|
Name |
Accession |
Description |
Interval |
E-value |
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-251 |
3.04e-178 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 489.63 E-value: 3.04e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDT 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 81 TLPLTVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALY 160
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAPEVVSMHPEFISMFGQRGAEQLGIYRHNHNHRHDLQG 240
Cdd:PRK09544 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVVSLHPEFISMFGPRGAEQLGIYRHHHNHRHDLQG 240
|
250
....*....|.
gi 489125078 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 |
8.03e-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: 8.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------LRIGYVPQ 74
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYLDTTLPLTV-----------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLV 143
Cdd:COG1121 83 RAEVDWDFPITVrdvvlmgrygrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 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 |
1.06e-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: 248.99 E-value: 1.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------LRIGYVPQKLYLD 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 80 TTLPLTVSRFMRL----------RPGTK-KEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:cd03235 81 RDFPISVRDVVLMglyghkglfrRLSKAdKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489125078 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSG 202
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-215 |
8.22e-57 |
|
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: 181.78 E-value: 8.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------RIGYV 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLylDTTLPLTV------------SRFMRLRpgtkKED---ILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLN 137
Cdd:COG1120 81 PQEP--PAPFGLTVrelvalgryphlGLFGRPS----AEDreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVsMHPEFIS 215
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLkDGRIVAQGPPEEV-LTPELLE 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-205 |
1.69e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.56 E-value: 1.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LRIGYVPQ 74
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYLDTTLplTV-------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEP 147
Cdd:COG1131 81 EPALYPDL--TVrenlrffARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 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 |
1.06e-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: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------RIGYVPQ 74
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkelarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 klyldttlpltvsrfmrlrpgtkkedilpALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVN 154
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489125078 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 |
5.10e-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: 161.80 E-value: 5.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LRIGYVPQ 74
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkepeevkRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYLDTTlpLTVsrfmrlrpgtkkEDILpalkrvqaghlmnapmqKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVN 154
Cdd:cd03230 81 EPSLYEN--LTV------------RENL-----------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489125078 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03230 130 SRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNN 170
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-193 |
1.06e-46 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 153.93 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 13 SYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTTLPLTVSRFMRL 92
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 93 ---------RPGTK--KEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYD 161
Cdd:NF040873 81 grwarrglwRRLTRddRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180 190
....*....|....*....|....*....|..
gi 489125078 162 LIDQLRRElDCAVLMVSHDLHLVMAKTDEVLC 193
Cdd:NF040873 161 LLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-196 |
2.68e-45 |
|
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: 151.50 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSY----GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL------------ 67
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 --RIGYVPQKLY--LDTTL--------PLTVsRFMRLRPGTKKEDILPALKRVQ--AGHLMNAPMQkLSGGETQRVLLAR 133
Cdd:cd03257 81 rkEIQMVFQDPMssLNPRMtigeqiaePLRI-HGKLSKKEARKEAVLLLLVGVGlpEEVLNRYPHE-LSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-214 |
2.37e-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: 149.02 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------RIGYV 72
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQklYLDTTL--PlTVSR---F----MRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLV 143
Cdd:COG1122 81 FQ--NPDDQLfaP-TVEEdvaFgpenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHH-ICCSGAPEVVSMHPEFI 214
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGrIVADGTPREVFSDYELL 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-196 |
8.50e-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: 148.03 E-value: 8.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQ----RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------R 68
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkafrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLY--------LDTTL--PLTVSRFMRLRpgtkkEDILPALKRV--QAGHLMNAPMQkLSGGETQRVLLARALL 136
Cdd:COG1124 81 VQMVFQDPYaslhprhtVDRILaePLRIHGLPDRE-----ERIAELLEQVglPPSFLDRYPHQ-LSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-196 |
1.11e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 149.10 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-------RIGYVPQK-- 75
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPldpedrrRIGYLPEErg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 LYLDTTLPLTVSRFMRLRpGTKKEDILPA----LKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGV 151
Cdd:COG4152 82 LYPKMKVGEQLVYLARLK-GLSKAEAKRRadewLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 152 D-VNGQVaLYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4152 161 DpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINK 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-195 |
2.77e-43 |
|
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: 145.50 E-value: 2.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG-------QLRIGYVPQK-- 75
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaaRNRIGYLPEErg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 LYLDTTLPLTVSRFMRLRpGTKKEDILPA----LKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGV 151
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLK-GLKKEEARRRidewLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489125078 152 DVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd03269 160 DPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLN 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-205 |
4.70e-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: 153.38 E-value: 4.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR-VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGYV 72
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpasWRrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYLdttLPLTVSRFMRL-RPGTKKEDILPALKRVQAGHLMNAPMQK-----------LSGGETQRVLLARALLNKPQ 140
Cdd:COG4988 417 PQNPYL---FAGTIRENLRLgRPDASDEELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCLNH-HICCSGAPE 205
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL-LAQADRILVLDDgRIVEQGTHE 556
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-180 |
4.76e-43 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 144.93 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL----------RIGYVP 73
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QKLYLDTTLPLT-----VSRFMRLRPGTkkEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:COG4133 82 HADGLKPELTVRenlrfWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|..
gi 489125078 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
Cdd:COG4133 160 TALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-196 |
9.12e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.59 E-value: 9.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQR-----RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL--------- 67
Cdd:COG1123 258 EPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrsl 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 -----RIGYVPQKLY--LDTTLPL--TVSRFMRLRPGTKKEDILP----ALKRVQ--AGHLMNAPMQkLSGGETQRVLLA 132
Cdd:COG1123 338 relrrRVQMVFQDPYssLNPRMTVgdIIAEPLRLHGLLSRAERRErvaeLLERVGlpPDLADRYPHE-LSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 133 RALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-212 |
2.02e-42 |
|
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: 150.82 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV---AADEGVIKRNGQ--------- 66
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGRdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 --LRIGYVPQKLylDTTL-PLTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALL 136
Cdd:COG1123 81 rgRRIGMVFQDP--MTQLnPVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEILAAPQ 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-197 |
6.00e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.26 E-value: 6.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------RIGYVPQ 74
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYLdttLPLTVSRFMRLRPGTKK-----EDILPALKRVQ-AGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:COG4619 82 EPAL---WGGTVRDNLPFPFQLRErkfdrERALELLERLGlPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489125078 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-211 |
7.56e-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: 146.01 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------RIGY 71
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLdttLP-LTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNA-PMQkLSGGETQRVLLARALLNKPQLL 142
Cdd:COG3842 82 VFQDYAL---FPhLTVAenvafglRMRGVPKAEIRARVAELLELVGLEGLADRyPHQ-LSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 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 |
7.64e-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: 143.26 E-value: 7.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-------------- 66
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 -------------------LRIGYVPQklyLDTTLPLTVSRFMRLRPGTKK--EDILPALKRVQAGHLMNAPMQKLSGGE 125
Cdd:COG0411 81 iartfqnprlfpeltvlenVLVAAHAR---LGRGLLAALLRLPRARREEREarERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 126 TQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAP 204
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFgRVIAEGTP 237
|
250
....*....|
gi 489125078 205 EVVSMHPEFI 214
Cdd:COG0411 238 AEVRADPRVI 247
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-215 |
1.34e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 142.56 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYVPQkl 76
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspwelaRRRAVLPQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 77 ylDTTL--PLTVSRFMRL------RPGTKKEDILP-ALKRVQAGHLMNAPMQKLSGGETQRVLLARALL-------NKPQ 140
Cdd:COG4559 83 --HSSLafPFTVEEVVALgraphgSSAAQDRQIVReALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVsMHPEFIS 215
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQgRLVAQGTPEEV-LTDELLE 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-183 |
1.65e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.72 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQ----RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------- 66
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 --LR---IGYVPQKLYLdttLP-LTV-------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLAR 133
Cdd:COG1136 81 arLRrrhIGFVFQFFNL---LPeLTAlenvalpLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489125078 134 ALLNKPQLLVLDEPTQGVD-VNGQvALYDLIDQLRRELDCAVLMVSHDLHL 183
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDsKTGE-EVLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-194 |
2.16e-41 |
|
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: 141.76 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGV----------------IKRng 65
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 qlRIGYVPQKLYLDTTLPLTV-----SRF---MRLRPGTKKEDILPA---LKRVQAGHLMNAPMQKLSGGETQRVLLARA 134
Cdd:COG1119 79 --RIGLVSPALQLRFPRDETVldvvlSGFfdsIGLYREPTDEQRERArelLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 135 LLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-214 |
2.47e-41 |
|
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: 141.66 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-------------- 66
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 LRIGYVPQK--LYLDTT------LPLTvsRFMRLRPGTKKEDILPALKRV---QAGHLMnaPMQkLSGGETQRVLLARAL 135
Cdd:COG1127 82 RRIGMLFQGgaLFDSLTvfenvaFPLR--EHTDLSEAEIRELVLEKLELVglpGAADKM--PSE-LSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 136 LNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVV--SMHP- 211
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLaDGKIIAEGTPEELlaSDDPw 236
|
....*
gi 489125078 212 --EFI 214
Cdd:COG1127 237 vrQFL 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-181 |
6.45e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.00 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY----GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------LRIG 70
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKlylDTTLP-LTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNA-PMQkLSGGETQRVLLARALLNKPQL 141
Cdd:COG1116 84 VVFQE---PALLPwLTVLdnvalglELRGVPKAERRERARELLELVGLAGFEDAyPHQ-LSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-197 |
1.06e-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: 139.14 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYV 72
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKlyldttlP------LTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKP 139
Cdd:cd03225 81 FQN-------PddqffgPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-195 |
1.15e-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: 137.38 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYVPQ 74
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdiaklpleelrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 klyldttlpltvsrfmrlrpgtkkedilpalkrvqaghlmnapmqkLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVN 154
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489125078 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-196 |
2.40e-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: 139.22 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----------QLRIGYVP 73
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkepreaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QKLYLDTTlpLTV-------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:COG4555 81 DERGLYDR--LTVreniryfAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489125078 147 PTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-196 |
2.82e-40 |
|
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: 136.74 E-value: 2.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYG--QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGY 71
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldlesLRknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLdttlpltvsrFmrlrPGTKKEDIlpalkrvqaghlmnapmqkLSGGETQRVLLARALLNKPQLLVLDEPTQGV 151
Cdd:cd03228 81 VPQDPFL----------F----SGTIRENI-------------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489125078 152 DVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03228 128 DPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-211 |
2.74e-39 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 136.09 E-value: 2.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ--------------LRIG 70
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQK--LYLDTT------LPLtvSRFMRLRPGTKKEDILPALKRV---QAGHLMnaPMQkLSGGETQRVLLARALLNKP 139
Cdd:cd03261 81 MLFQSgaLFDSLTvfenvaFPL--REHTRLSEEEIREIVLEKLEAVglrGAEDLY--PAE-LSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVV--SMHP 211
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEGTPEELraSDDP 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-180 |
3.62e-39 |
|
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: 135.31 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQ----RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR 68
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 ---IGYVPQKLYLdttLP-LTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLN 137
Cdd:cd03255 81 rrhIGFVFQSFNL---LPdLTALenvelplLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489125078 138 KPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSHD 180
Cdd:cd03255 158 DPKIILADEPTGNLDsETGKEVM-ELLRELNKEAGTTIVVVTHD 200
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-184 |
3.74e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.18 E-value: 3.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQ-RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR--I 69
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipyLRrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 70 GYVPQ--KLYLDTT------LPLTVsrfMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQL 141
Cdd:COG2884 82 GVVFQdfRLLPDRTvyenvaLPLRV---TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLV 184
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELV 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-212 |
1.05e-38 |
|
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: 134.49 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRIGYVP 73
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QK----------------LYLDTTLPLTVSRFMRLRPGTKkEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLN 137
Cdd:cd03219 82 QIprlfpeltvlenvmvaAQARTGSGLLLARARREEREAR-ERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQgRVIAEGTPDEVRNNPR 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-198 |
1.98e-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: 133.37 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR----VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------LRIGYVPQ 74
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KlylDTTLP-LTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNA-PMQkLSGGETQRVLLARALLNKPQLLVLD 145
Cdd:cd03293 81 Q---DALLPwLTVLdnvalglELQGVPKAEARERAEELLELVGLSGFENAyPHQ-LSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489125078 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHI 198
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI-------DEAVFLADRV 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-196 |
3.43e-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: 132.64 E-value: 3.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------RIGYVPQK 75
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 LYLdttLP-LTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEP 147
Cdd:cd03259 81 YAL---FPhLTVAeniafglKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489125078 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-215 |
1.51e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 132.20 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYVPQKl 76
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelaRRRAVLPQH- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 77 yldTTL--PLTVSRFMRL----RPGTKKED---ILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALL------NKPQL 141
Cdd:PRK13548 85 ---SSLsfPFTVEEVVAMgrapHGLSRAEDdalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVsMHPEFIS 215
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQgRLVADGTPAEV-LTPETLR 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-192 |
2.00e-37 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 137.50 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKL-YLDTT 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQeELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 82 lpLTVSRFMR-LRPGTKKEDILPALKRVQ-AGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVAL 159
Cdd:COG0488 394 --KTVLDELRdGAPGGTEQEVRGYLGRFLfSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
170 180 190
....*....|....*....|....*....|...
