnpqqaiaQGIAMVPEDRKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 PLTvnrflrlrpGTQKTDILPALKRVQAGHLIDA--------------------PMQK---LSGGETQRVLLARALLNRP 139
Cdd:PRK13549 354 PVM---------GVGKNITLAALDRFTGGSRIDDaaelktilesiqrlkvktasPELAiarLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVL 476
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
6.33e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------QLR 68
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYLDTTLPLTVNRFL-RL-------------RPGTQKTDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARA 134
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIgRHltkkvcgvniidwREMRVRAAMM--LLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 135 LLNRPQLLVLDEPTQGVdVNGQV-ALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHpE 212
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL-TNKEVdYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMkDGSSVCSGMVSDVSND-D 236
|
....
gi 446125168 213 FISM 216
Cdd:PRK09700 237 IVRL 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-196 |
6.85e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQR---RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----QLRIGYVP 73
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvQYDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 QKLYLDTTLPLTVNRFLRLRPG-----TQKTDILPALKRVQAGHLI-----------DAPMQKLSGGETQRVLLARALLN 137
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAygltdTPDEEIMAAAKAANAHDFImefpngydtevGEKGSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYdlidQLRRELDCAVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQ----ESRSRASRTVLLIAHRLSTV-ERADQILVLKK 688
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-196 |
8.25e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.82 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRR-----------VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIKRNGQlRIgyv 72
Cdd:COG4172 275 LLEARDLKVWFPIKRglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQ-DL--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 pqklyldTTLPLTVNRFLR------------------------------LRPGTQKTD----ILPALKRVqagHLIDAPM 118
Cdd:COG4172 350 -------DGLSRRALRPLRrrmqvvfqdpfgslsprmtvgqiiaeglrvHGPGLSAAErrarVAEALEEV---GLDPAAR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 119 QK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:COG4172 420 HRypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM 499
|
..
gi 446125168 195 NH 196
Cdd:COG4172 500 KD 501
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-195 |
1.04e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.55 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQ---RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------- 67
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 -RIGYV---PQKLYLDTTLPLTV-----NRFLRLRpgTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNR 138
Cdd:PRK13650 81 hKIGMVfqnPDNQFVGATVEDDVafgleNKGIPHE--EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMK 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-214 |
1.07e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQlRIGYVP------- 73
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-DLSHVPpyqrpin 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 ---QKLYLdttLP-LTVNRFL-------RLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
Cdd:PRK11607 95 mmfQSYAL---FPhMTVEQNIafglkqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 143 VLDEPTQGVD--VNGQVALyDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP------EF 213
Cdd:PRK11607 172 LLDEPMGALDkkLRDRMQL-EVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIYEHPttrysaEF 249
|
.
gi 446125168 214 I 214
Cdd:PRK11607 250 I 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-195 |
1.21e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LR--IGYVPQ---------KLY 77
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmkLResVGMVFQdpdnqlfsaSVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 LDTTLPlTVNrfLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
Cdd:PRK13636 102 QDVSFG-AVN--LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 446125168 158 ALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-192 |
1.49e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.91 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 22 DVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ--LRIGYVP--------QKLYLDttlPLTvnrflR 91
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdlLGMKDDEwravrsdiQMIFQD---PLA-----S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 92 LRPGTQKTDIL--------PALKRVQAGHLIDAPMQKL--------------SGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:PRK15079 111 LNPRMTIGEIIaeplrtyhPKLSRQEVKDRVKAMMLKVgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125168 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-191 |
2.25e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLR------------ 68
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYLdttLP-LTV----------NRFLRLRPGTQKTDILPALKRVqaGHLID--APMQKLSGGETQRVLLARAL 135
Cdd:PRK11288 81 VAIIYQELHL---VPeMTVaenlylgqlpHKGGIVNRRLLNYEAREQLEHL--GVDIDpdTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAI 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-198 |
3.36e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------QLR 68
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarltpakahQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYLDTTLPLTVNRFLRLrPGTQKTdilpaLKRVQA------GHL-IDAPMQKLSGGETQRVLLARALLNRPQL 141
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGL-PKRQAS-----MQKMKQllaalgCQLdLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHlvmaktdEVLCLNHHI 198
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLP-------EIRQLADRI 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-182 |
4.24e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.55 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVV---LGLVaPD---EGVIKRNGQ-------- 66
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLI-PGarvEGEILLDGEdiydpdvd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 ---LR--IGYVPQKLyldTTLPLTVnrF------LRLRpGTQKTDILP-----ALKRVqagHL-------IDAPMQKLSG 123
Cdd:COG1117 87 vveLRrrVGMVFQKP---NPFPKSI--YdnvaygLRLH-GIKSKSELDeiveeSLRKA---ALwdevkdrLKKSALGLSG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLH 182
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNMQ 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-169 |
5.70e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LR-- 68
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakiMRea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQ--KLYLDTTLP--LTVNRFLRLRPGTQKT-----DILPAL--KRVQ-AGhlidapmqKLSGGETQRVLLARALL 136
Cdd:PRK11614 82 VAIVPEgrRVFSRMTVEenLAMGGFFAERDQFQERikwvyELFPRLheRRIQrAG--------TMSGGEQQMLAIGRALM 153
|
170 180 190
....*....|....*....|....*....|...
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ 186
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-195 |
7.05e-19 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 85.30 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 33 LTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKlYLDTtLPLTVNRFL---RLRPGTQKTDILPALKRVQ 109
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQH-HVDG-LDLSSNPLLymmRCFPGVPEQKLRAHLGSFG 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 110 -AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqvALYDLIDQLRReLDCAVLMVSHDLHLVMAKT 188
Cdd:PLN03073 616 vTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQGLVL-FQGGVLMVSHDEHLISGSV 691
|
....*..
gi 446125168 189 DEVLCLN 195
Cdd:PLN03073 692 DELWVVS 698
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-181 |
8.20e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLR------------ 68
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYLDTTLPLTVNRFLRLRPGT-----------QKTDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVNrfgridwkkmyAEADKL--LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRL 201
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-195 |
8.24e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 8.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR-- 68
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpfLRrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQ--------KLYLDTTLPLTVnrflrlrPGTQKTDILpalKRVQAG----HLIDA----PMQkLSGGETQRVLLA 132
Cdd:PRK10908 81 IGMIFQdhhllmdrTVYDNVAIPLII-------AGASGDDIR---RRVSAAldkvGLLDKaknfPIQ-LSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125168 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLS 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-195 |
9.35e-19 |
|
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: 81.69 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQR--RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGY 71
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistipledLRssLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQK-LYLDTTLPLTVNRFLRLrpgtQKTDILPALkRVQAGHLidapmqKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
Cdd:cd03369 87 IPQDpTLFSGTIRSNLDPFDEY----SDEEIYGAL-RVSEGGL------NLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 151 VDVNGQVALYDLIdqlRREL-DCAVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:cd03369 156 IDYATDALIQKTI---REEFtNSTILTIAHRLRTI-IDYDKILVMD 197
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-192 |
9.79e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 82.58 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF---------GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----- 66
Cdd:COG4167 1 MSALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 -----------------------LRIGYVpqklyLDTTLPLTVNrflrLRPGTQKTDILPALKRVqaGHLIDA---PMQK 120
Cdd:COG4167 81 dykyrckhirmifqdpntslnprLNIGQI-----LEEPLRLNTD----LTAEEREERIFATLRLV--GLLPEHanfYPHM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVL 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-192 |
1.13e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.48 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRV--LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR--IGYVPQKLY- 77
Cdd:PRK11308 24 PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllkadpeaqklLRqkIQIVFQNPYg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 -------LDTTL--PLTVNrflrlrpgtqkTDILPALKRVQAGHLidapMQKL--------------SGGETQRVLLARA 134
Cdd:PRK11308 104 slnprkkVGQILeePLLIN-----------TSLSAAERREKALAM----MAKVglrpehydryphmfSGGQRQRIAIARA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-214 |
1.43e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.43 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQlRIGY-------VPQKLYL------DTTLPLT 85
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-PIKYdkkslleVRKTVGIvfqnpdDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 86 VNR---FLRLRPGTQKTDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
Cdd:PRK13639 96 VEEdvaFGPLNLGLSKEEVekrvKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 159 LYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFI 214
Cdd:PRK13639 176 IMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDgKIIKEGTPKEVFSDIETI 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-179 |
1.74e-18 |
|
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: 81.00 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVlsDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQK--------- 75
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvsmlfqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 ------LYLDTTLPLTVNRFLRLRPGTQKTdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:cd03298 79 nnlfahLTVEQNVGLGLSPGLKLTAEDRQA-IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190
....*....|....*....|....*....|
gi 446125168 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTH 187
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-189 |
1.80e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVvLGLVAPDEGVIKRNGqlRIGYVPQKLY------- 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEG--RVEFFNQNIYerrvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 -----------LDTTLPLTVN-------RFLRLRPGTQKTDIL-PALKRV----QAGHLIDAPMQKLSGGETQRVLLARA 134
Cdd:PRK14258 85 rlrrqvsmvhpKPNLFPMSVYdnvaygvKIVGWRPKLEIDDIVeSALKDAdlwdEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTD 189
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-181 |
1.85e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.09 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 27 LSPGKILTLLGPNGAGKSTLVRVVLGLVAPD----------EGVIKR--------------NGQLRIGYVPQklYLDTtL 82
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswDEVLKRfrgtelqnyfkklyNGEIKVVHKPQ--YVDL-I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 PL----TVNRFLRlrpGTQKTDILPAL-KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
Cdd:PRK13409 173 PKvfkgKVRELLK---KVDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRL 249
|
170 180
....*....|....*....|....*.