gi 489125078 160 YDLIDqlrrELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:COG0488 472 EEALD----DFPGTVLLVSHDRYFLDRVATRIL 500
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-205 |
8.98e-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: 136.05 E-value: 8.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IGY 71
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldedDLRrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYL-DTTLP--LtvsrfmRL-RPGTKKEDILPALKRVQAGHL-------MNAPM----QKLSGGETQRVLLARALL 136
Cdd:COG4987 414 VPQRPHLfDTTLRenL------RLaRPDATDEELWAALERVGLGDWlaalpdgLDTWLgeggRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCL-NHHICCSGAPE 205
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAG-LERMDRILVLeDGRIVEQGTHE 554
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-196 |
1.20e-36 |
|
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: 127.69 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-------------RIGYVP 73
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplrrRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QKLYLDTTLpltvsrfmrlrpgTKKEDIlpalkrvqaghlmnapMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDV 153
Cdd:cd03229 83 QDFALFPHL-------------TVLENI----------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489125078 154 NGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03229 134 ITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-197 |
4.05e-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: 4.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQklyldttlpl 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 tvsrfmrlrpgtkkedilpalkrvqaghlmnapmqkLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLId 164
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL- 113
|
170 180 190
....*....|....*....|....*....|...
gi 489125078 165 qlrRELDCAVLMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:cd03221 114 ---KEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-212 |
1.12e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.50 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL----------RIGYVPQ 74
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnlpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KlYLdttL-P-LTVSR----FMRLRPGTK---KEDILPALKRVQAGHLMNA-PMQkLSGGETQRVLLARALLNKPQLLVL 144
Cdd:COG1118 83 H-YA---LfPhMTVAEniafGLRVRPPSKaeiRARVEELLELVQLEGLADRyPSQ-LSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 145 DEPTQGVDVngQVAlYDLIDQLRR---ELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:COG1118 158 DEPFGALDA--KVR-KELRRWLRRlhdELGGTTVFVTHDQEEALELADRVVVMNQgRIEQVGTPDEVYDRPA 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-196 |
1.63e-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: 133.42 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR--VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGY 71
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpasLRrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLdttLPLTVSRFMRL-RPGTKKEDILPALKRVQAGH-LMNAPM----------QKLSGGETQRVLLARALLNKP 139
Cdd:COG2274 554 VLQDVFL---FSGTIRENITLgDPDATDEEIIEAARLAGLHDfIEALPMgydtvvgeggSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:COG2274 631 RILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDK 684
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-166 |
2.55e-35 |
|
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: 125.00 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGkILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LRIGYVPQ 74
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLyldTTLP-LTVSRFM-------RLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:cd03264 80 EF---GVYPnFTVREFLdyiawlkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180
....*....|....*....|
gi 489125078 147 PTQGVDVNGQVALYDLIDQL 166
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSEL 176
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-191 |
3.41e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 3.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR 68
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLYLdttLP-LTV----------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLN 137
Cdd:COG1129 81 IAIIHQELNL---VPnLSVaeniflgrepRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRV 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-205 |
7.89e-35 |
|
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: 124.08 E-value: 7.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRIGYVP 73
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppherarAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QKLYLDTTLP----LTVSRFMRLRPGTKKE-----DILPALKRvqaghLMNAPMQKLSGGETQRVLLARALLNKPQLLVL 144
Cdd:cd03224 82 EGRRIFPELTveenLLLGAYARRRAKRKARlervyELFPRLKE-----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 145 DEPTQG-----VDVngqvaLYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:cd03224 157 DEPSEGlapkiVEE-----IFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERgRVVLEGTAA 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-196 |
1.79e-34 |
|
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: 123.55 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRI 69
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 70 GYVPQ--KLYLDttlpLTV---------SRFMRLRPGTKKEDIL---PALK---RVQAGHlmnapmqkLSGGETQRVLLA 132
Cdd:COG0410 81 GYVPEgrRIFPS----LTVeenlllgayARRDRAEVRADLERVYelfPRLKerrRQRAGT--------LSGGEQQMLAIG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 133 RALLNKPQLLVLDEPTQG-----VDvngqvALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLER 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-191 |
2.73e-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: 121.00 E-value: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRIGYV 72
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfasprdarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQklyldttlpltvsrfmrlrpgtkkedilpalkrvqaghlmnapmqkLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:cd03216 81 YQ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 489125078 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:cd03216 115 PAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRV 152
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-180 |
2.90e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.64 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTTLPL-- 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 -----------TVSRFMRL--RPGTKKEDILpALKRVQA------------------------GHLMNAPMQKLSGGETQ 127
Cdd:COG0488 81 tvldgdaelraLEAELEELeaKLAEPDEDLE-RLAELQEefealggweaearaeeilsglgfpEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 128 RVLLARALLNKPQLLVLDEPTQGVDVNGqvalydlIDQLRREL---DCAVLMVSHD 180
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLES-------IEWLEEFLknyPGTVLVVSHD 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-222 |
2.90e-34 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 126.88 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYVP 73
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QK--LYLDTTLPLTV--------SRFMRLRPgTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLV 143
Cdd:PRK09536 84 QDtsLSFEFDVRQVVemgrtphrSRFDTWTE-TDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHPEFISMFGQRGA 222
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLaDGRVRAAGPPADVLTADTLRAAFDARTA 241
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-194 |
3.20e-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: 128.56 E-value: 3.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------RIGYV 72
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYLdttLPLTVSRFMRL-RPGTKKEDILPALKRVQAGHLMNAPMQ-----------KLSGGETQRVLLARALLNKPQ 140
Cdd:TIGR02857 402 PQHPFL---FAGTIAENIRLaRPDASDAEIREALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCL 194
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-196 |
3.96e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.24 E-value: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR---- 68
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtalrgraLRrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 -IGYVPQKLYLDTTLP-----LT-----VSRFMRLRPGTKKEDI---LPALKRVQAGHLMNAPMQKLSGGETQRVLLARA 134
Cdd:COG3638 81 rIGMIFQQFNLVPRLSvltnvLAgrlgrTSTWRSLLGLFPPEDReraLEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489125078 135 LLNKPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG3638 161 LVQEPKLILADEPVASLDpKTARQVM-DLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-196 |
5.45e-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: 5.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGYV 72
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltlesLRrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYLdttLPLTVSRFMRL-RPGTKKEDILPALKRVQAGH-LMNAPMQ----------KLSGGETQRVLLARALLNKPQ 140
Cdd:COG1132 420 PQDTFL---FSGTIRENIRYgRPDATDEEVEEAAKAAQAHEfIEALPDGydtvvgergvNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-NADRILVLDD 549
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-217 |
8.55e-34 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 122.06 E-value: 8.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRrVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLRIGYVPQKLY 77
Cdd:cd03299 3 VENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppeKRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 78 LdttLP-LTVSRF----MRLRPGTKKED---ILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:cd03299 82 L---FPhMTVYKNiaygLKKRKVDKKEIerkVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP--EFISMF 217
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNgKLIQVGKPEEVFKKPknEFVAEF 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-196 |
1.27e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVsygqRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRIG 70
Cdd:COG1129 255 VVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVP-----QKLYLD------TTLPL--TVSRFMRLRPGTKKEDILPALKR--VQAGHlMNAPMQKLSGGETQRVLLARAL 135
Cdd:COG1129 331 YVPedrkgEGLVLDlsirenITLASldRLSRGGLLDRRRERALAEEYIKRlrIKTPS-PEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 136 LNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRE 469
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-205 |
1.34e-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: 121.52 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQ-RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG------------QLR--IGY 71
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrQLRrqIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLdtTLPLTV---------------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALL 136
Cdd:cd03256 83 IFQQFNL--IERLSVlenvlsgrlgrrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDgRIVFDGPPA 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-222 |
1.65e-33 |
|
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: 124.06 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 22 DVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------------RIGYVPQklylDTTL-P-L 84
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQ----EARLfPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 TVSR-----FMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVAL 159
Cdd:COG4148 93 SVRGnllygRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 160 YDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFISMFGQRGA 222
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQgRVVASGPLAEVLSRPDLLPLAGGEEA 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-195 |
1.69e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.05 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYG-QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG--------QLRIGYVPQ-- 74
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerRKSIGYVMQdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 --KLYLDTtlpltVSRFMRLR---PGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:cd03226 81 dyQLFTDS-----VREELLLGlkeLDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 150 GVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-148 |
3.64e-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: 117.75 E-value: 3.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYVPQKLYLDTTLP----- 83
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrKEIGYVFQDPQLFPRLTvrenl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 84 LTVSRFMRLRPGTKKEDILPALKRVQAGHLMN----APMQKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-217 |
4.06e-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: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTT--- 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 82 ---LP-LTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQG 150
Cdd:cd03300 81 yalFPhLTVFeniafglRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE--FISMF 217
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKgKIQQIGTPEEIYEEPAnrFVADF 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-205 |
4.66e-33 |
|
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: 119.40 E-value: 4.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEG--------VIKRNGQLR--IGYVPQKLY 77
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPREVRrrIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 78 LDTTLPLTVSRFMRLR----PGTK-KEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:cd03265 84 VDDELTGWENLYIHARlygvPGAErRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489125078 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEGTPE 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-191 |
6.80e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.75 E-value: 6.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR 68
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaiaLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLyldtTL--PLTV--------SRFMRLRPGTKKedilpALKRVQAghLM---------NAPMQKLSGGETQRV 129
Cdd:COG3845 82 IGMVHQHF----MLvpNLTVaenivlglEPTKGGRLDRKA-----ARARIRE--LSerygldvdpDAKVEDLSVGEQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 130 LLARALLNKPQLLVLDEPT-----QGVDvngqvALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:COG3845 151 EILKALYRGARILILDEPTavltpQEAD-----ELFEILRRLAAE-GKSIIFITHKLREVMAIADRV 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-152 |
1.59e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.59 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLvSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR 68
Cdd:COG1137 1 MMTL-EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQ------KlyldttlpLTVSR----FMRLRPGTKKEdilpALKRVQA-------GHLMNAPMQKLSGGETQRVLL 131
Cdd:COG1137 80 IGYLPQeasifrK--------LTVEDnilaVLELRKLSKKE----REERLEElleefgiTHLRKSKAYSLSGGERRRVEI 147
|
170 180
....*....|....*....|.