gi 446125168 158 ALYDLIdqlrREL--DCAVLMVSHDL 181
Cdd:PRK13409 250 NVARLI----RELaeGKYVLVVEHDL 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-192 |
1.97e-18 |
|
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: 83.72 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 16 QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGlVAPD--EGVIKRNGQ------------LRIGYVPQKLYLDTT 81
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKpvdirnpaqairAGIAMVPEDRKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 82 LPL----------TVNRF---LRLRPGTQKTDILPALKR--VQAGHlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:TIGR02633 351 VPIlgvgknitlsVLKSFcfkMRIDAAAELQIIGSAIQRlkVKTAS-PFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 147 PTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVL 474
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-192 |
2.15e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQK------LYLDT-------TLPLTV 86
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangiVYISEdrkrdglVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 87 --NRFL-RLRPGTQKTDILPALKRVQA-GHLI----------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:PRK10762 348 keNMSLtALRYFSRAGGSLKHADEQQAvSDFIrlfniktpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125168 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK10762 428 VGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-191 |
2.45e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQR--RVLSDVSLELSPGKILTLLGPNGAGKSTLvrvvLGLVA----PDEGVIKRNGQ---------LR 68
Cdd:PRK11160 338 SLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTrawdPQQGEILLNGQpiadyseaaLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 --IGYVPQKLYLDTTlplTVNRFLRLrPGTQKTD--ILPALKRVQAGHLIDAPM----------QKLSGGETQRVLLARA 134
Cdd:PRK11160 414 qaISVVSQRVHLFSA---TLRDNLLL-AAPNASDeaLIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEV 191
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTG-LEQFDRI 543
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-217 |
7.36e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.16 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGL--VAPDEGVI--------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 62 -----------------------KRNGQLRIGYVPQK---LYLDTTLPLTVNRFLRL--RPGTQKTD-ILPALKRVQAGH 112
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRtfaLYGDDTVLDNVLEALEEigYEGKEAVGrAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 113 LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|....*..
gi 446125168 193 CL-NHHICCSGAP-EVVSMHPEFISMF 217
Cdd:TIGR03269 241 WLeNGEIKEEGTPdEVVAVFMEGVSEV 267
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-198 |
8.45e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.07 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 22 DVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------------RIGYVPQklylDTTL-P-L 84
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrRIGYVFQ----DARLfPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 TV--NrflrLRPGTQKTDILPALKRVQ---AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
Cdd:PRK11144 92 KVrgN----LRYGMAKSMVAQFDKIVAllgIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125168 160 YDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHI 198
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSL-------DEILRLADRV 199
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-218 |
1.01e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.05 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LR--IGYV---PQKLYLDTTL 82
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllaLRqqVATVfqdPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 PLTVNRFLRlRPGTQKTDIL----PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
Cdd:PRK13638 96 DSDIAFSLR-NLGVPEAEITrrvdEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 159 LYDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFISMFG 218
Cdd:PRK13638 175 MIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQgQILTHGAPGEVFACTEAMEQAG 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
1.10e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.06 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 16 QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGQLR-----IGYVPQ----KL 76
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagKKNKKLKplrkkVGIVFQfpehQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 YLDTtlpltVNRFLRLRP---GTQKTDIL----PALKRVQAGH--LIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEP 147
Cdd:PRK13634 99 FEET-----VEKDICFGPmnfGVSEEDAKqkarEMIELVGLPEelLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHPEFISMFG 218
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMhKGTVFLQGTPREIFADPDELEAIG 244
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-196 |
1.29e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 81.69 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFG--QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR-- 68
Cdd:TIGR02203 328 RGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlaSLRrq 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYL-DTTLPLTVnRFLRLRpGTQKTDILPALKRVQAGHLIDA-PM----------QKLSGGETQRVLLARALL 136
Cdd:TIGR02203 408 VALVSQDVVLfNDTIANNI-AYGRTE-QADRAEIERALAAAYAQDFVDKlPLgldtpigengVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTI-EKADRIVVMDD 542
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-196 |
1.45e-17 |
|
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: 78.74 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQR---RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IG 70
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwLRsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQKLYLDTTlplTVNRFLRL-RPGTQKTDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNR 138
Cdd:cd03249 81 LVSQEPVLFDG---TIAENIRYgKPDATDEEVEEAAKKANIHDFIMSLPDGydtlvgergsqLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCavLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTIR-NADLIAVLQN 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-215 |
1.61e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.46 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGQLR----------IGYVPQKLYlDTTLP 83
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsVLIRGEPITkenirevrkfVGLVFQNPD-DQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 84 LTVNRFLRLRP-------GTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
Cdd:PRK13652 94 PTVEQDIAFGPinlgldeETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFIS 215
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIFLQPDLLA 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-195 |
2.33e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.02 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------RIGYV---PQKLYLDTTLPLT 85
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnfeklrkHIGIVfqnPDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 86 VNRFLR--LRPGTQKTDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDL 162
Cdd:PRK13648 105 VAFGLEnhAVPYDEMHRRVSeALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190
....*....|....*....|....*....|...
gi 446125168 163 IDQLRRELDCAVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEAM-EADHVIVMN 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-180 |
2.35e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.93 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRVLSDVSLELSPG-KIlTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDTTlpLTV------- 86
Cdd:PRK11819 18 PKKQILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPE--KTVrenveeg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 87 --------NRFLRL-----RPGTQKTDILPALKRVQA------GHLI----------------DAPMQKLSGGETQRVLL 131
Cdd:PRK11819 95 vaevkaalDRFNEIyaayaEPDADFDALAAEQGELQEiidaadAWDLdsqleiamdalrcppwDAKVTKLSGGERRRVAL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125168 132 ARALLNRPQLLVLDEPTQGVDVNgQVAlydLIDQLRRELDCAVLMVSHD 180
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAE-SVA---WLEQFLHDYPGTVVAVTHD 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-179 |
3.40e-17 |
|
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: 80.56 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSFGQRRVL-SDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKLYLDT- 80
Cdd:TIGR00954 450 NGIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 81 TL------PLTVNRFLRlrPGTQKTDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLLVLD 145
Cdd:TIGR00954 530 TLrdqiiyPDSSEDMKR--RGLSDKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 446125168 146 EPTQGVDVNGQVALYdlidQLRRELDCAVLMVSH 179
Cdd:TIGR00954 608 ECTSAVSVDVEGYMY----RLCREFGITLFSVSH 637
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-215 |
3.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQR-----RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--------------IKRNGQL 67
Cdd:PRK13645 9 LDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanlkkIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 R--IGYVPQ----KLYLDTtlpltVNRFLRLRPGTQKTDILPALKRV-QAGHLIDAPMQ-------KLSGGETQRVLLAR 133
Cdd:PRK13645 89 RkeIGLVFQfpeyQLFQET-----IEKDIAFGPVNLGENKQEAYKKVpELLKLVQLPEDyvkrspfELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEgKVISIGSPFEIFSNQE 243
|
...
gi 446125168 213 FIS 215
Cdd:PRK13645 244 LLT 246
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-181 |
3.60e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.70 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 24 SLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQK-----LYLDTTL--PLTV--NRFLRLRP 94
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvsmLFQENNLfsHLTVaqNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 95 G-----TQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
Cdd:PRK10771 99 GlklnaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170
....*....|..
gi 446125168 170 LDCAVLMVSHDL 181
Cdd:PRK10771 179 RQLTLLMVSHSL 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-181 |
4.97e-17 |
|
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: 79.83 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 29 PGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKR--------------NGQLRIGYVPQklYLDTtLPL 84
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGdydeepswdeVLKRfrgtelqdyfkklaNGEIKVAHKPQ--YVDL-IPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 ----TVNRFLRlrpgtqKTD----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
Cdd:COG1245 175 vfkgTVRELLE------KVDergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180
....*....|....*....|....*
gi 446125168 157 VALYDLIDQLRRElDCAVLMVSHDL 181
Cdd:COG1245 249 LNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-194 |
5.42e-17 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 77.79 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 29 PGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIK--------------RNGQLRIGYVPQklYLDTtLPL 84
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeILDefrgselqnyftklLEGDVKVIVKPQ--YVDL-IPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 TVN-RFLRLRPGTQKTDILPAL-KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDL 162
Cdd:cd03236 102 AVKgKVGELLKKKDERGKLDELvDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181
|
170 180 190
....*....|....*....|....*....|..
gi 446125168 163 IDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:cd03236 182 IRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-180 |
6.16e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.39 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQklyldttlpltvN 87
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQ------------S 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 88 RfLRLRPgtQKT---------DILPALKR-------VQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEP 147
Cdd:PRK11819 396 R-DALDP--NKTvweeisgglDIIKVGNReipsrayVGRFNFKGGDQQKkvgvLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
170 180 190
....*....|....*....|....*....|....*.
gi 446125168 148 TQGVDVNGQVALYDLIdqlrreLD---CAVLmVSHD 180
Cdd:PRK11819 473 TNDLDVETLRALEEAL------LEfpgCAVV-ISHD 501
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-183 |
8.81e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.74 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 16 QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR---IGYVPQKLYLDT 80
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeearakLRakhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 81 TLPLTVN----RFLRLRPGTQ-KTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
Cdd:PRK10584 102 TLNALENvelpALLRGESSRQsRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*...
gi 446125168 156 QVALYDLIDQLRRELDCAVLMVSHDLHL 183
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-187 |
9.12e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.12 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 23 VSLELSPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRNGQ-LR----------IGYVPQklylDTTLPL-TVNRFL 90
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIeLReldpeswrkhLSWVGQ----NPQLPHgTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 91 RL-RPGTQKTDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
Cdd:PRK11174 444 LLgNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190
....*....|....*....|....*....|....*..
gi 446125168 159 LYDLIDQLRRELDCavLMVSH---DLH-----LVMAK 187
Cdd:PRK11174 524 VMQALNAASRRQTT--LMVTHqleDLAqwdqiWVMQD 558
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-196 |
9.22e-17 |
|
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: 76.76 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFG--QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGY 71
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawLRrqVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQklylDTTLpltVNRFLR-----LRPGTQKTDILPALKRVQAGHLI-DAPM----------QKLSGGETQRVLLARAL 135
Cdd:cd03252 81 VLQ----ENVL---FNRSIRdnialADPGMSMERVIEAAKLAGAHDFIsELPEgydtivgeqgAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVAlydLIDQLRRELDC-AVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHA---IMRNMHDICAGrTVIIIAHRLSTVK-NADRIIVMEK 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-207 |
1.29e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.01 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 16 QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------------QLRIGYVPQ----KLYL 78
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdiRKKVGLVFQypeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 DTtlpltVNRFLRLRP---GTQKTDILPALKRVQAGHLIDAPMQK------LSGGETQRVLLARALLNRPQLLVLDEPTQ 149
Cdd:PRK13637 99 ET-----IEKDIAFGPinlGLSEEEIENRVKRAMNIVGLDYEDYKdkspfeLSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHIC-CSGAPEVV 207
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCeLQGTPREV 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-180 |
1.35e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.61 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSF----GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------- 66
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 --LR---IGYVPQKLYLDTTLPLTVN-RFLRLRPGTQKTDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
Cdd:PRK10535 81 aqLRrehFGFIFQRYHLLSHLTAAQNvEVPAVYAGLERKQRLLRaqelLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHD 180
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-181 |
1.51e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.35 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTS-LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVV--LGLVAPD---EGVIKRNG--------- 65
Cdd:PRK14239 1 MTEpILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGhniysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 66 --QLR--IGYVPQKlylDTTLPLTV--NRFLRLRpgtqktdilpaLKRVQAGHLIDAPMQK------------------- 120
Cdd:PRK14239 81 tvDLRkeIGMVFQQ---PNPFPMSIyeNVVYGLR-----------LKGIKDKQVLDEAVEKslkgasiwdevkdrlhdsa 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 121 --LSGGETQRVLLARALLNRPQLLVLDEPTQGVD--VNGQV--ALYDLIDqlrrelDCAVLMVSHDL 181
Cdd:PRK14239 147 lgLSGGQQQRVCIARVLATSPKIILLDEPTSALDpiSAGKIeeTLLGLKD------DYTMLLVTRSM 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-207 |
1.86e-16 |
|
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: 78.31 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG------------VIKRNGQLR---- 68
Cdd:TIGR03269 285 VSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvdMTKPGPDGRgrak 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 --IGYVPQK--LYLDTTL--PLTVNRFLRLRPGTQKTDILPALKRV-----QAGHLIDAPMQKLSGGETQRVLLARALLN 137
Cdd:TIGR03269 365 ryIGILHQEydLYPHRTVldNLTEAIGLELPDELARMKAVITLKMVgfdeeKAEEILDKYPDELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV-LCLNHHICCSGAPEVV 207
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAaLMRDGKIVKIGDPEEI 515
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-152 |
2.17e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.94 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkRNGQLRIgyvpqklylDTTL 82
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI-RVGDITI---------DTAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 PLTVN----RFLRLRPG--TQKTDILP---ALKRVQAGHLI--------------------------DAPMQKLSGGETQ 127
Cdd:PRK11264 72 SLSQQkgliRQLRQHVGfvFQNFNLFPhrtVLENIIEGPVIvkgepkeeatararellakvglagkeTSYPRRLSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 446125168 128 RVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALD 176
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-194 |
2.20e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.24 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 17 RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------------RIGYVPQK---- 75
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqidaiklrkEVGMVFQQpnpf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 ----LYLDTTLPLTVNRFLRLRpgTQKTDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
Cdd:PRK14246 103 phlsIYDNIAYPLKSHGIKEKR--EIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446125168 148 TQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFL 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-194 |
2.38e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------RIGYVPQ 74
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 KLylDTTLPLTVNRFLRL----------------RPGTQKTDILPALKRVqAGHLIDApmqkLSGGETQRVLLARALLNR 138
Cdd:PRK10575 93 QL--PAAEGMTVRELVAIgrypwhgalgrfgaadREKVEEAISLVGLKPL-AHRLVDS----LSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVAL 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-191 |
2.49e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGlVAPD---EGVIKRNGQ-LR-------- 68
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEeLQasnirdte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 ---IGYVPQKLYLDTTLPLTVNRFL--RLRPG--------TQKTDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
Cdd:PRK13549 81 ragIAIIHQELALVKELSVLENIFLgnEITPGgimdydamYLRAQKL--LAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTI 213
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-190 |
2.51e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.99 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 9 NVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------QLRIGYVPQKLYL 78
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlctyQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 DTTLPLTVNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvngQVA 158
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELS 162
|
170 180 190
....*....|....*....|....*....|....*
gi 446125168 159 LYDLIDQLR--RELDCAVLMVSH-DLHLVMAKTDE 190
Cdd:PRK13540 163 LLTIITKIQehRAKGGAVLLTSHqDLPLNKADYEE 197
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-215 |
2.98e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.02 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 17 RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLG----LVAPD----EGVIKRNGQ-LRIGYVPQKLYLDTTLP---- 83
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEpLAAIDAPRLARLRAVLPqaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 84 ----------LTVNRFLRLRPGTQKT----DIL-PALKRVQAGHLIDAPMQKLSGGETQRVLLARAL---------LNRP 139
Cdd:PRK13547 94 pafafsareiVLLGRYPHARRAGALThrdgEIAwQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVsMHPEFIS 215
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLaDGAIVAHGAPADV-LTPAHIA 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-195 |
3.94e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.97 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 16 QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------------QLRIGYVPQ----KL 76
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVFQfpesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 YLDTtlpltVNRFLRLRPGTQKTDILPALKR-----VQAGHLID----APMQkLSGGETQRVLLARALLNRPQLLVLDEP 147
Cdd:PRK13646 99 FEDT-----VEREIIFGPKNFKMNLDEVKNYahrllMDLGFSRDvmsqSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446125168 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMK 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-196 |
4.27e-16 |
|
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: 74.04 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR-----VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGqlRIGYVPQKLYLd 79
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 80 ttLPLTV---------------NRFLR---LRPgtqKTDILPALKRVQAGhlidapmQK---LSGGETQRVLLARALLNR 138
Cdd:cd03250 78 --QNGTIrenilfgkpfdeeryEKVIKacaLEP---DLEILPDGDLTEIG-------EKginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYD-LIDQLRRELDCAVLmVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRIL-VTHQLQLLP-HADQIVVLDN 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-194 |
4.74e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.51 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQR---RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL---------- 67
Cdd:PRK13642 1 MNKILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 -RIGYV---PQKLYLDTTLPLTVnRFLRLRPGTQKTDILpalKRVQ----AGHLIDAPMQ---KLSGGETQRVLLARALL 136
Cdd:PRK13642 81 rKIGMVfqnPDNQFVGATVEDDV-AFGMENQGIPREEMI---KRVDeallAVNMLDFKTRepaRLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL 194
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVM 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-179 |
5.26e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 6 SLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVA--PDEGVIKRNGQ------------LRIGY 71
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEdilelspderarAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQklYldttlP-----LTVNRFLRLRPGTQKTDILPA----------LKRVQaghlIDAPMQK------LSGGETQRVL 130
Cdd:COG0396 82 AFQ--Y-----PveipgVSVSNFLRTALNARRGEELSAreflkllkekMKELG----LDEDFLDryvnegFSGGEKKRNE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125168 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH 198
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-214 |
6.45e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.25 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFG-----QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------------Q 66
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 LR--IGYVPQ----KLYLDTTLPLTVNRFLRLRPGTQKTDIlPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALL 136
Cdd:PRK13641 83 LRkkVSLVFQfpeaQLFENTVLKDVEFGPKNFGFSEDEAKE-KALKWLKKVGLSEDLISKspfeLSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFI 214
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHgKLIKHASPKEIFSDKEWL 239
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-152 |
7.45e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 7.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 9 NVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLV--APDEGVIKrngqlrigyVPQ-KLYLDTTLplt 85
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVD---------VPDnQFGREASL--- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 86 VNRFLRLRPGTQKTDILPALKRVQAgHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:COG2401 103 IDAIGRKGDFKDAVELLNAVGLSDA-VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-196 |
9.51e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSF-----------GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNGQ---- 66
Cdd:PRK15134 273 SPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQplhn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 67 ----------LRIGYVPQKLYLDTTLPLTVNRFL---------RLRPGTQKTDILPALKRVQaghlIDAPMQ-----KLS 122
Cdd:PRK15134 352 lnrrqllpvrHRIQVVFQDPNSSLNPRLNVLQIIeeglrvhqpTLSAAQREQQVIAVMEEVG----LDPETRhrypaEFS 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
7-179 |
9.67e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 74.22 E-value: 9.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGlvAPD----EGVIKRNGQLRIGYVPQK-----LY 77
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDEraragLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 LDTTLP-----LTVNRFLR-----LRPGTQKTDI-----LPALKRVQAGHLIDAPMQK------LSGGETQRVLLARALL 136
Cdd:TIGR01978 81 LAFQYPeeipgVSNLEFLRsalnaRRSARGEEPLdlldfEKLLKEKLALLDMDEEFLNrsvnegFSGGEKKRNEILQMAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLREP-DRSFLIITH 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-208 |
1.01e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.39 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQ-RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL-----------R 68
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYlDTTLPLTV-------NRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
Cdd:PRK13647 81 VGLVFQDPD-DQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVS 208
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEgRVLAEGDKSLLT 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
2.02e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.12 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQR-----RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkRNGQLRIG-YVPQKLY 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDIYIGdKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 LDTTLPLTVNRFLRLR---------PGTQ------KTDIL--P-AL-------KRVQAGHL---------IDAPMQKLSG 123
Cdd:PRK13631 100 ITNPYSKKIKNFKELRrrvsmvfqfPEYQlfkdtiEKDIMfgPvALgvkkseaKKLAKFYLnkmglddsyLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSG 202
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKgKILKTG 258
|
250
....*....|...