gi 489125078 132 ARALLNKPQLLVLDEPTQGVD 152
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVD 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-195 |
1.81e-32 |
|
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: 116.55 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYG--QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IGYV 72
Cdd:cd03246 2 EVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnELGdhVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLyldttlpltvsrfmRLRPGTKKEDILpalkrvqaghlmnapmqklSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:cd03246 82 PQDD--------------ELFSGSIAENIL-------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489125078 153 VNGQVALYDLIDQLrRELDCAVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:cd03246 129 VEGERALNQAIAAL-KAAGATRIVIAHRPETL-ASADRILVLE 169
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-182 |
5.53e-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: 116.55 E-value: 5.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LRIGYV--P 73
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkniealRRIGALieA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QKLYLDttlpLTVSRFMRLR---PGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQG 150
Cdd:cd03268 81 PGFYPN----LTARENLRLLarlLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190
....*....|....*....|....*....|..
gi 489125078 151 VDVNGQVALYDLIDQLRRElDCAVLMVSHDLH 182
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLS 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-184 |
6.12e-32 |
|
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: 119.00 E-value: 6.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQR----RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV---AADEGVIKRNGQ---------- 66
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEdllklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 --LR---IGYVPQklylD--TTL-P-LTVSR-----FMRLRPGTKKE---DILPALKRV---QAGHLMNA-PMQkLSGGE 125
Cdd:COG0444 81 rkIRgreIQMIFQ----DpmTSLnPvMTVGDqiaepLRIHGGLSKAEareRAIELLERVglpDPERRLDRyPHE-LSGGM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 126 TQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVV 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-196 |
7.17e-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: 117.05 E-value: 7.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 14 YGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL----------RIGYV-PQKLYLDTTL 82
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkflrRIGVVfGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 PLTVS-----RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQV 157
Cdd:cd03267 111 PVIDSfyllaAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 489125078 158 ALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-182 |
1.13e-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: 116.13 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV-----AADEGVIKRNGQ------------- 66
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 LRIGYVPQKLYLdttLPLTVSRFMRLRP---GTKKEDILP-----ALKRVQAGHLMN--APMQKLSGGETQRVLLARALL 136
Cdd:cd03260 81 RRVGMVFQKPNP---FPGSIYDNVAYGLrlhGIKLKEELDerveeALRKAALWDEVKdrLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDLH 182
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQ 201
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-212 |
2.05e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 118.65 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LRIGYVPQK 75
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 LYL--------DTTLPLTV-SRfmRLRPGTK--KEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVL 144
Cdd:PRK10851 83 YALfrhmtvfdNIAFGLTVlPR--RERPNAAaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQgNIEQAGTPDQVWREPA 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-196 |
2.85e-31 |
|
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: 114.77 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 19 VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----------QLRIGYVPQK--LYLDTTLPLTV 86
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaeaRRRLGFVSDStgLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 87 SRFMRLRpGTKKEDILPALK----RVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDL 162
Cdd:cd03266 100 EYFAGLY-GLKGDELTARLEeladRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190
....*....|....*....|....*....|....
gi 489125078 163 IDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03266 179 IRQL-RALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-195 |
3.90e-31 |
|
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: 115.02 E-value: 3.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR-VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGYV 72
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldsLRraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQklylDTTL-PLTVSRFMRL-RPGTKKEDILPALKRVQ-AGHLMNAPMQ----------KLSGGETQRVLLARALLNKP 139
Cdd:cd03253 81 PQ----DTVLfNDTIGYNIRYgRPDATDEEVIEAAKAAQiHDKIMRFPDGydtivgerglKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLK 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-202 |
4.18e-31 |
|
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: 114.52 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR--VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----------QLRIGYV 72
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYLDTTlpLTV-------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGeTQRVL-LARALLNKPQLLVL 144
Cdd:cd03263 81 PQFDALFDE--LTVrehlrfyARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGG-MKRKLsLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 145 DEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDLHLVmaktdEVLCLNHHICCSG 202
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEA-----EALCDRIAIMSDG 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-224 |
4.71e-31 |
|
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: 115.09 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR-VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IGYV 72
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvELRrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYLdttLP-LTVSRFMRLRP---GTKKEDI------LPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLL 142
Cdd:cd03295 81 IQQIGL---FPhMTVEENIALVPkllKWPKEKIreradeLLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHICCSGAPEVV----------SMHPE 212
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDI-------DEAFRLADRIAIMKNGEIVqvgtpdeilrSPAND 230
|
250
....*....|..
gi 489125078 213 FISMFGQRGAEQ 224
Cdd:cd03295 231 FVAEFVGADRLL 242
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-196 |
1.03e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.33 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTlVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------RIGY 71
Cdd:COG3839 1 MAS-LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQK--LYldttlP-LTVSR---F-MRLRpGTKKEDI----LPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQ 140
Cdd:COG3839 80 VFQSyaLY-----PhMTVYEniaFpLKLR-KVPKAEIdrrvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-217 |
3.51e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.43 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTT 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 82 ------LP-LTVsrF--------MRLRPgtkKEDILP----ALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLL 142
Cdd:PRK09452 92 fqsyalFPhMTV--FenvafglrMQKTP---AAEITPrvmeALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE--FISMF 217
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDgRIEQDGTPREIYEEPKnlFVARF 244
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-214 |
3.80e-30 |
|
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: 113.29 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGqlrigyvpqklyLDTTL 82
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG------------LDTLD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 PLTVsRFMRLRPG-------------TKKEDI--------LP----------ALKRVQAGHLMNAPMQKLSGGETQRVLL 131
Cdd:TIGR04520 69 EENL-WEIRKKVGmvfqnpdnqfvgaTVEDDVafglenlgVPreemrkrvdeALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 132 ARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL-HLVMAktDEVLCLNH-HICCSGAPEVVSM 209
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeEAVLA--DRVIVMNKgKIVAEGTPREIFS 225
|
....*
gi 489125078 210 HPEFI 214
Cdd:TIGR04520 226 QVELL 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-192 |
4.56e-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: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QL--RIGY 71
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreELgrHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQklylDTTL-PLTV----SRFMRLRPgtkkEDILPALKRVQAgHLM------------NAPMQKLSGGETQRVLLARA 134
Cdd:COG4618 411 LPQ----DVELfDGTIaeniARFGDADP----EKVVAAAKLAGV-HEMilrlpdgydtriGEGGARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 135 LLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH--------DLHLVMA--------KTDEVL 192
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHrpsllaavDKLLVLRdgrvqafgPRDEVL 554
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-196 |
5.21e-30 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 111.57 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL--------------R 68
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvnrlrgrqlpllrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQ--KLYLDTTLPLTVSRFMRLRpGTKKEDI----LPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLL 142
Cdd:TIGR02673 81 IGVVFQdfRLLPDRTVYENVALPLEVR-GKKEREIqrrvGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489125078 143 VLDEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-152 |
5.99e-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: 111.98 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRIGYVPQ- 74
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlpmherarLGIGYLPQe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 -----KLYLDTTLPLTVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:TIGR04406 85 asifrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
...
gi 489125078 150 GVD 152
Cdd:TIGR04406 165 GVD 167
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-152 |
6.50e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.16 E-value: 6.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK----------RNGQLRIGY 71
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLDTTLP-----LTVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:PRK13536 119 VPQFDNLDLEFTvrenlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
....*.
gi 489125078 147 PTQGVD 152
Cdd:PRK13536 199 PTTGLD 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-179 |
8.22e-30 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.83 E-value: 8.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSV-SYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYL-DTTL 82
Cdd:COG4178 363 LALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLpLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 ------PLTVSRFmrlrpgtKKEDILPALKRVQAGHLmnAPM--------QKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:COG4178 443 reallyPATAEAF-------SDAELREALEAVGLGHL--AERldeeadwdQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|..
gi 489125078 149 QGVDVNGQVALYDLidqLRREL-DCAVLMVSH 179
Cdd:COG4178 514 SALDEENEAALYQL---LREELpGTTVISVGH 542
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-211 |
1.07e-29 |
|
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: 111.28 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LRIGYVPQK 75
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqeRNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 --LYLDTTLPLTVSRFMRLRPG-------TKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:cd03296 83 yaLFRHMTVFDNVAFGLRVKPRserppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP 211
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKgRIEQVGTPDEVYDHP 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-196 |
1.40e-29 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 112.48 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 14 YGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEG--------VIKRNGQLR--IGYVPQKLYLDTTLP 83
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGtarvagydVVREPRKVRrsIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 -----LTVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVA 158
Cdd:TIGR01188 83 grenlEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 489125078 159 LYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:TIGR01188 163 IWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDH 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-196 |
2.10e-29 |
|
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: 108.67 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVsygqRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRIG 70
Cdd:cd03215 3 PVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPqklyldttlpltvsrfmrlrpgtkkEDilpalkRVQAGHLMNAPM-------QKLSGGETQRVLLARALLNKPQLLV 143
Cdd:cd03215 79 YVP-------------------------ED------RKREGLVLDLSVaenialsSLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489125078 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYE 179
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-214 |
4.34e-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: 110.62 E-value: 4.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYG-----QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG------------QL 67
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrditakkkkklkDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 R--IGYVPQ----KLYLDTTL------PltvsrfMRLrpGTKKEDilpALKRVQ-AGHLMNAPMQ-------KLSGGETQ 127
Cdd:TIGR04521 81 RkkVGLVFQfpehQLFEETVYkdiafgP------KNL--GLSEEE---AEERVKeALELVGLDEEylerspfELSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 128 RVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEV 206
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDGTPRE 229
|
....*...
gi 489125078 207 VSMHPEFI 214
Cdd:TIGR04521 230 VFSDVDEL 237
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-196 |
4.70e-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: 108.88 E-value: 4.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQlRIGYVPQK--------- 75
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-DVTDLPPKdrdiamvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 ---LYLDTTLPLTVSRFMRLRpGTKKEDILPALKRV----QAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:cd03301 80 nyaLYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVaellQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489125078 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-194 |
8.19e-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: 108.09 E-value: 8.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------------RIGY 71
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtpplnskkaskfrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYL--DTT------LPLtvsRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLV 143
Cdd:TIGR03608 81 LFQNFALieNETveenldLGL---KYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489125078 144 LDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLhLVMAKTDEVLCL 194
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-152 |
1.03e-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: 108.40 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRIGYV 72
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQK--LYLDTTLPLTVSRFMRLRPGTKKE--DILPA-LKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEP 147
Cdd:cd03218 81 PQEasIFRKLTVEENILAVLEIRGLSKKEreEKLEElLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
....*
gi 489125078 148 TQGVD 152
Cdd:cd03218 161 FAGVD 165
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-152 |
1.58e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.89 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK----------RNGQLRIG 70
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKLYLDTTLP-----LTVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLD 145
Cdd:PRK13537 84 VVPQFDNLDPDFTvrenlLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
....*..
gi 489125078 146 EPTQGVD 152
Cdd:PRK13537 164 EPTTGLD 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-181 |
1.64e-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: 112.84 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG-----------QLRIGYVPQ 74
Cdd:TIGR02868 337 LRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYLDTTlplTVSRFMRL-RPGTKKEDILPALKRVQAGHL-------MNAPMQ----KLSGGETQRVLLARALLNKPQLL 142
Cdd:TIGR02868 417 DAHLFDT---TVRENLRLaRPDATDEELWAALERVGLADWlralpdgLDTVLGeggaRLSGGERQRLALARALLADAPIL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489125078 143 VLDEPTQGVDVNGQVALY-DLIDQLRREldcAVLMVSHDL 181
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLeDLLAALSGR---TVVLITHHL 530
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-230 |
3.81e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.81 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEG--------VIKRNGQLR-IGYVPQK 75
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedVTHRSIQQRdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 --LYLDTTLPLTVSRFMRLRpGTKKEDIL----PALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:PRK11432 87 yaLFPHMSLGENVGYGLKML-GVPKEERKqrvkEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP--EFISMF--------G 218
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKgKIMQIGSPQELYRQPasRFMASFmgdanifpA 245
|
250
....*....|..