gi 446125168 203 APEVVSMHPEFIS 215
Cdd:PRK13631 259 TPYEIFTDQHIIN 271
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-232 |
3.08e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 18 RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkRNGQL----------------RIGYVPQ----KLY 77
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-TVGDIvvsstskqkeikpvrkKVGVVFQfpesQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 78 LDTTLPLTVNRFLRLRPGTQKTDILPALKRVQAG---HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGladEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 155 GQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFISmfgprgAEQLGIYRHHH 232
Cdd:PRK13643 179 ARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKgHIISCGTPSDVFQEVDFLK------AHELGVPKATH 250
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-152 |
3.21e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNG--------QLRIGYVPQ-KLYLDTtl 82
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemRAISAYVQQdDLFIPT-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 pLTVNRFL----RLRPGTQKT---------DILPALKRVQAGH-LIDAP--MQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:TIGR00955 114 -LTVREHLmfqaHLRMPRRVTkkekrervdEVLQALGLRKCANtRIGVPgrVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
....*.
gi 446125168 147 PTQGVD 152
Cdd:TIGR00955 193 PTSGLD 198
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-179 |
4.27e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.57 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVR-----VVLGLVAPDEGVIKRNG---------- 65
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGrniyspdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 66 ---QLRIGYVPQ--------KLYLDTTLPLTVNRFLRLRPGTQKTdILPALKRVQ-----AGHLIDAPMQkLSGGETQRV 129
Cdd:PRK14267 81 ievRREVGMVFQypnpfphlTIYDNVAIGVKLNGLVKSKKELDER-VEWALKKAAlwdevKDRLNDYPSN-LSGGQRQRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125168 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSH 179
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-196 |
7.26e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSfGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPdeGVIKRNGQLRIG---YVPQKL- 76
Cdd:PRK10418 1 MPQQIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDgkpVAPCALr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 --YLDTTL--------PL---------TVNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
Cdd:PRK10418 78 grKIATIMqnprsafnPLhtmhthareTCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-184 |
2.56e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 22 DVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ------------LR--IGYVPQKLY--LDTTL--- 82
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklqaLRrdIQFIFQDPYasLDPRQtvg 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 -----PLTVNRFLRLRPGTQKTDILpaLKRV--QAGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
Cdd:PRK10261 422 dsimePLRVHGLLPGKAAAARVAWL--LERVglLPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180
....*....|....*....|....*....
gi 446125168 156 QVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVV 527
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-191 |
2.71e-14 |
|
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: 71.78 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGlVAPD---EGVIKRNGQ------LR------ 68
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSplkasnIRdterag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 69 IGYVPQKLYLDTTLPLTVNRFLR---LRPGTQKTD---ILPA---LKRVQAGHLIDA-PMQKLSGGETQRVLLARALLNR 138
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneiTLPGGRMAYnamYLRAknlLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTI 211
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-166 |
4.91e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 13 SFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD--EGVIKRNGQ-------LRIGYVPQK--LYLDTT 81
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRkptkqilKRTGFVTQDdiLYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 82 L--PLTVNRFLRLRPGTQKTD-------ILPALKRVQAGHLI--DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
Cdd:PLN03211 157 VreTLVFCSLLRLPKSLTKQEkilvaesVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170
....*....|....*.
gi 446125168 151 VDVngqVALYDLIDQL 166
Cdd:PLN03211 237 LDA---TAAYRLVLTL 249
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-196 |
7.30e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.43 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRV--LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGY 71
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlasLRnqVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYL--DTTlpltVNRFLRLRPGT-QKTDILPALKRVQAGHLIDaPMQK------------LSGGETQRVLLARALL 136
Cdd:PRK11176 422 VSQNVHLfnDTI----ANNIAYARTEQySREQIEEAARMAYAMDFIN-KMDNgldtvigengvlLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEILVVED 553
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-227 |
7.93e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.39 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFG-----QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL--------RIGY 71
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLDTTLPL------TVNRFLRLRP---GTQKTDIlPALKRVQ------AGHLIDAPMQKLSGGETQRVLLARALL 136
Cdd:PRK13649 83 IRKKVGLVFQFPEsqlfeeTVLKDVAFGPqnfGVSQEEA-EALAREKlalvgiSESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFIS 215
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDIFQDVDFLE 240
|
250
....*....|..
gi 446125168 216 mfgprgAEQLGI 227
Cdd:PRK13649 241 ------EKQLGV 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-212 |
7.94e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.84 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 14 FGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-----------GQLRIGYVPQKLYLDTTL 82
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkdGQLKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 PLTVNRFLRLRPGTQKTDILPA------LKRVQAGHL---------IDAPMQ-----KLSGGETQRVLLARALLNRPQLL 142
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEApiqvlgLSKQEARERavkylakvgIDERAQgkypvHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLmVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQgKIEEEGAPEQLFGNPQ 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-180 |
7.98e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIG------------ 70
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpprnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 ----YVPQKLYLDTTLPLTVNRFLRLRPGTQKTDILPALKRVQA--GHL-------------------IDAPMQKLSGGE 125
Cdd:PRK11147 82 tvydFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEqlDHHnlwqlenrinevlaqlgldPDAALSSLSGGW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 126 TQRVLLARALLNRPQLLVLDEPTQGVDVngqvalyDLIDQLR---RELDCAVLMVSHD 180
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDI-------ETIEWLEgflKTFQGSIIFISHD 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-192 |
1.14e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 17 RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-LRIGYVPQklyldttlplTVNRFLRLRPG 95
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpIDIRSPRD----------AIRAGIMLCPE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 96 TQKTDILPALKRVQ-------------AGHLIDA-----------------------PMQKLSGGETQRVLLARALLNRP 139
Cdd:PRK11288 336 DRKAEGIIPVHSVAdninisarrhhlrAGCLINNrweaenadrfirslniktpsreqLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-192 |
1.15e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKL-------------------YLDT 80
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvteerrstgiyaYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 81 TLPLTV-------NRFLRLRPGTQKTD---ILPALKRVQAGHliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
Cdd:PRK10982 344 GFNSLIsnirnykNKVGLLDNSRMKSDtqwVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125168 151 VDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRIL 462
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-181 |
1.81e-13 |
|
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: 66.44 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 26 ELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGqLRIGYVPQKLyldttlpltvnrflrlrpgtqktdilpal 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI----------------------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 106 krvqaghlidapmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
Cdd:cd03222 71 --------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-152 |
2.53e-13 |
|
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: 66.50 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 10 VSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVV-----LGLVapdEGVIKRNGQLR-------IGYVPQkly 77
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPLdknfqrsTGYVEQ--- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 78 LDTTLP-LTVNRFLRLrpgtqktdilpalkrvqaghliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:cd03232 87 QDVHSPnLTVREALRF----------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-199 |
4.22e-13 |
|
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: 68.78 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGqlRIGYVPQklyldttlpltvnrFLRLRPGTQK 98
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQ--------------TSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 99 TDILPAL-----------KRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
Cdd:TIGR01271 505 DNIIFGLsydeyrytsviKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125168 157 VALYD------LIDQLRreldcaVLMVSHDLHLvmAKTDEVLCLNHHIC 199
Cdd:TIGR01271 585 KEIFEsclcklMSNKTR------ILVTSKLEHL--KKADKILLLHEGVC 625
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-179 |
4.99e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.03 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------QLRIGYVPQKLylDTTLPLTV 86
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdiRNKAGMVFQNP--DNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 87 ----------NrfLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
Cdd:PRK13633 103 veedvafgpeN--LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180
....*....|....*....|...
gi 446125168 157 VALYDLIDQLRRELDCAVLMVSH 179
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITH 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-194 |
6.66e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRR----VLSDVSLELSPGKILTLLGPNGAGKS----TLVRVVL---GLVAPDEGVIKRNGQLRIGYV 72
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQK-----------LYLDTTLPLT-----------VNRFLRLRPGTQKTDILPALKRV-------QAGHLIDAPMQKLSG 123
Cdd:PRK10261 92 EQSaaqmrhvrgadMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMldqvripEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-207 |
9.15e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.69 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 3 SLVSLENVSVSFGQR----RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGL------VAPDEGVIKRNGQLRIGYV 72
Cdd:PRK11022 2 ALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQKLYLDTTL------PLTvnrflRLRPG-TQKTDILPALKRVQAGH----------------------LIDAPMQKLSG 123
Cdd:PRK11022 82 ERRNLVGAEVamifqdPMT-----SLNPCyTVGFQIMEAIKVHQGGNkktrrqraidllnqvgipdpasRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTdevlclnHHICCSGA 203
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAA-------HKIIVMYA 229
|
....
gi 446125168 204 PEVV 207
Cdd:PRK11022 230 GQVV 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-215 |
1.10e-12 |
|
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: 66.03 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGqlRIGYVPQklyldttlpltvnrFLRLRPGTQK 98
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQ--------------FSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 99 TDILPALKR--------VQAGHL---IDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
Cdd:cd03291 116 ENIIFGVSYdeyryksvVKACQLeedITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 157 VALYD-----LIDQLRReldcaVLMVSHDLHLvmAKTDEVLCLNHHIC--CSGAPEVVSMHPEFIS 215
Cdd:cd03291 196 KEIFEscvckLMANKTR-----ILVTSKMEHL--KKADKILILHEGSSyfYGTFSELQSLRPDFSS 254
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-169 |
1.34e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.58 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLvSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGviKRNGQLRigyVPQKLYLDT 80
Cdd:PRK10938 1 MSSL-QISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--ERQSQFS---HITRLSFEQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 81 TLPLTVNRFLR-----LRPGTQKT-----DIL------PAL-----KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
Cdd:PRK10938 75 LQKLVSDEWQRnntdmLSPGEDDTgrttaEIIqdevkdPARceqlaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190
....*....|....*....|....*....|
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-195 |
1.44e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 18 RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGQLRIGYVPQKLYLDT-TLPLTVNRF---- 89
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifKDEKNKKKTKEKEKVLEKlVIQKTRFKKikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 90 --LRLRPG-------------TQKTDIL-----------PALKRVQAG-HLIDAP---MQK----LSGGETQRVLLARAL 135
Cdd:PRK13651 101 keIRRRVGvvfqfaeyqlfeqTIEKDIIfgpvsmgvskeEAKKRAAKYiELVGLDesyLQRspfeLSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-152 |
1.70e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 22 DVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LRIGYVPQ--KLYLDttlpLTV--N 87
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagdiatrRRVGYMSQafSLYGE----LTVrqN 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 88 -----RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:NF033858 360 lelhaRLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-196 |
2.73e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLVSLENVSVSFGQR---------RVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-QLRIG 70
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 ---YVPQKLYL-----DTTL------------PLTVNRflRLRPGTQKTDILPALKRV--QAGHLIDAPmQKLSGGETQR 128
Cdd:PRK15112 81 dysYRSQRIRMifqdpSTSLnprqrisqildfPLRLNT--DLEPEQREKQIIETLRQVglLPDHASYYP-HMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHdlHLVMAK--TDEVLCLNH 196
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQ--HLGMMKhiSDQVLVMHQ 225
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-192 |
3.62e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.93 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAP------------DEGVIKRNGQLR-------IGYVPQ- 74
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtadrfrwnGIDLLKLSPRERrkiigreIAMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 -KLYLDTTLPL-----------TVNRFLRLRPGTQKTDILPALKRV---QAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
Cdd:COG4170 98 pSSCLDPSAKIgdqlieaipswTFKGKWWQRFKWRKKRAIELLHRVgikDHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV--MAKTDEVL 192
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESIsqWADTITVL 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-211 |
3.66e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.44 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGqrrvLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR------IGY 71
Cdd:PRK10070 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaELRevrrkkIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLDTTLPLTVNRFLRLR----PGTQKTD-ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
Cdd:PRK10070 111 VFQSFALMPHMTVLDNTAFGMElagiNAEERREkALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHP 211
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILNNP 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-191 |
5.43e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LE--NVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGlVAPD---EGVIKRNGQLR------------I 69
Cdd:NF040905 2 LEmrGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCrfkdirdsealgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 70 GYVPQKLYLDTTLPLTVNRFL---RLRPG-------TQKTDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLgneRAKRGvidwnetNRRAREL--LAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125168 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRE-LDCavLMVSHDLHLVMAKTDEV 191
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQgITS--IIISHKLNEIRRVADSI 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-191 |
6.00e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 17 RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------QLRIGYVPQKLYLDTTLP- 83
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprspldavKKGMAYITESRRDNGFFPn 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 84 ------LTVNRFLRL---------------RPGTQKTDILPALKrvqaGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
Cdd:PRK09700 356 fsiaqnMAISRSLKDggykgamglfhevdeQRTAENQRELLALK----CHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125168 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRI 479
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-211 |
1.79e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 16 QRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----QLRIGYVPQKLYLDTTLPL----TVN 87
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltKLQLDSWRSRLAVVSQTPFlfsdTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 88 RFLRL-RPGTQKTDILPALK---------RVQAGHLIDAPMQ--KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnG 155
Cdd:PRK10789 407 NNIALgRPDATQQEIEHVARlasvhddilRLPQGYDTEVGERgvMLSGGQKQRISIARALLLNAEILILDDALSAVD--G 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 156 QVAlYDLIDQLRRELDCAVLMVS-HDLHlVMAKTDEVLCLNH-HICCSGAPEVVSMHP 211
Cdd:PRK10789 485 RTE-HQILHNLRQWGEGRTVIISaHRLS-ALTEASEILVMQHgHIAQRGNHDQLAQQS 540
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-195 |
1.92e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR--IGYVPQKLYLDTTlplTVn 87
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmDLRkvLGIIPQAPVLFSG---TV- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 88 RFlRLRPGTQKTD--ILPALKRvqaGHLIDA--------PMQKLSGGET----QRVLL--ARALLNRPQLLVLDEPTQGV 151
Cdd:PLN03130 1330 RF-NLDPFNEHNDadLWESLER---AHLKDVirrnslglDAEVSEAGENfsvgQRQLLslARALLRRSKILVLDEATAAV 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 152 DVNGQValydLIDQLRRE--LDCAVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:PLN03130 1406 DVRTDA----LIQKTIREefKSCTMLIIAHRLNTII-DCDRILVLD 1446
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-179 |
2.61e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.39 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRNG---------QLR--IGYVPQKLYLdttlp 83
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGvswnsvtlqTWRkaFGVIPQKVFI----- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 84 LTVNRFLRLRPGTQKTD--ILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
Cdd:TIGR01271 1304 FSGTFRKNLDPYEQWSDeeIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180 190
....*....|....*....|....*....|....*
gi 446125168 151 VD-VNGQValydlidqLRREL-----DCAVLMVSH 179
Cdd:TIGR01271 1384 LDpVTLQI--------IRKTLkqsfsNCTVILSEH 1410
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-197 |
4.11e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD--EGVIKRNGQLRIGYVPQK---- 75
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEErahl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 76 -LYLDTTLPLTVN-----RFLRLRPGT-QKTDILPALKRVQAGHLIdapMQKL------------------SGGETQR-V 129
Cdd:CHL00131 85 gIFLAFQYPIEIPgvsnaDFLRLAYNSkRKFQGLPELDPLEFLEII---NEKLklvgmdpsflsrnvnegfSGGEKKRnE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 130 LLARALLNrPQLLVLDEPTQGVDvngqvalydlIDQLRreldcavlMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:CHL00131 162 ILQMALLD-SELAILDETDSGLD----------IDALK--------IIAEGINKLMTSENSIILITHY 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-216 |
5.42e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------QLRIGYVPQKlyldttlPLTVN 87
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlRFKITIIPQD-------PVLFS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 88 RFLR--LRPGTQKTD--ILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:TIGR00957 1374 GSLRmnLDPFSQYSDeeVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 153 VNGQvalyDLIDQLRREL--DCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAP-EVVSMHPEFISM 216
Cdd:TIGR00957 1454 LETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPsNLLQQRGIFYSM 1516
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-192 |
7.10e-11 |
|
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: 59.26 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLglvapdegviKRNGQLRIGYVPQKLYLDTTLPLtvnrflrlrpgtqkt 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------YASGKARLISFLPKFSRNKLIFI--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 100 DILPALKRVQAGHL-IDAPMQKLSGGETQRVLLARALLNRPQ--LLVLDEPTQGVDvngQVALYDLIDQLRRELDC--AV 174
Cdd:cd03238 66 DQLQFLIDVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDINQLLEVIKGLIDLgnTV 142
|
170
....*....|....*...