gi 489125078 219 QRGAEQLGIYRH 230
Cdd:PRK11432 246 TLSGDYVDIYGY 257
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-196 |
5.89e-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: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGYV 72
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrksLRsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYLdttLPLTVSRFMRL-RPGTKKEDILPALKRVQAGHL-MNAPM----------QKLSGGETQRVLLARALLNKPQ 140
Cdd:cd03254 83 LQDTFL---FSGTIMENIRLgRPNATDEEVIEAAKEAGAHDFiMKLPNgydtvlgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIK-NADKILVLDD 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-192 |
6.47e-28 |
|
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: 105.84 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 22 DVSLELrPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------------RIGYVPQKLYLdttLP-LT 85
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQYAL---FPhLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 86 VSR-----FMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALY 160
Cdd:cd03297 92 VREnlafgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|..
gi 489125078 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-216 |
1.05e-27 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 106.08 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSygqRRvLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAdEGVIKRNGQLRIGYVPQKL-----YL-- 78
Cdd:COG4138 2 QLNDVAVA---GR-LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELarhraYLsq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 --DTTLPLTVSRFMRL-RPGTKKEDILPAL-----KRVQAGHLMNAPMQKLSGGETQRVLLARALLN-------KPQLLV 143
Cdd:COG4138 77 qqSPPFAMPVFQYLALhQPAGASSEAVEQLlaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 144 LDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVsMHPEFISM 216
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEV-MTPENLSE 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-196 |
1.41e-27 |
|
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: 105.36 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRR----VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK--------------RNG 65
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 QLRIGYVPQ--------KLYLDTTLPLTVSRFMRLRpgtKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLN 137
Cdd:cd03258 81 RRRIGMIFQhfnllssrTVFENVALPLEIAGVPKAE---IEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-212 |
2.99e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYVPQK 75
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlaRRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 LyldtTLP--LTV--------SRFMRL--RPGTKKEDILP-ALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLL 142
Cdd:PRK11231 85 H----LTPegITVrelvaygrSPWLSLwgRLSAEDNARVNqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL--------HLVMAKTDEVLclnhhicCSGAPEVVsMHPE 212
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLnqasrycdHLVVLANGHVM-------AQGTPEEV-MTPG 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-181 |
8.95e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.30 E-value: 8.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRRVlsDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK-----LYLDTT 81
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvsmLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 82 L--PLTVSRFMRL--RPGTK-----KEDILPALKRVQ-AGHLMNAPMQkLSGGETQRVLLARALLNKPQLLVLDEPTQGV 151
Cdd:COG3840 82 LfpHLTVAQNIGLglRPGLKltaeqRAQVEQALERVGlAGLLDRLPGQ-LSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190
....*....|....*....|....*....|
gi 489125078 152 DVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDP 190
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-179 |
9.08e-27 |
|
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: 101.46 E-value: 9.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVL-SDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLdttlP 83
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 ltvsrfmrlrPGTKKEDILPALKRVqaghlmnapmqkLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLI 163
Cdd:cd03223 77 ----------LGTLREQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170
....*....|....*.
gi 489125078 164 dqlrRELDCAVLMVSH 179
Cdd:cd03223 135 ----KELGITVISVGH 146
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-210 |
1.09e-26 |
|
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: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYG-QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ--------------LRIGYV 72
Cdd:TIGR02315 5 ENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklrRRIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYL-----------------DTTLPLTVSRFmrlrPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARAL 135
Cdd:TIGR02315 85 FQHYNLierltvlenvlhgrlgyKPTWRSLLGRF----SEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 136 LNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMH 210
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAgEIVFDGAPSELDDE 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-183 |
1.36e-26 |
|
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: 102.90 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRR----VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------- 66
Cdd:COG4181 6 APIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 -LR---IGYVPQKLYLDTTL--------PLTVSRFMRLRPGTKKEdilpaLKRVQAGHLMNA-PMQkLSGGETQRVLLAR 133
Cdd:COG4181 86 rLRarhVGFVFQSFQLLPTLtalenvmlPLELAGRRDARARARAL-----LERVGLGHRLDHyPAQ-LSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489125078 134 ALLNKPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSHDLHL 183
Cdd:COG4181 160 AFATEPAILFADEPTGNLDaATGEQII-DLLFELNRERGTTLVLVTHDPAL 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-180 |
2.73e-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: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAD---EGVIKRNGQL---------RIGYVP 73
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRltalpaeqrRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 Q------------KLYLDttLPLTVSRfmrlrpGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQL 141
Cdd:COG4136 83 QddllfphlsvgeNLAFA--LPPTIGR------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 142 LVLDEPTQGVDVngqvalyDLIDQLR-------RELDCAVLMVSHD 180
Cdd:COG4136 155 LLLDEPFSKLDA-------ALRAQFRefvfeqiRQRGIPALLVTHD 193
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-184 |
3.83e-26 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 106.43 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSYGqrrvlsDVSL-----ELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIkrNGQLRIGYVPQklY 77
Cdd:PRK13409 339 TLVEYPDLTKKLG------DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQ--Y 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 78 LDTTLPLTVSRFMRLRPGT-----KKEDILpalKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:PRK13409 409 IKPDYDGTVEDLLRSITDDlgssyYKSEII---KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180 190
....*....|....*....|....*....|..
gi 489125078 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALVVDHDIYMI 517
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-195 |
5.62e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.40 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL----------- 67
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 RIGYV---PQKLYLDTTLPLTVSrFMRLRPGTKKEDILP----ALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQ 140
Cdd:PRK13635 82 QVGMVfqnPDNQFVGATVQDDVA-FGLENIGVPREEMVErvdqALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMN 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-250 |
6.35e-26 |
|
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: 103.65 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 22 DVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------------RIGYVPQKLYLDTTLplTV 86
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQEARLFPHL--SV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 87 SRfmRLRPGTKKEDilPALKRVQ---------AGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQV 157
Cdd:TIGR02142 93 RG--NLRYGMKRAR--PSERRISferviellgIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 158 ALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHPEFISM-FGQRGAEQLGIYRHNHNHR 235
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAGPIAEVWASPDLPWLaREDQGSLIEGVVAEHDQHY 248
|
250
....*....|....*
gi 489125078 236 HDLQgrivLRRGNGH 250
Cdd:TIGR02142 249 GLTA----LRLGGGH 259
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-207 |
1.06e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 100.74 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSlENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVI---------------KRNG 65
Cdd:PRK10895 1 MATLTA-KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplharARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 qlrIGYVPQ------KLYLDTTLPLTVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKP 139
Cdd:PRK10895 80 ---IGYLPQeasifrRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVV 207
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEI 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-184 |
2.08e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.08 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQR----RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--- 68
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalsereLRaar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 --IGYVPQKLYLDTT--------LPLTVSrfmrlrpGTKKEDI----LPALKRVQAGHLMNA-PMQkLSGGETQRVLLAR 133
Cdd:COG1135 82 rkIGMIFQHFNLLSSrtvaenvaLPLEIA-------GVPKAEIrkrvAELLELVGLSDKADAyPSQ-LSGGQKQRVGIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVV 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-184 |
2.51e-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: 104.10 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSYGQRRvLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIkrNGQLRIGYVPQklYLDTTL 82
Cdd:COG1245 340 TLVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQ--YISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 PLTVSRFMRLRPGTK------KEDILpalKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQ 156
Cdd:COG1245 415 DGTVEEFLRSANTDDfgssyyKTEII---KPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180
....*....|....*....|....*...
gi 489125078 157 VALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:COG1245 492 LAVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-197 |
6.41e-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: 98.28 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY-----GQRR--VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEG--VIKRNGQ----- 66
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsiLVRHDGGwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 ---------LR---IGYVPQklyldttlpltvsrFMRLRPGTKKEDIL--PALK--------RVQAGHL---MNAPmQKL 121
Cdd:COG4778 81 qaspreilaLRrrtIGYVSQ--------------FLRVIPRVSALDVVaePLLErgvdreeaRARARELlarLNLP-ERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 122 --------SGGETQRVLLARALLNKPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:COG4778 146 wdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDaANRAVVV-ELIEEAKAR-GTAIIGIFHDEEVREAVADRVV 223
|
....*
gi 489125078 193 CLNHH 197
Cdd:COG4778 224 DVTPF 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-196 |
6.77e-25 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 98.46 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYG--QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IGY 71
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaSLRrqIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLDTTlplTVSRFMRL-RPGTKKEDILPALKRVQAgH--LMNAPMQ----------KLSGGETQRVLLARALLNK 138
Cdd:cd03251 81 VSQDVFLFND---TVAENIAYgRPGATREEVEEAARAANA-HefIMELPEGydtvigergvKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIE-NADRIVVLED 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-148 |
7.36e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.53 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-------------RIG 70
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltdskkdinklrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQK--LY-----LD-TTLPLTVSRfmrlrpGTKKEDI----LPALKRVQAGHLMNA-PMQkLSGGETQRVLLARALLN 137
Cdd:COG1126 81 MVFQQfnLFphltvLEnVTLAPIKVK------KMSKAEAeeraMELLERVGLADKADAyPAQ-LSGGQQQRVAIARALAM 153
|
170
....*....|.
gi 489125078 138 KPQLLVLDEPT 148
Cdd:COG1126 154 EPKVMLFDEPT 164
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-179 |
8.09e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.64 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ--------LRIGYVPQKLYLD 79
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaEACHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 80 TTlpLTVS---RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQ 156
Cdd:PRK13539 86 PA--LTVAenlEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|...
gi 489125078 157 VALYDLIdQLRRELDCAVLMVSH 179
Cdd:PRK13539 164 ALFAELI-RAHLAQGGIVIAATH 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
7-215 |
1.11e-24 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 98.08 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVsyGQRrvLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAdEGVIKRNGQLRIGYVPQKL-----YL--D 79
Cdd:PRK03695 3 LNDVAV--STR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELarhraYLsqQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 80 TTLPLTVSRF----MRLRPGTKKEDILPALKRV----QAGHLMNAPMQKLSGGETQRVLLARALL-----NKP--QLLVL 144
Cdd:PRK03695 78 QTPPFAMPVFqyltLHQPDKTRTEAVASALNEVaealGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 145 DEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLNHHIC-CSGAPEVVsMHPEFIS 215
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLlASGRRDEV-LTPENLA 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-192 |
1.35e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.21 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGvikrngQLRIGYVPQKLYLDTTl 82
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------ELLAGTAPLAEAREDT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 pltvsRFM----RLRP-------------GTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLD 145
Cdd:PRK11247 84 -----RLMfqdaRLLPwkkvidnvglglkGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489125078 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-191 |
1.36e-24 |
|
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: 101.68 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQ----RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL----VAADEGVIKRNGQ------ 66
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQdllgls 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 ---LR------IGYV---PQklyldTTL-PL-TVSRFM--------RLRPGTKKEDILPALKRVQ---AGHLMNA-PMQk 120
Cdd:COG4172 83 ereLRrirgnrIAMIfqePM-----TSLnPLhTIGKQIaevlrlhrGLSGAAARARALELLERVGipdPERRLDAyPHQ- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489125078 121 LSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV--MAktDEV 191
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVrrFA--DRV 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-181 |
2.67e-24 |
|
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: 96.44 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LR--IGY 71
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkknineLRqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYL--------DTTLPLTVSRFMrlrpgTKKEDI---LPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQ 140
Cdd:cd03262 81 VFQQFNLfphltvleNITLAPIKVKGM-----SKAEAEeraLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489125078 141 LLVLDEPTQGVD--VNGQValYDLIDQLRRElDCAVLMVSHDL 181
Cdd:cd03262 156 VMLFDEPTSALDpeLVGEV--LDVMKDLAEE-GMTMVVVTHEM 195
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-181 |
3.13e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 97.30 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK---RNGQLRI-------- 69
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRDlyalseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 70 ---------GYVPQklYLDTTLPLTVS-------RFMRL---RPGTKKEDILPALKRVQ--AGHLMNAPMQkLSGGETQR 128
Cdd:PRK11701 83 rrrllrtewGFVHQ--HPRDGLRMQVSaggnigeRLMAVgarHYGDIRATAGDWLERVEidAARIDDLPTT-FSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489125078 129 VLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDL 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-192 |
4.48e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLvSLENVSVSYG----QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQlRI------- 69
Cdd:COG4525 1 MSML-TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-PVtgpgadr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 70 GYVPQKlylDTTLP-LTVS-------RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQL 141
Cdd:COG4525 79 GVVFQK---DALLPwLNVLdnvafglRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLH--LVMAkTDEVL 192
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEeaLFLA-TRLVV 207
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-191 |
4.91e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 100.24 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK----LYLD 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqlefLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 80 TTlPLtvSRFMRLRPGTKKEDILPALKRVQ-AGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVA 158
Cdd:PRK10636 392 ES-PL--QHLARLAPQELEQKLRDYLGGFGfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
170 180 190
....*....|....*....|....*....|....