gi 446125168 175 LMVSHDLHlVMAKTDEVL 192
Cdd:cd03238 143 ILIEHNLD-VLSSADWII 159
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-180 |
8.11e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.01 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQL--------R-IGYVPQ 74
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadRdIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 75 K--LYldttlP-LTVNR----FLRLRpGTQKTDILpalKRVQA-------GHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
Cdd:PRK11650 84 NyaLY-----PhMSVREnmayGLKIR-GMPKAEIE---ERVAEaarilelEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125168 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD 194
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-181 |
8.90e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 8 ENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVR-------VVLGLVApdEGVIKRNGQ-------------L 67
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKnlyapdvdpvevrR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 68 RIGYVPQK-------LYLDTTLPLTVNRF---------LRLRPGTQKTDILPALKrvQAGhlidapmQKLSGGETQRVLL 131
Cdd:PRK14243 92 RIGMVFQKpnpfpksIYDNIAYGARINGYkgdmdelveRSLRQAALWDEVKDKLK--QSG-------LSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125168 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-204 |
2.17e-10 |
|
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: 60.41 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 17 RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LRIGYVPQK--LYLDTTLPL 84
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrQSLGMCPQHniLFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 TVNRFLRLRPGTQ---KTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
Cdd:TIGR01257 1023 HILFYAQLKGRSWeeaQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446125168 162 LIDQLRRELdcAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAP 204
Cdd:TIGR01257 1103 LLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQgRLYCSGTP 1144
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-218 |
2.76e-10 |
|
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: 60.41 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 29 PGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ----------LRIGYVPQKLYLDTTLPLTVNRFL--RLR--P 94
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisdvhQNMGYCPQFDAIDDLLTGREHLYLyaRLRgvP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 95 GTQKTDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCA 173
Cdd:TIGR01257 2044 AEEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRA 2122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125168 174 VLMVSHDLhlvmaKTDEVLCLNHHICCSGAPEVVSMHPEFISMFG 218
Cdd:TIGR01257 2123 VVLTSHSM-----EECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-194 |
3.46e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 7 LENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQlRIGYVPQKLYLDTTLPLtV 86
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFKSSKEALENGISM-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 87 NRFLRLRPGTQKTDILPALKRVQAGHLIDA-------------------PMQK---LSGGETQRVLLARALLNRPQLLVL 144
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQdkmyrdtkaifdeldididPRAKvatLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125168 145 DEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-152 |
4.47e-10 |
|
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: 59.57 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQlrIGYVPQKLYL-DTTL--------PLTVNRFl 90
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQAWIqNDSLrenilfgkALNEKYY- 730
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 91 rlRPGTQKTDILPALKRVQAGHL--IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:TIGR00957 731 --QQVLEACALLPDLEILPSGDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
114-181 |
6.34e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 6.34e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 114 IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSEL 464
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-195 |
7.89e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR--IG 70
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltDLRrvLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQKLYLDTTlplTVnRFlRLRPGTQKTD--ILPALKRVQAGHLID-APM----QKLSGGET----QRVLL--ARALLN 137
Cdd:PLN03232 1314 IIPQSPVLFSG---TV-RF-NIDPFSEHNDadLWEALERAHIKDVIDrNPFgldaEVSEGGENfsvgQRQLLslARALLR 1388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 138 RPQLLVLDEPTQGVDVNGQvalyDLIDQLRRE--LDCAVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTD----SLIQRTIREefKSCTMLVIAHRLNTII-DCDKILVLS 1443
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-152 |
8.11e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 10 VSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLV-----RVVLGLVAPDEGVIkrNG-------QLRIGYVPQK-L 76
Cdd:TIGR00956 769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVITGGDRLV--NGrpldssfQRSIGYVQQQdL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 YLDTTlplTVNRFLR----LR-----PGTQKTDILPALKRV-----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
Cdd:TIGR00956 847 HLPTS---TVRESLRfsayLRqpksvSKSEKMEYVEEVIKLlemesYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170
....*....|.
gi 446125168 143 V-LDEPTQGVD 152
Cdd:TIGR00956 924 LfLDEPTSGLD 934
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-196 |
1.72e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF-GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ---------LR--IGYV 72
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvLRqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 73 PQK--LYLDTTLP-LTVNRFLRlrpgtqKTDILPALKRVQAGHL-------IDAPM----QKLSGGETQRVLLARALLNR 138
Cdd:PRK10790 421 QQDpvVLADTFLAnVTLGRDIS------EEQVWQALETVQLAELarslpdgLYTPLgeqgNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIV-EADTILVLHR 549
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-152 |
1.79e-09 |
|
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: 55.73 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 2 TSLVSLENVSVSFGQRRV----LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNG--------- 65
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSkipiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGipykefaek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 66 -QLRIGYVPQKlylDTTLP-LTVNRFLRLRPGTQKTDILpalkrvqaghlidapmQKLSGGETQRVLLARALLNRPQLLV 143
Cdd:cd03233 81 yPGEIIYVSEE---DVHFPtLTVRETLDFALRCKGNEFV----------------RGISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 446125168 144 LDEPTQGVD 152
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
120-197 |
2.44e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.73 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 120 KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL---------VM----- 185
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMlsqwadkinVLycgqt 237
|
90
....*....|....*
gi 446125168 186 ---AKTDEVLCLNHH 197
Cdd:PRK15093 238 vetAPSKELVTTPHH 252
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-180 |
2.61e-09 |
|
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: 54.30 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 29 PGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrngqlrigyvpqkLYLDTtlpltvnrflrlrpgtqkTDILPALKRV 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------IYIDG------------------EDILEEVLDQ 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 109 QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID-----QLRRELDCAVLMVSHD 180
Cdd:smart00382 49 LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTND 125
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-181 |
4.62e-09 |
|
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: 55.63 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF--GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPdEGVIKRNG---------QLR--IGY 71
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGvswnsvplqKWRkaFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 72 VPQKLYLDTTlPLTVNrflrLRPGTQKTD--ILPALKRVQAGHLIDA-PMQ----------KLSGGETQRVLLARALLNR 138
Cdd:cd03289 82 IPQKVFIFSG-TFRKN----LDPYGKWSDeeIWKVAEEVGLKSVIEQfPGQldfvlvdggcVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125168 139 PQLLVLDEPTQGVD-VNGQValydlidqLRREL-----DCAVLMVSHDL 181
Cdd:cd03289 157 AKILLLDEPSAHLDpITYQV--------IRKTLkqafaDCTVILSEHRI 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-181 |
5.73e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.49 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 9 NVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGViKRNGQL------------------RIG 70
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVllggrsifnyrdvlefrrRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YVPQKlylDTTLPLTVN-------RFLRLRPGTQKTDILPAlKRVQAG-------HLIDAPMqKLSGGETQRVLLARALL 136
Cdd:PRK14271 105 MLFQR---PNPFPMSIMdnvlagvRAHKLVPRKEFRGVAQA-RLTEVGlwdavkdRLSDSPF-RLSGGQQQLLCLARTLA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125168 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNL 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-207 |
6.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.38 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQ-RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------QLR--IG 70
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqGIRklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 71 YV---PQKLYLDTTLPLTVN---RFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
Cdd:PRK13644 81 IVfqnPETQFVGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125168 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAkTDEVLCLNH-HICCSGAPEVV 207
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRgKIVLEGEPENV 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-231 |
8.09e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 119 QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLNHHI 198
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNNPD 1435
|
90 100 110
....*....|....*....|....*....|...
gi 446125168 199 CCSGAPEVVSMHPEFISMfgprgaeQLGIYRHH 231
Cdd:PTZ00265 1436 RTGSFVQAHGTHEELLSV-------QDGVYKKY 1461
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-184 |
1.38e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.05 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIgyVPQKLYLDTTLPLTVN-RFLRLRPGTQK 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV--IAISAGLSGQLTGIENiEFKMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 99 TDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEptqGVDVNGQVALYDLIDQLR--RELDC 172
Cdd:PRK13546 118 KEIKAMTPKIiefsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCLDKIYefKEQNK 194
|
170
....*....|..
gi 446125168 173 AVLMVSHDLHLV 184
Cdd:PRK13546 195 TIFFVSHNLGQV 206
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-155 |
2.17e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQ-----------LRIGYVPQ-KLYLDTTLPLTV 86
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfmAYLGHLPGlKADLSTLENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125168 87 NRFLRLRPGTQKTDilPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
Cdd:PRK13543 106 LCGLHGRRAKQMPG--SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-182 |
2.18e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSF---GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAP--DEGVIKRNgqlRIGYVPQKLYL- 78
Cdd:PLN03130 615 ISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrsDASVVIRG---TVAYVPQVSWIf 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 -----DTTL------PLTVNRFLRLRPGTQKTDILPalkrvqAGHL--IDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
Cdd:PLN03130 692 natvrDNILfgspfdPERYERAIDVTALQHDLDLLP------GGDLteIGERGVNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125168 146 EPTQGVD--VNGQVALYDLIDQLRREldcAVLMVSHDLH 182
Cdd:PLN03130 766 DPLSALDahVGRQVFDKCIKDELRGK---TRVLVTNQLH 801
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-182 |
2.28e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQK--LYLDTT 81
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDqfAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 82 LPLTV--------------NRFLRLRPGTQKTDILPALKRVQ------------AGHLI----------DAPMQKLSGGE 125
Cdd:PRK15064 81 VLDTVimghtelwevkqerDRIYALPEMSEEDGMKVADLEVKfaemdgytaearAGELLlgvgipeeqhYGLMSEVAPGW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIdqlrRELDCAVLMVSHDLH 182
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHDRH 213
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-163 |
2.96e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRrVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-RNGQLR------IGYVPQKL 76
Cdd:PRK13541 1 MLSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYyKNCNINniakpyCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 YLdtTLPLTVNRFLRL--RPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
Cdd:PRK13541 80 GL--KLEMTVFENLKFwsEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
....*....
gi 446125168 155 GQVALYDLI 163
Cdd:PRK13541 158 NRDLLNNLI 166
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-184 |
3.72e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR---VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDE--GVIKRNGqlrIGYVPQKLYL- 78
Cdd:PLN03232 615 ISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtsSVVIRGS---VAYVPQVSWIf 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 DTTLPLTV--------NRFLRLRPGT---QKTDILPALKRVQAGHlidaPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
Cdd:PLN03232 692 NATVRENIlfgsdfesERYWRAIDVTalqHDLDLLPGRDLTEIGE----RGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125168 148 TQGVDVNGQVALYD--LIDQLRREldcAVLMVSHDLHLV 184
Cdd:PLN03232 768 LSALDAHVAHQVFDscMKDELKGK---TRVLVTNQLHFL 803
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-152 |
4.60e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 17 RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVL----GLVAPDEGVIKRNGQLRIGYVPQK----LY---LDTTLP-L 84
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYrgdvVYnaeTDVHFPhL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 TVNRFL----RLRpgTQKTDILPALKRVQAGHLIDAPMQKL------------------SGGETQRVLLARALLNRPQLL 142
Cdd:TIGR00956 154 TVGETLdfaaRCK--TPQNRPDGVSREEYAKHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSIAEASLGGAKIQ 231
|
170
....*....|
gi 446125168 143 VLDEPTQGVD 152
Cdd:TIGR00956 232 CWDNATRGLD 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-154 |
6.20e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRvVLGLVAPDEgvIKRNGQlrIGYVPQKLYLDTTLPL 84
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLR-YMAMHAIDG--IPKNCQ--ILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 85 T------VNRFLRLRP---------------------GTQKTDIL--PALKRVQAGH----LIDA--------------- 116
Cdd:PLN03073 253 QcvlntdIERTQLLEEeaqlvaqqrelefetetgkgkGANKDGVDkdAVSQRLEEIYkrleLIDAytaearaasilagls 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125168 117 ---PMQK-----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
Cdd:PLN03073 333 ftpEMQVkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-181 |
7.17e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRR---VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------QLRI 69
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 70 GYVPQKLYL----------------------------------------------------DTTLPLTVNRFLRLRPGTQ 97
Cdd:PTZ00265 463 GVVSQDPLLfsnsiknnikyslyslkdlealsnyynedgndsqenknkrnscrakcagdlnDMSNTTDSNELIEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 98 ---KTDILPALKRV-----------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
Cdd:PTZ00265 543 tikDSEVVDVSKKVlihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250
....*....|....*...
gi 446125168 164 DQLRRELDCAVLMVSHDL 181
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRL 640
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-182 |
2.69e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.02 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLR---------------IGYVPQKLYL-DTTL- 82
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLlNATVe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 -------PLTVNRF------LRLRPgtqKTDILPALKRVQAGHL-IDapmqkLSGGETQRVLLARALLNRPQLLVLDEPT 148
Cdd:cd03290 97 enitfgsPFNKQRYkavtdaCSLQP---DIDLLPFGDQTEIGERgIN-----LSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|....*
gi 446125168 149 QGVDVN-GQVALYDLIDQLRRELDCAVLMVSHDLH 182
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-181 |
2.71e-07 |
|
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: 48.90 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 17 RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIG-YVPQklyldttlpltvnrflrlrpg 95
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGcIVAA--------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 96 tqkTDILPALKRVQaghlidapmqkLSGGETQRV----LLARALLNRPQLLVLDEPTQGVD-VNGQVALYDLIDQLRRel 170
Cdd:cd03227 67 ---VSAELIFTRLQ-----------LSGGEKELSalalILALASLKPRPLYILDEIDRGLDpRDGQALAEAILEHLVK-- 130
|
170
....*....|.
gi 446125168 171 DCAVLMVSHDL 181
Cdd:cd03227 131 GAQVIVITHLP 141
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-196 |
4.28e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrnGQLRIGYVPQKLYL------DTTLPLTVNRFLRL 92
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQQAWImnatvrGNILFFDEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 93 RPGTQKTDILPALKRVQAG--HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN-GQVALYDLIdqlRRE 169
Cdd:PTZ00243 753 ADAVRVSQLEADLAQLGGGleTEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECF---LGA 829
|
170 180
....*....|....*....|....*...
gi 446125168 170 LDCAV-LMVSHDLHLVmAKTDEVLCLNH 196
Cdd:PTZ00243 830 LAGKTrVLATHQVHVV-PRADYVVALGD 856
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-179 |
7.32e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 4 LVSLENVSVSFGQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGL--VAPDEGVIKRNGQLRIGYVPQK-----L 76
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDragegI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 77 YLDTTLPLTV----NRFLRLRP--GTQKTDILPALKRVQAGHLIDAPMQKL---------------SGGETQRV-LLARA 134
Cdd:PRK09580 81 FMAFQYPVEIpgvsNQFFLQTAlnAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNdILQMA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125168 135 LLNrPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
Cdd:PRK09580 161 VLE-PELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-222 |
1.09e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------QLR--IGYVPQKLYL-DTTLPLTV 86
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreigayglrELRrqFSMIPQDPVLfDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 87 NRFLRLRPGtqktDILPALK------RVQA-GHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVL-DEPTQGVDvn 154
Cdd:PTZ00243 1405 DPFLEASSA----EVWAALElvglreRVASeSEGIDSRVLEggsnYSVGQRQLMCMARALLKKGSGFILmDEATANID-- 1478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125168 155 gqVALYDLIDQLRRELDCA--VLMVSHDLHLVmAKTDEVLCLNHHICCS-GAPEVVSMHPE--FISM---FGPRGA 222
Cdd:PTZ00243 1479 --PALDRQIQATVMSAFSAytVITIAHRLHTV-AQYDKIIVMDHGAVAEmGSPRELVMNRQsiFHSMveaLGRSEA 1551
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
121-184 |
1.14e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.38 E-value: 1.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125168 121 LSGGETQRVLLARALLNR---PQLLVLDEPTQGV---DVNgqvalyDLIDQLRRELDC--AVLMVSHDLHLV 184
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVK------KLLEVLQRLVDKgnTVVVIEHNLDVI 235
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-184 |
1.19e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 1.19e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 117 PMQKLSGGETQRVLLARALLN---RPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLV 184
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVV 875
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-242 |
1.39e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 15 GQRRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKL-YLDTTLPLTV---NRFL 90
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpALPQPALEYVidgDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 91 R-----LRPGTQKTD---------ILPALK----RVQAGHLIDA----------PMQKLSGGETQRVLLARALLNRPQLL 142
Cdd:PRK10636 92 RqleaqLHDANERNDghaiatihgKLDAIDawtiRSRAASLLHGlgfsneqlerPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 143 VLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHDLHLVMAKTDEVLclnhHICCSGAPEVVSMHPEFISMFGPRGA 222
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWL----EKWLKSYQGTLILISHDRDFLDPIVDKII----HIEQQSLFEYTGNYSSFEVQRATRLA 243
|
250 260
....*....|....*....|
gi 446125168 223 EQLGIYRHHHNHRHDLQGRI 242
Cdd:PRK10636 244 QQQAMYESQQERVAHLQSYI 263
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
117-208 |
1.72e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 117 PMQKLSGGETQRVLLARALLNR---PQLLVLDEPTQGV---DVNgqvalyDLIDQLRRELDC--AVLMVSHDLHlVMAKT 188
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIK------KLLEVLQRLVDKgnTVVVIEHNLD-VIKTA 898
|
90 100
....*....|....*....|....*..