gi 489125078 159 LYD-LIDqlrreLDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK10636 469 LTEaLID-----FEGALVVVSHDRHLLRSTTDDL 497
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-179 |
5.15e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 95.73 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----QL-------RIGY 71
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirQLdpadlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYL-DTTLP--LTVSRfmrlrPGTKKEDILPALKRVQAGHLMNA-PM----------QKLSGGETQRVLLARALLN 137
Cdd:cd03245 83 VPQDVTLfYGTLRdnITLGA-----PLADDERILRAAELAGVTDFVNKhPNgldlqigergRGLSGGQRQAVALARALLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVAlydLIDQLRREL-DCAVLMVSH 179
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEER---LKERLRQLLgDKTLIIITH 197
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-148 |
8.83e-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: 99.51 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR-VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGYV 72
Cdd:COG5265 358 VRFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdvtqasLRaaIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQklylDTTLpltvsrF-------MRL-RPGTKKEDILPALKRVQAGHL-MNAPMQ----------KLSGGETQRVLLAR 133
Cdd:COG5265 438 PQ----DTVL------FndtiaynIAYgRPDASEEEVEAAARAAQIHDFiESLPDGydtrvgerglKLSGGEKQRVAIAR 507
|
170
....*....|....*
gi 489125078 134 ALLNKPQLLVLDEPT 148
Cdd:COG5265 508 TLLKNPPILIFDEAT 522
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-194 |
9.18e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 93.92 E-value: 9.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR--VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG--------QLR--IGYV 72
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekALSslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYL-DTTLpltvsrfmrlrpgtkkedilpalkrvqaghlMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGV 151
Cdd:cd03247 81 NQRPYLfDTTL-------------------------------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489125078 152 DVNGQVALYDLI-DQLRrelDCAVLMVSHdlHLV-MAKTDEVLCL 194
Cdd:cd03247 130 DPITERQLLSLIfEVLK---DKTLIWITH--HLTgIEHMDKILFL 169
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-196 |
9.79e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.08 E-value: 9.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 14 YGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGqlrigYVPQK------------------ 75
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPFKrrkefarrigvvfgqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 LYLDttLPLTVSrFMRLR-----PgtkKEDILPALKRV----QAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:COG4586 107 LWWD--LPAIDS-FRLLKaiyriP---DAEYKKRLDELvellDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489125078 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-199 |
1.27e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.01 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQ----RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL-----VAADEGVIKRNGQL----- 67
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESllhas 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 ----------RIGYVPQK----LYLDTTLPLTVSRFMRLRPGTKKE----DILPALKRV----QAGHLMNAPMQkLSGGE 125
Cdd:PRK15134 83 eqtlrgvrgnKIAMIFQEpmvsLNPLHTLEKQLYEVLSLHRGMRREaargEILNCLDRVgirqAAKRLTDYPHQ-LSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 126 TQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHIC 199
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-192 |
1.62e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.58 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 21 SDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LRIG--YVPQK-----LYLDTTLP 83
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKeinalstaqrLARGlvYLPEDrqssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 LTVSRFMRLRPG----TKKED-ILPALKR---VQAGHLmNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNG 155
Cdd:PRK15439 360 WNVCALTHNRRGfwikPARENaVLERYRRalnIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190
....*....|....*....|....*....|....*..
gi 489125078 156 QVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVL 474
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-214 |
3.05e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.67 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LRIG 70
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpghqiARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQ----KLYLDTTL--PLTVSRFMRLRPG-------------TKKEDILPA---LKRVQAGHLMNAPMQKLSGGETQR 128
Cdd:PRK11300 82 VVRTfqhvRLFREMTVieNLLVAQHQQLKTGlfsgllktpafrrAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 129 VLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHI-CCSGAPEVV 207
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTpLANGTPEEI 241
|
....*..
gi 489125078 208 SMHPEFI 214
Cdd:PRK11300 242 RNNPDVI 248
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-184 |
3.86e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.75 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSY---------GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG------- 65
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplakln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 ---------------QLRIGYV-PQKlyldtTLPLTVSRFMR----LRPGTKKEDILPALKRVQ--AGHLMNAPMQkLSG 123
Cdd:PRK10419 81 raqrkafrrdiqmvfQDSISAVnPRK-----TVREIIREPLRhllsLDKAERLARASEMLRAVDldDSVLDKRPPQ-LSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 124 GETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLV 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-152 |
4.64e-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: 92.61 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 11 SVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV--AADEGVIKRNGQ--------LRIGYVPQKlylDT 80
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRpldkrsfrKIIGYVPQD---DI 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489125078 81 TLP-LTVSRFMRlrpgtkkedilpalkrvqaghlMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:cd03213 93 LHPtLTVRETLM----------------------FAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-169 |
5.32e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.50 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLvrvvLGLVAadeGVIK-RNGQL---------------- 67
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIA---GARKiQQGRVevlggdmadarhrrav 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 --RIGYVPQ----KLYLDttlpLTVSR----FMRLRPGTKKEdilpalKRVQAGHLMNA---------PMQKLSGGETQR 128
Cdd:NF033858 75 cpRIAYMPQglgkNLYPT----LSVFEnldfFGRLFGQDAAE------RRRRIDELLRAtglapfadrPAGKLSGGMKQK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489125078 129 VLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-194 |
5.57e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSV-SYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LRI 69
Cdd:COG3845 256 VVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 70 GYVP---QKLYLDTTLPLT------------VSRFMRLRPGTKKEDILPALKR--VQAGHLmNAPMQKLSGGETQRVLLA 132
Cdd:COG3845 336 AYIPedrLGRGLVPDMSVAenlilgryrrppFSRGGFLDRKAIRAFAEELIEEfdVRTPGP-DTPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 133 RALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLhlvmaktDEVLCL 194
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDL-------DEILAL 468
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-166 |
6.39e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVI---------------KRNGQLR- 68
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqfdfsqkpseKAIRLLRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 -IGYVPQKLYLdttLP-LTVSRF-----MRLRPGTKKEDILPA---LKRVQAGHLMNAPMQKLSGGETQRVLLARALLNK 138
Cdd:COG4161 83 kVGMVFQQYNL---WPhLTVMENlieapCKVLGLSKEQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190
....*....|....*....|....*....|
gi 489125078 139 PQLLVLDEPTQGVD--VNGQVAlyDLIDQL 166
Cdd:COG4161 160 PQVLLFDEPTAALDpeITAQVV--EIIREL 187
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
6.64e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYG--QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR-- 68
Cdd:PRK13632 5 SVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkEIRkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYV---PQKLYLDTTLPLTVSrF----MRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQL 141
Cdd:PRK13632 85 IGIIfqnPDNQFIGATVEDDIA-FglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMaKTDEVLCLNH-HICCSGAPEVVSMHPEFI 214
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgKLIAQGKPKEILNNKEIL 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-181 |
7.45e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.23 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVR-------------VVLGLVAADEGVIKRNGQLRIG 70
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKLYL---DTTLPLTVSRFMRLRpGTKKEDI----LPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLV 143
Cdd:PRK09493 81 MVFQQFYLfphLTALENVMFGPLRVR-GASKEEAekqaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 489125078 144 LDEPTQGVDvngqvalydliDQLRREldcaVLMVSHDL 181
Cdd:PRK09493 160 FDEPTSALD-----------PELRHE----VLKVMQDL 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-152 |
8.19e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRvVLGLVAadegvIKRNGQLRI--------------- 69
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLE-----MPRSGTLNIagnhfdfsktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 70 --------GYVPQKLYLdttLP-LTVSRF-----MRLRPGTKKEDILPA---LKRVQAGHLMNA-PMQkLSGGETQRVLL 131
Cdd:PRK11124 77 irelrrnvGMVFQQYNL---WPhLTVQQNlieapCRVLGLSKDQALARAeklLERLRLKPYADRfPLH-LSGGQQQRVAI 152
|
170 180
....*....|....*....|.
gi 489125078 132 ARALLNKPQLLVLDEPTQGVD 152
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALD 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-207 |
1.42e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY----------------------GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADE 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 59 GVIKRNGqlRI--------GYVPQklyldttlpLT-------VSRFMrlrpGTKKEDILPALKRVQA----GHLMNAPMQ 119
Cdd:COG1134 81 GRVEVNG--RVsallelgaGFHPE---------LTgreniylNGRLL----GLSRKEIDEKFDEIVEfaelGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 120 KLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HI 198
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKgRL 224
|
....*....
gi 489125078 199 CCSGAPEVV 207
Cdd:COG1134 225 VMDGDPEEV 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-192 |
1.91e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.02 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 22 DVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAD---EGVIKRNGQlRIGYVPQK------------LYLDttlPLT- 85
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGR-EILNLPEKelnklraeqismIFQD---PMTs 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 86 VSRFMR----------LRPGTKKED-------ILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:PRK09473 110 LNPYMRvgeqlmevlmLHKGMSKAEafeesvrMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489125078 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-192 |
2.06e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.38 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 17 RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL-VAADEGVIKRNGQ------------LRIGYVPQKLYLDTTLP 83
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKpvkirnpqqaiaQGIAMVPEDRKRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 L-------------TVSRFMRLRPGTKKEDILPALKR--VQAGHLMnAPMQKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:PRK13549 355 VmgvgknitlaaldRFTGGSRIDDAAELKTILESIQRlkVKTASPE-LAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489125078 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVL 476
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-197 |
2.07e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK------ 75
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrqqvs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 -------LYLDTT-----LPLTVSRfmrLRPGTKKedILPALKRVQ-AGHLMNAPMQKLSGGETQRVLLARALLNKPQLL 142
Cdd:PRK10247 85 ycaqtptLFGDTVydnliFPWQIRN---QQPDPAI--FLDDLERFAlPDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLNHH 197
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQPH 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-165 |
2.12e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.88 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----QLRIGYVPQKLYL--- 78
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaEQRDEPHENILYLghl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 DTTLP-LTVS---RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVN 154
Cdd:TIGR01189 82 PGLKPeLSALenlHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170
....*....|.
gi 489125078 155 GQVALYDLIDQ 165
Cdd:TIGR01189 162 GVALLAGLLRA 172
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-194 |
2.17e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 92.20 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK---RNGQLRIGYV---PQKLY 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimRSGAELELYQlseAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 78 LDTT------------LPLTVS-------RFMRL---RPGTKKEDILPALKRVQ--AGHLMNAPMQkLSGGETQRVLLAR 133
Cdd:TIGR02323 83 LMRTewgfvhqnprdgLRMRVSaganigeRLMAIgarHYGNIRATAQDWLEEVEidPTRIDDLPRA-FSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-179 |
2.48e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 91.56 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 17 RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV---AADEGVIKRNGQLR--------IGYVPQklyLDTTLP-L 84
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRkpdqfqkcVAYVRQ---DDILLPgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 TVSRF------MRLR-----PGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDv 153
Cdd:cd03234 97 TVRETltytaiLRLPrkssdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD- 175
|
170 180
....*....|....*....|....*...