gi 446125168 189 DEVLCL-------NHHICCSGAPEVVS 208
Cdd:TIGR00630 899 DYIIDLgpeggdgGGTVVASGTPEEVA 925
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-169 |
2.25e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 14 FGQRRVLSDVSLELSPGKILTLLGPNGAG--KSTLVRVVLGlvaPDEG------------------VIKRNGQLRIGYVP 73
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGrrpwrf*twcanrralrrTIG*HRPVR*GRRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 74 -----QKLYLdttlpltVNRFLRLRPGTQKTDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
Cdd:NF000106 100 sfsgrENLYM-------IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180
....*....|....*....|.
gi 446125168 149 QGVDVNGQVALYDLIDQLRRE 169
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRD 193
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-184 |
2.98e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQKlyLDTTLPLTVNRFLR-LRPGTQK 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSG--LNGQLTGIENIELKgLMMGLTK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 99 TDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEptqGVDVNGQVALYDLIDQLR--RELDC 172
Cdd:PRK13545 118 EKIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMNefKEQGK 194
|
170
....*....|..
gi 446125168 173 AVLMVSHDLHLV 184
Cdd:PRK13545 195 TIFFISHSLSQV 206
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-182 |
6.17e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQRRV-LSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGQLRIGYVPQK-LYLDTTL 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 83 PLTVNRFLRLRpGTQKTDILPA-----LKRVQAGH---LIDAPMQ--KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:PRK10522 403 FTDFHLFDQLL-GPEGKPANPAlvekwLERLKMAHkleLEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190
....*....|....*....|....*....|
gi 446125168 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLH 182
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISHDDH 511
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-184 |
1.32e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 33 LTLL-GPNGAGKSTL---VRVVL-GLVAP--DEGVIKRN---GQLRIGYVPQKLYLDTTLPLTVNRFLR-------LRPG 95
Cdd:cd03240 24 LTLIvGQNGAGKTTIieaLKYALtGELPPnsKGGAHDPKlirEGEVRAQVKLAFENANGKKYTITRSLAilenvifCHQG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 96 TQKTDILPALKRVQAGhlidapmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV-NGQVALYDLIDQLRRELDCAV 174
Cdd:cd03240 104 ESNWPLLDMRGRCSGG-------EKVLASLIIRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQL 176
|
170
....*....|
gi 446125168 175 LMVSHDLHLV 184
Cdd:cd03240 177 IVITHDEELV 186
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-186 |
1.54e-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: 41.86 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 20 LSDVSLELSPGKILTLLGPNGAGKSTLV----------RVVLGLVA-----------PD----EGV-----IKrngQLRI 69
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAyarqflgqmdkPDvdsiEGLspaiaID---QKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 70 GYVPQKLYLDTTlplTVNRFLRL---RPGTQKTdiLPALKRVQAGHL-IDAPMQKLSGGETQRVLLARALLNRPQ--LLV 143
Cdd:cd03270 88 SRNPRSTVGTVT---EIYDYLRLlfaRVGIRER--LGFLVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125168 144 LDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMA 186
Cdd:cd03270 163 LDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA 204
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-150 |
1.55e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.55e-04
10 20 30
....*....|....*....|....*....|...
gi 446125168 121 LSGGETQRVLLARALLNRPQ---LLVLDEPTQG 150
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTG 859
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-150 |
1.78e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.78e-04
10 20 30
....*....|....*....|....*....|...
gi 446125168 121 LSGGETQRVLLARALLNRP---QLLVLDEPTQG 150
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTG 863
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
1-185 |
4.38e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.72 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 1 MTSLvSLENvsvsFGQrrvLSDVSLELSPgkiLTLL-GPNGAGKSTLVRVVLGLVapdegvikrngQLRIGYVP-QKLYL 78
Cdd:COG4938 1 IKSI-SIKN----FGP---FKEAELELKP---LTLLiGPNGSGKSTLIQALLLLL-----------QSNFIYLPaERSGP 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 DTTLPLTVNRFLRLRPGTQKT-DILPALKRVQAG--------HLIDAPMQKLSGGET----------------------- 126
Cdd:COG4938 59 ARLYPSLVRELSDLGSRGEYTaDFLAELENLEILddkskellEQVEEWLEKIFPGKVevdassdlvrlvfrpsgngkrip 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125168 127 -------QR-----VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIdqlrreldcaVLMVSHDLHLVM 185
Cdd:COG4938 139 lsnvgsgVSellpiLLALLSAAKPGSLLIIEEPEAHLHPKAQSALAELL----------AELANSGVQVII 199
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-68 |
7.54e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 7.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 5 VSLENVsvsfgqrRVLSDVSLELSPGkiLTLL-GPNGAGKSTLV---RVVLGLVAPDEGVIKRNGQLR 68
Cdd:pfam13476 1 LTIENF-------RSFRDQTIDFSKG--LTLItGPNGSGKTTILdaiKLALYGKTSRLKRKSGGGFVK 59
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-194 |
1.08e-03 |
|
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: 39.51 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 5 VSLENVSVSFGQ--RRVLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----QLRIGYVPQKLYL 78
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 79 DTTLPLTVNRFLR--LRPGTQKTD--ILPALKRVQAGHLI-------DAPM----QKLSGGETQRVLLARALLNRPQLLV 143
Cdd:cd03288 100 ILQDPILFSGSIRfnLDPECKCTDdrLWEALEIAQLKNMVkslpgglDAVVteggENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125168 144 LDEPTQGVDVNGQVALYDLIdqLRRELDCAVLMVSHDLHLVMaKTDEVLCL 194
Cdd:cd03288 180 MDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTIL-DADLVLVL 227
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
18-55 |
1.37e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 1.37e-03
10 20 30
....*....|....*....|....*....|....*....
gi 446125168 18 RVLSDVSLELSPgkiLTLL-GPNGAGKSTLVRvVLGLVA 55
Cdd:COG4637 11 KSLRDLELPLGP---LTVLiGANGSGKSNLLD-ALRFLS 45
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
24-152 |
1.60e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 38.73 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 24 SLELSPGKILTL-LGPNGAGKSTLV-RVVLGLVAP------------------DEGVI-----KRNGQLRIGYVPQKLYL 78
Cdd:cd03277 16 ETEFRPGPSLNMiIGPNGSGKSSIVcAICLGLGGKpkllgrakkvgefvkrgcDEGTIeielyGNPGNIQVDNLCQFLPQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125168 79 DttlplTVNRFLRLRPgtqkTDILPALKRVQAGHLIDAPMQklSGGE----TQRVLLARALLNRPQLLVLDEPTQGVD 152
Cdd:cd03277 96 D-----RVGEFAKLSP----IELLVKFREGEQLQELDPHHQ--SGGErsvsTMLYLLSLQELTRCPFRVVDEINQGMD 162
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
27-52 |
2.69e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.38 E-value: 2.69e-03
10 20
....*....|....*....|....*.
gi 446125168 27 LSPGKILTLLGPNGAGKSTLVRVVLG 52
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
121-179 |
3.38e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 3.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125168 121 LSGGETQ------RVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID-QLRRELDC-AVLMVSH 179
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDIpQVIMISH 868
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
5-48 |
3.38e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 3.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446125168 5 VSLENVsvsfgqrRVLSDVSLELSPGKILTLL-GPNGAGKSTLVR 48
Cdd:COG3950 6 LTIENF-------RGFEDLEIDFDNPPRLTVLvGENGSGKTTLLE 43
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
27-179 |
4.95e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 37.57 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 27 LSPGKILTLLGPNGAGKSTL-----VRVVLGLVAPDEGVIKRNgqlrigyVpqkLYLDTTLPltvnrflrlrpgtqKTDI 101
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLalqlaAAVAAGGPWLGRRVPPGK-------V---LYLAAEDD--------------RGEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 102 LPALKRVQAGH-----LIDAPMQKLSGGETQ------RVLLARALLNRPQLLVLDePTQ---GVDVN--GQV-ALYDLID 164
Cdd:COG3598 66 RRRLKALGADLglpfaDLDGRLRLLSLAGDLddtddlEALERAIEEEGPDLVVID-PLArvfGGDENdaEEMrAFLNPLD 144
|
170
....*....|....*
gi 446125168 165 QLRRELDCAVLMVSH 179
Cdd:COG3598 145 RLAERTGAAVLLVHH 159
|
|
| PrkA |
COG2766 |
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]; |
31-48 |
7.51e-03 |
|
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
Pssm-ID: 442049 [Multi-domain] Cd Length: 675 Bit Score: 37.51 E-value: 7.51e-03
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-75 |
8.97e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.13 E-value: 8.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125168 19 VLSDVSLELSPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNGQLRIGYVPQK 75
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRK 239
|
|
| |