gi 489125078 154 ngQVALYDLIDQLRR--ELDCAVLMVSH 179
Cdd:cd03234 176 --SFTALNLVSTLSQlaRRNRIVILTIH 201
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-196 |
2.80e-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: 91.40 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGY 71
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiglhdLRsrISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKlyldttlPLTVSRFMR--LRPGTKKED--ILPALKRVQ-AGHLMNAPMQK----------LSGGETQRVLLARALL 136
Cdd:cd03244 83 IPQD-------PVLFSGTIRsnLDPFGEYSDeeLWQALERVGlKEFVESLPGGLdtvveeggenLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIdqlRREL-DCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTI---REAFkDCTVLTIAHRLDTII-DSDRILVLDK 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-215 |
3.38e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.68 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGqLRIGYVPQKLY------- 77
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG-LDVATTPSRELakrlail 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 78 ---LDTTLPLTVS------RFmrlrPGTK----KED---ILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQL 141
Cdd:COG4604 81 rqeNHINSRLTVRelvafgRF----PYSKgrltAEDreiIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVsMHPEFIS 215
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEI-ITPEVLS 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-195 |
4.73e-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: 91.79 E-value: 4.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSY---------GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG-------- 65
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 --------------QLRIGYVPQKLYLDTTLPLTVSRFMRLRPGTKKEDILPALKRV--QAGHLMNAPMQkLSGGETQRV 129
Cdd:TIGR02769 81 kqrrafrrdvqlvfQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVglRSEDADKLPRQ-LSGGQLQRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 130 LLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMD 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-205 |
4.90e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.87 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----LR---IGY 71
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqaLQknlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLDTTLPLTVSR-----------FMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQ 140
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDvvmmgryghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAPE 205
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-182 |
7.62e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.87 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVV---LGLV--AADEGVIKRNGQ--------- 66
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIpgARVEGEILLDGEdiydpdvdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 --LR--IGYVPQKLyldTTLPLTV-------SRFMRLRPGTKKEDILP-ALKRVqagHL-------MNAPMQKLSGGETQ 127
Cdd:COG1117 88 veLRrrVGMVFQKP---NPFPKSIydnvaygLRLHGIKSKSELDEIVEeSLRKA---ALwdevkdrLKKSALGLSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 128 RVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLH 182
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNMQ 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-196 |
1.04e-21 |
|
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: 93.60 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRR-----------VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAdEGVIKRNGQ---- 66
Cdd:COG4172 273 PPLLEARDLKVWFPIKRglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQdldg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 --------LR--IGYVPQKLY--LDttlP-LTVSRF----MRL-RPGTKKED----ILPALKRVqagHLMNAPMQK---- 120
Cdd:COG4172 352 lsrralrpLRrrMQVVFQDPFgsLS---PrMTVGQIiaegLRVhGPGLSAAErrarVAEALEEV---GLDPAARHRyphe 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 121 LSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKD 501
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-194 |
1.17e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 89.84 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQR---RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYvpQKLYLDT 80
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--EHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 81 TLPLtVSRFMRLRPGTKKEDILPALKRVQAGHLMNAP-----------MQK------------LSGGETQRVLLARALLN 137
Cdd:cd03248 89 KVSL-VGQEPVLFARSLQDNIAYGLQSCSFECVKEAAqkahahsfiseLASgydtevgekgsqLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCL 194
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTV-ERADQILVL 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-220 |
1.31e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYVPQKL 76
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 77 YL--DTTLPLTVSR--------FMRLRpgtkKED---ILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLV 143
Cdd:PRK10253 91 TTpgDITVQELVARgryphqplFTRWR----KEDeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAP-EVVSmhPEFIS-MFGQR 220
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREgKIVAQGAPkEIVT--AELIErIYGLR 244
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-196 |
1.59e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.01 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQlRIGYVPQK--------- 75
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-RMNDVPPAergvgmvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 ---LYLDTTLPLTVSRFMRLrPGTKKEDILpalKRV-------QAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLD 145
Cdd:PRK11000 83 syaLYPHLSVAENMSFGLKL-AGAKKEEIN---QRVnqvaevlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489125078 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-196 |
1.68e-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: 93.27 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYG-QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IGYV 72
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhTLRqfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQKLYLDTTLPLTvSRFMRLRPGTKKEDILPALKRVQ-AGHLMNAPM----------QKLSGGETQRVLLARALLNKPQL 141
Cdd:TIGR01193 554 PQEPYIFSGSILE-NLLLGAKENVSQDEIWAACEIAEiKDDIENMPLgyqtelseegSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 142 LVLDEPTQGVDVngqVALYDLIDQLRRELDCAVLMVSHDLHlVMAKTDEVLCLNH 196
Cdd:TIGR01193 633 LILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLDH 683
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-207 |
1.77e-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: 88.74 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL--VAADEGVIKRNGQL----------RIGyvp 73
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdlppeeraRLG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 qkLYLDTTLPLTVsrfmrlrPGTKKEDILpalKRVQAGhlmnapmqkLSGGETQRVLLARALLNKPQLLVLDEPTQGVDV 153
Cdd:cd03217 79 --IFLAFQYPPEI-------PGVKNADFL---RYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 154 NGQVALYDLIDQLRRElDCAVLMVSHDLH-LVMAKTDEV-LCLNHHICCSGAPEVV 207
Cdd:cd03217 138 DALRLVAEVINKLREE-GKSVLIITHYQRlLDYIKPDRVhVLYDGRIVKSGDKELA 192
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-183 |
1.95e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.71 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----LRIGYVPQKLYL- 78
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrQRDEYHQDLLYLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 -----DTTL-PLTVSRF-MRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGV 151
Cdd:PRK13538 81 hqpgiKTELtALENLRFyQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489125078 152 DVNGqVAlyDLIDQLRRELD---CAVLMVSHDLHL 183
Cdd:PRK13538 161 DKQG-VA--RLEALLAQHAEqggMVILTTHQDLPV 192
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-192 |
2.48e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.37 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------LRIGYVPQKly 77
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgAERGVVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 78 lDTTLPL-----TVSRFMRLRPGTKKEDILPA---LKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:PRK11248 79 -EGLLPWrnvqdNVAFGLQLAGVEKMQRLEIAhqmLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489125078 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDL-HLVMAKTDEVL 192
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIeEAVFMATELVL 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-179 |
2.81e-21 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 92.00 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLG-----------LVAADEGV------IKRNgq 66
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGSgetiwdIKKH-- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 lrIGYVPQKLYLDTTLPLTV-----SRFM-----------RLRPGTKKE-DILPALKRvqaghLMNAPMQKLSGGETQRV 129
Cdd:PRK10938 338 --IGYVSSSLHLDYRVSTSVrnvilSGFFdsigiyqavsdRQQKLAQQWlDILGIDKR-----TADAPFHSLSWGQQRLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489125078 130 LLARALLNKPQLLVLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSH 179
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDpLNRQLVR-RFVDVLISEGETQLLFVSH 460
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-195 |
3.45e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR-- 68
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpfLRrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQ--------KLYLDTTLPLTVSrfmrlrpGTKKEDILpalKRVQAG--------HLMNAPMQkLSGGETQRVLLA 132
Cdd:PRK10908 81 IGMIFQdhhllmdrTVYDNVAIPLIIA-------GASGDDIR---RRVSAAldkvglldKAKNFPIQ-LSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489125078 133 RALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLS 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-196 |
5.34e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 91.71 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQR---RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----QLRIGYVP 73
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvQYDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QKLYLDTTLPLTVSrfmrlrpGTKKEDILPALKRVQAGHLMNAPMQ-----------------------KLSGGETQRVL 130
Cdd:TIGR00958 555 RQVALVGQEPVLFS-------GSVRENIAYGLTDTPDEEIMAAAKAanahdfimefpngydtevgekgsQLSGGQKQRIA 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 131 LARALLNKPQLLVLDEPTQGVDVNGQVALYdlidQLRRELDCAVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQ----ESRSRASRTVLLIAHRLSTV-ERADQILVLKK 688
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-179 |
5.66e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV-----AADEGVIKRNGQ---------LR-- 68
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQdifkmdvieLRrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 ---IGYVPQ-----KLYLDTTLPLTVSRFMRLRpGTKKEDILPALKRVQ----AGHLMNAPMQKLSGGETQRVLLARALL 136
Cdd:PRK14247 84 vqmVFQIPNpipnlSIFENVALGLKLNRLVKSK-KELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSH 179
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-180 |
6.70e-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: 91.15 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQ---KLYLDTTLPL 84
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrdALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 TVS---RFMRLrpGTKKediLPALKRVQAGHLMNAPMQK----LSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQV 157
Cdd:TIGR03719 406 EISgglDIIKL--GKRE---IPSRAYVGRFNFKGSDQQKkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
170 180
....*....|....*....|...
gi 489125078 158 ALYDLIDQLRrelDCAVLmVSHD 180
Cdd:TIGR03719 481 ALEEALLNFA---GCAVV-ISHD 499
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-168 |
7.80e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.18 E-value: 7.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGY 71
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtrasLRrnIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLdttLPLTVSRFMRL-RPGTKKEDILPALKRVQAGHLMNAPMQK-----------LSGGETQRVLLARALLNKP 139
Cdd:PRK13657 414 VFQDAGL---FNRSIEDNIRVgRPDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrqLSGGERQRLAIARALLKDP 490
|
170 180
....*....|....*....|....*....
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMK 519
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-192 |
8.39e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 89.38 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 22 DVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ--LRIGYVP--------QKLYLDttlPLTvsrfmR 91
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdlLGMKDDEwravrsdiQMIFQD---PLA-----S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 92 LRPGTKKEDIL--------PALKRVQAGHLMNAPMQKL--------------SGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:PRK15079 111 LNPRMTIGEIIaeplrtyhPKLSRQEVKDRVKAMMLKVgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489125078 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-191 |
8.41e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.78 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----QLRIGYVPQKLYL----- 78
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldFQRDSIARGLLYLghapg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 -DTTL-PLTVSRFmrLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQ 156
Cdd:cd03231 84 iKTTLsVLENLRF--WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 489125078 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-183 |
9.30e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 9.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 19 VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR---IGYVPQKLYL----- 78
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaeLRnqkLGFIYQFHHLlpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 ---DTTLPLTVSRfmrLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNG 155
Cdd:PRK11629 104 aleNVAMPLLIGK---KKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180
....*....|....*....|....*...
gi 489125078 156 QVALYDLIDQLRRELDCAVLMVSHDLHL 183
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-180 |
1.02e-20 |
|
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: 90.76 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTTlpL 84
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPT--K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 TV---------------SRFMR---------------LRPGTKKEDILPALK---------------RVQAGhlmNAPMQ 119
Cdd:TIGR03719 84 TVrenveegvaeikdalDRFNEisakyaepdadfdklAAEQAELQEIIDAADawdldsqleiamdalRCPPW---DADVT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 120 KLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNgQVAlydLIDQLRRELDCAVLMVSHD 180
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVA---WLERHLQEYPGTVVAVTHD 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-180 |
1.29e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 90.34 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTTLPL 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 TVSRFMRL--RPGTKKEDILPALKRVQ-AGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYD 161
Cdd:PRK15064 400 TLFDWMSQwrQEGDDEQAVRGTLGRLLfSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNM 479
|
170
....*....|....*....
gi 489125078 162 LIDQLRRELdcavLMVSHD 180
Cdd:PRK15064 480 ALEKYEGTL----IFVSHD 494
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-218 |
2.00e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADE---GVIKRNG-----------QLR 68
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGitltaktvwdiREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYV---PQKLYLDTTLPLTVSRFMRLRpGTKKEDILPALKRV--QAGHL--MNAPMQKLSGGETQRVLLARALLNKPQL 141
Cdd:PRK13640 86 VGIVfqnPDNQFVGATVGDDVAFGLENR-AVPRPEMIKIVRDVlaDVGMLdyIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL-HLVMAktDEVLCLNH-HICCSGAPEVVSMHPEFISMFG 218
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIdEANMA--DQVLVLDDgKLLAQGSPVEIFSKVEMLKEIG 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-212 |
2.60e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.13 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-------LRIGYVP 73
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QK---------LYLDTTL------PLtvSRFMRLRPGTKKEDILPALKRV---QAGHLMNApmqKLSGGETQRVLLARAL 135
Cdd:PRK11831 84 KRmsmlfqsgaLFTDMNVfdnvayPL--REHTQLPAPLLHSTVMMKLEAVglrGAAKLMPS---ELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 136 LNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHPE 212
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVaDKKIVAHGSAQALQANPD 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-191 |
3.04e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.93 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRR----VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR----- 68
Cdd:PRK11153 4 LKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekeLRkarrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLYL--------DTTLPLTVSrfmrlrpGTKKEDI----LPALKRVQAGHLMNA-PMQkLSGGETQRVLLARAL 135
Cdd:PRK11153 84 IGMIFQHFNLlssrtvfdNVALPLELA-------GTPKAEIkarvTELLELVGLSDKADRyPAQ-LSGGQKQRVAIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 136 LNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRV 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-180 |
3.09e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.24 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYV--------PQKLYL 78
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFdqhraeldPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 DTtlpltvsrfmrLRPGtKKEDILPALKRVQAGHL-------MNA--PMQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:PRK11147 402 DN-----------LAEG-KQEVMVNGRPRHVLGYLqdflfhpKRAmtPVKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|.
gi 489125078 150 GVDVNGQVALYDLIDqlrrELDCAVLMVSHD 180
Cdd:PRK11147 470 DLDVETLELLEELLD----SYQGTVLLVSHD 496
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-195 |
4.35e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.71 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQ---RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------- 67
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 -RIGYV---PQKLYLDTTLPLTVSrFMRLRPG----TKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKP 139
Cdd:PRK13650 81 hKIGMVfqnPDNQFVGATVEDDVA-FGLENKGipheEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMK 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-169 |
4.51e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.70 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LR-- 68
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakiMRea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQ--KLYLDTTLP--LTVSRFMRLRPGTKKE-----DILPAL--KRVQAGHLMnapmqklSGGETQRVLLARALLN 137
Cdd:PRK11614 82 VAIVPEgrRVFSRMTVEenLAMGGFFAERDQFQERikwvyELFPRLheRRIQRAGTM-------SGGEQQMLAIGRALMS 154
|
170 180 190
....*....|....*....|....*....|..
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ 186
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-195 |
4.61e-20 |
|
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: 85.16 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQR--RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGY 71
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistipledLRssLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQK-LYLDTTLPLTVSRFMRLrpgtKKEDILPALkRVQAGHLmnapmqKLSGGETQRVLLARALLNKPQLLVLDEPTQG 150
Cdd:cd03369 87 IPQDpTLFSGTIRSNLDPFDEY----SDEEIYGAL-RVSEGGL------NLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 151 VDVNGQVALYDLIdqlRREL-DCAVLMVSHDLHLVmAKTDEVLCLN 195
Cdd:cd03369 156 IDYATDALIQKTI---REEFtNSTILTIAHRLRTI-IDYDKILVMD 197
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-184 |
6.04e-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: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQR-----------RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ--- 66
Cdd:COG4608 4 AEPLLEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdit 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 -----------LRIGYVPQKLY--LDTTL--------PLTVSRfmRLRPGTKKEDILPALKRV--QAGHLMNAPMQkLSG 123
Cdd:COG4608 84 glsgrelrplrRRMQMVFQDPYasLNPRMtvgdiiaePLRIHG--LASKAERRERVAELLELVglRPEHADRYPHE-FSG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 124 GETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVV 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-189 |
7.36e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 7.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVvLGLVAADEGVIKRNGqlRIGYVPQKLY------- 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEG--RVEFFNQNIYerrvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 78 -----------LDTTLPLTV-------SRFMRLRPGTKKEDIL-PALKRV----QAGHLMNAPMQKLSGGETQRVLLARA 134
Cdd:PRK14258 85 rlrrqvsmvhpKPNLFPMSVydnvaygVKIVGWRPKLEIDDIVeSALKDAdlwdEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 135 LLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTD 189
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-182 |
9.37e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 9.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYG-----QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LR 68
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeykraKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLYLDTTLPLTV----------SRFMRLRPGTKKEDI---LPALKRVQAG--HLMNAPMQKLSGGETQRVLLAR 133
Cdd:COG1101 82 IGRVFQDPMMGTAPSMTIeenlalayrrGKRRGLRRGLTKKRRelfRELLATLGLGleNRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLH 182
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-195 |
1.02e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSYGQ-RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LR-- 68
Cdd:PRK13636 4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmkLRes 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQ---------KLYLDTTL-PLTvsrfMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNK 138
Cdd:PRK13636 84 VGMVFQdpdnqlfsaSVYQDVSFgAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-205 |
1.08e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGV----------IKRNGQL--- 67
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshiellgrtVQREGRLard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 ------RIGYVPQKLYLDTTL--------------PLTVSRFMRLRPgTKKEDILPALKRVQAGHLMNAPMQKLSGGETQ 127
Cdd:PRK09984 81 irksraNTGYIFQQFNLVNRLsvlenvligalgstPFWRTCFSWFTR-EQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 128 RVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPE 205
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQgHVFYDGSSQ 238
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-194 |
1.47e-19 |
|
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: 84.05 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYL---DTTLP---------LTVS 87
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVfqnYSLLPwltvreniaLAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 88 RFMRLRPGTKKEDILPA-LKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEhIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180
....*....|....*....|....*...
gi 489125078 167 RRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVML 188
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-196 |
2.09e-19 |
|
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: 83.61 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRV-LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR--I 69
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipyLRrkI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 70 GYVPQ--KLYLDTTLPLTVSRFMRL---RPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVL 144
Cdd:cd03292 81 GVVFQdfRLLPDRNVYENVAFALEVtgvPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489125078 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALER 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-214 |
2.85e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.36 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 19 VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQlRIGY-------VPQKLYL------DTTLPLT 85
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-PIKYdkkslleVRKTVGIvfqnpdDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 86 VSR---FMRLRPGTKKEDI----LPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVA 158
Cdd:PRK13639 96 VEEdvaFGPLNLGLSKEEVekrvKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 159 LYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFI 214
Cdd:PRK13639 176 IMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDgKIIKEGTPKEVFSDIETI 231
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-192 |
4.08e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.73 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY---------GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----- 66
Cdd:COG4167 1 MSALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 -----------------------LRIGYVpqklyLDTTLPLTVSrfmrLRPGTKKEDILPALKRVqaGHL---MNAPMQK 120
Cdd:COG4167 81 dykyrckhirmifqdpntslnprLNIGQI-----LEEPLRLNTD----LTAEEREERIFATLRLV--GLLpehANFYPHM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 121 LSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVL 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-191 |
4.57e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQR--RVLSDVSLELRPGKILTLLGPNGAGKSTLvrvvLGLVA----ADEGVIKRNG---------QLR 68
Cdd:PRK11160 338 SLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTrawdPQQGEILLNGqpiadyseaALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 --IGYVPQKLYL--DTtlpltvsrfmrLR-------PGTKKEDILPALKRVQAGHLMNAPM----------QKLSGGETQ 127
Cdd:PRK11160 414 qaISVVSQRVHLfsAT-----------LRdnlllaaPNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 128 RVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEV 191
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTG-LEQFDRI 543
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-217 |
4.87e-19 |
|
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: 83.46 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 15 GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR---IGYVPQKLYL- 78
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelreLRrkkISMVFQSFALl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 -------DTTLPLT---VSRFMRLRPGTKkedilpALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:cd03294 115 phrtvleNVAFGLEvqgVPRAEREERAAE------ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHICC--------SGAPEVVSMHP--EFISMF 217
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDL-------DEALRLGDRIAImkdgrlvqVGTPEEILTNPanDYVREF 260
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-196 |
5.92e-19 |
|
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: 82.58 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY----------------------GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK 62
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 63 RNGQLR------IGYVPQklyldttlpLTVS---RFMRLRPGTKKEDILPALKRVQA----GHLMNAPMQKLSGGETQRV 129
Cdd:cd03220 81 VRGRVSsllglgGGFNPE---------LTGReniYLNGRLLGLSRKEIDEKIDEIIEfselGDFIDLPVKTYSSGMKARL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 130 LLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEK 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-192 |
7.23e-19 |
|
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: 85.26 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 16 QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV-AADEGVIKRNGQ----------------------LRIGYV 72
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKpvdirnpaqairagiamvpedrKRHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQkLYLDTTLPLTV----SRFMRLRPGTKKEDILPALKR--VQAGHlMNAPMQKLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:TIGR02633 352 PI-LGVGKNITLSVlksfCFKMRIDAAAELQIIGSAIQRlkVKTAS-PFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 147 PTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVL 474
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-192 |
9.46e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK------LYLDT-------TLPLTV 86
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangiVYISEdrkrdglVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 87 SRFMR---LRPGTKKEDILPALKRVQA-GHL----------MNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:PRK10762 348 KENMSltaLRYFSRAGGSLKHADEQQAvSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489125078 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK10762 428 VGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRIL 466
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-179 |
1.07e-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: 81.39 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLElrPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK--------- 75
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvsmlfqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 ------LYLDTTLPLTVSRFMRLRPgTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:cd03298 79 nnlfahLTVEQNVGLGLSPGLKLTA-EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190
....*....|....*....|....*....|
gi 489125078 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTH 187
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-196 |
1.20e-18 |
|
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: 81.82 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQR---RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IG 70
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwLRsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKLYLDTTlplTVSRFMRL-RPGTKKEDILPALKrvQAGH---LMNAPMQ----------KLSGGETQRVLLARALL 136
Cdd:cd03249 81 LVSQEPVLFDG---TIAENIRYgKPDATDEEVEEAAK--KANIhdfIMSLPDGydtlvgergsQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCavLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTIR-NADLIAVLQN 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
1.24e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.76 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 16 QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVI----------KRNGQLR-----IGYVPQ----KL 76
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagKKNKKLKplrkkVGIVFQfpehQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 77 YLDTtlpltVSRFMRLRP---GTKKEDIL----PALKRVQAGH--LMNAPMQkLSGGETQRVLLARALLNKPQLLVLDEP 147
Cdd:PRK13634 99 FEET-----VEKDICFGPmnfGVSEEDAKqkarEMIELVGLPEelLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHPEFISMFG 218
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMhKGTVFLQGTPREIFADPDELEAIG 244
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-215 |
1.31e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.75 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQR-----RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGV--------------IKRNGQL 67
Cdd:PRK13645 9 LDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanlkkIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 R--IGYV---PQKLYLDTTLPLTVSrFMRLRPGTKKEDI---LPAL-KRVQ--AGHLMNAPMQkLSGGETQRVLLARALL 136
Cdd:PRK13645 89 RkeIGLVfqfPEYQLFQETIEKDIA-FGPVNLGENKQEAykkVPELlKLVQlpEDYVKRSPFE-LSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFIS 215
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEgKVISIGSPFEIFSNQELLT 246
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-195 |
2.48e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 83.76 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 33 LTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK----LYLDTTlPLTVsrFMRLRPGTKKEDILPALKRV 108
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHhvdgLDLSSN-PLLY--MMRCFPGVPEQKLRAHLGSF 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 109 Q-AGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNgqvALYDLIDQLRReLDCAVLMVSHDLHLVMAK 187
Cdd:PLN03073 615 GvTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQGLVL-FQGGVLMVSHDEHLISGS 690
|
....*...
gi 489125078 188 TDEVLCLN 195
Cdd:PLN03073 691 VDELWVVS 698
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-191 |
3.07e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLR------------ 68
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLYLdttLP-LTV----------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLN 137
Cdd:PRK11288 81 VAIIYQELHL---VPeMTVaenlylgqlpHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAI 210
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-179 |
3.63e-18 |
|
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: 83.26 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 19 VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDT-TL------PLTVSRFMR 91
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgTLrdqiiyPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 92 lrPGTKKEDILPALKRVQAGHLMNAP---------MQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYdl 162
Cdd:TIGR00954 547 --RGLSDKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY-- 622
|
170
....*....|....*..
gi 489125078 163 idQLRRELDCAVLMVSH 179
Cdd:TIGR00954 623 --RLCREFGITLFSVSH 637
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-196 |
6.65e-18 |
|
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: 79.05 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR-----VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGqlRIGYVPQKLYld 79
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPW-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 80 ttlpltvsrfmrLRPGTKKEDIL--------------------PALKRVQAGHL-------MNapmqkLSGGETQRVLLA 132
Cdd:cd03250 77 ------------IQNGTIRENILfgkpfdeeryekvikacalePDLEILPDGDLteigekgIN-----LSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 133 RALLNKPQLLVLDEPTQGVDVNGQVALYD-LIDQLRRELDCAVLmVSHDLHLVmAKTDEVLCLNH 196
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRIL-VTHQLQLL-PHADQIVVLDN 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-215 |
7.02e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 80.64 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV--------AADEGVIKRNGQ-LRIGYVPQ 74
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEpLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYLDTTLP--------------LTVSRFMRLRPG--TKKED---ILPALKRVQAGHLMNAPMQKLSGGETQRVLLARAL 135
Cdd:PRK13547 81 LARLRAVLPqaaqpafafsareiVLLGRYPHARRAgaLTHRDgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 136 ---------LNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPE 205
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLaDGAIVAHGAPA 240
|
250
....*....|
gi 489125078 206 VVsMHPEFIS 215
Cdd:PRK13547 241 DV-LTPAHIA 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-196 |
1.04e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.68 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSY-----------GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAdEGVIKRNGQLRIG 70
Cdd:PRK15134 273 SPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKLyldttlpLTVSRFMR---------LRPGTKKEDIL--------PALKRVQAGHLMNAPMQKL------------ 121
Cdd:PRK15134 352 LNRRQL-------LPVRHRIQvvfqdpnssLNPRLNVLQIIeeglrvhqPTLSAAQREQQVIAVMEEVgldpetrhrypa 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 122 --SGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:PRK15134 425 efSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
1.18e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.75 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG------------QLR 68
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLYLDTTL-------------------PLTVSRFMRLRPGTkkedilpALKRVQAGHLMNAPMQKLSGGETQRV 129
Cdd:PRK09700 82 IGIIYQELSVIDELtvlenlyigrhltkkvcgvNIIDWREMRVRAAM-------MLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 130 LLARALLNKPQLLVLDEPTQGVdVNGQV-ALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVV 207
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSL-TNKEVdYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMkDGSSVCSGMVSDV 232
|
....*....
gi 489125078 208 SMHpEFISM 216
Cdd:PRK09700 233 SND-DIVRL 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-214 |
1.26e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQlRIGYVP------- 73
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-DLSHVPpyqrpin 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 ---QKLYLdttLP-LTVSRFM-------RLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLL 142
Cdd:PRK11607 95 mmfQSYAL---FPhMTVEQNIafglkqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 143 VLDEPTQGVD--VNGQVALyDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP------EF 213
Cdd:PRK11607 172 LLDEPMGALDkkLRDRMQL-EVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIYEHPttrysaEF 249
|
.
gi 489125078 214 I 214
Cdd:PRK11607 250 I 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-192 |
1.36e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 79.37 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 26 ELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQlRIGYVPQKLYLDTtlPLTVSRFmrLRPGTK-------- 97
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADY--EGTVRDL--LSSITKdfythpyf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 98 KEDILPALKRVQaghLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMV 177
Cdd:cd03237 96 KTEIAKPLQIEQ---ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVV 172
|
170
....*....|....*
gi 489125078 178 SHDLHLVMAKTDEVL 192
Cdd:cd03237 173 EHDIIMIDYLADRLI 187
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-191 |
1.48e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.32 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 17 RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------------RIGYVPQK---- 75
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqidaiklrkEVGMVFQQpnpf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 ----LYLDTTLPLTVSRFMRLRpgTKKEDILPALKRV----QAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEP 147
Cdd:PRK14246 103 phlsIYDNIAYPLKSHGIKEKR--EIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489125078 148 TQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-195 |
2.00e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.02 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRR--VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------R 68
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnfeklrkH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYV---PQKLYLDTTLPLTVSRFMR--LRPGTKKEDILP-ALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLL 142
Cdd:PRK13648 85 IGIVfqnPDNQFVGSIVKYDVAFGLEnhAVPYDEMHRRVSeALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489125078 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMN 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-196 |
2.03e-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: 80.92 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYG--QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IG 70
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlaSLRrqVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKLYL-DTTLPLTVsRFMRLRpGTKKEDILPALKRVQAGHLMNA-PM----------QKLSGGETQRVLLARALLNK 138
Cdd:TIGR02203 410 LVSQDVVLfNDTIANNI-AYGRTE-QADRAEIERALAAAYAQDFVDKlPLgldtpigengVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTI-EKADRIVVMDD 542
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-198 |
2.09e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.30 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 22 DVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------------RIGYVPQklylDTTL-P-L 84
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrRIGYVFQ----DARLfPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 TVSRfmRLRPGTKKED------------ILPALKRVqaghlmnaPMqKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:PRK11144 92 KVRG--NLRYGMAKSMvaqfdkivallgIEPLLDRY--------PG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHI 198
Cdd:PRK11144 161 LPRKRELLPYLERLAREINIPILYVSHSL-------DEILRLADRV 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-181 |
3.13e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLR------------ 68
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLYLdttLP-LT-----------VSRFMRL--RPGTKKEDILpaLKRVQAGHLMNAPMQKLSGGETQRVLLARA 134
Cdd:PRK10762 81 IGIIHQELNL---IPqLTiaeniflgrefVNRFGRIdwKKMYAEADKL--LARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489125078 135 LLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRL 201
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-179 |
3.99e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVA--ADEGVIKRNGQ------------LRIGY 71
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEdilelspderarAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQklYldttlP-----LTVSRFMRLRPGTKKEDILPALKRVQaghLMNAPMQKL---------------SGGETQRVLL 131
Cdd:COG0396 82 AFQ--Y-----PveipgVSVSNFLRTALNARRGEELSAREFLK---LLKEKMKELgldedfldryvnegfSGGEKKRNEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489125078 132 ARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-181 |
4.08e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.24 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 27 LRPGKILTLLGPNGAGKSTLVRVV-------LGLVAAD---EGVIKR--------------NGQLRIGYVPQklYLDTtL 82
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnLGDYEEEpswDEVLKRfrgtelqnyfkklyNGEIKVVHKPQ--YVDL-I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 PL----TVSRFMRlrpGTKKEDILPAL-KRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQV 157
Cdd:PRK13409 173 PKvfkgKVRELLK---KVDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRL 249
|
170 180
....*....|....*....|....*.
gi 489125078 158 ALYDLIdqlrREL--DCAVLMVSHDL 181
Cdd:PRK13409 250 NVARLI----RELaeGKYVLVVEHDL 271
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-207 |
5.27e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.17 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQ-----RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG-------------Q 66
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 LRIGYVPQ----KLYLDTtlpltVSRFMRLRP---GTKKEDILpalKRVQAGhlMNA------------PMQkLSGGETQ 127
Cdd:PRK13637 83 KKVGLVFQypeyQLFEET-----IEKDIAFGPinlGLSEEEIE---NRVKRA--MNIvgldyedykdksPFE-LSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 128 RVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHIC-CSGAPEV 206
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCeLQGTPRE 231
|
.
gi 489125078 207 V 207
Cdd:PRK13637 232 V 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-196 |
5.28e-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: 77.53 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYG--QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGY 71
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawLRrqVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKlylDTTLPLTVSRFMRL-RPGTKKEDILPALKRVQA-----------GHLMNAPMQKLSGGETQRVLLARALLNKP 139
Cdd:cd03252 81 VLQE---NVLFNRSIRDNIALaDPGMSMERVIEAAKLAGAhdfiselpegyDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 140 QLLVLDEPTQGVDVNGQVAlydLIDQLRRELDC-AVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:cd03252 158 RILIFDEATSALDYESEHA---IMRNMHDICAGrTVIIIAHRLSTVK-NADRIIVMEK 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-219 |
5.75e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.85 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL--VAADEGVI--------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 62 -----------------------KRNGQLRIGYVPQK---LYLDTTLPLTVSRFMRLRPGTKKEDILPA---LKRVQAGH 112
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRtfaLYGDDTVLDNVLEALEEIGYEGKEAVGRAvdlIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 113 LMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|....*....
gi 489125078 193 CL-NHHICCSGAP-EVVSMHPEFISMFGQ 219
Cdd:TIGR03269 241 WLeNGEIKEEGTPdEVVAVFMEGVSEVEK 269
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-198 |
5.84e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK----- 75
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKahqlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 LYLDTTLPLTvsrFMRLrpgTKKEDIL-------PALKRVQA------GHL-MNAPMQKLSGGETQRVLLARALLNKPQL 141
Cdd:PRK15439 88 IYLVPQEPLL---FPNL---SVKENILfglpkrqASMQKMKQllaalgCQLdLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHlvmaktdEVLCLNHHI 198
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLP-------EIRQLADRI 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-218 |
6.38e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.74 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 14 YGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LR--IGYV-----PQK 75
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllaLRqqVATVfqdpeQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 LYLDTTLPLTVSrfmrLRP-GTKKEDIL----PALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQG 150
Cdd:PRK13638 91 FYTDIDSDIAFS----LRNlGVPEAEITrrvdEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 151 VDVNGQVALYDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFISMFG 218
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQgQILTHGAPGEVFACTEAMEQAG 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-214 |
6.53e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.95 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYG-----QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG-------------Q 66
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 LR--IGYVPQ----KLYLDTTL------PLTVSrfmrLRPGTKKEDILPALKRVQ-AGHLMNAPMQKLSGGETQRVLLAR 133
Cdd:PRK13641 83 LRkkVSLVFQfpeaQLFENTVLkdvefgPKNFG----FSEDEAKEKALKWLKKVGlSEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHgKLIKHASPKEIFSDKE 237
|
..
gi 489125078 213 FI 214
Cdd:PRK13641 238 WL 239
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-180 |
8.91e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.01 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 6 SLENVSVSYG-QRRVLSDVSLELRPG-KIlTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTTlp 83
Cdd:PRK11819 8 TMNRVSKVVPpKKQILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 LTV---------------SRF----MRL-RPGTKKEDILPALKRVQA------GH--------LMNA--------PMQKL 121
Cdd:PRK11819 85 KTVrenveegvaevkaalDRFneiyAAYaEPDADFDALAAEQGELQEiidaadAWdldsqleiAMDAlrcppwdaKVTKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 122 SGGETQRVLLARALLNKPQLLVLDEPTQGVDVNgQVAlydLIDQLRRELDCAVLMVSHD 180
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-SVA---WLEQFLHDYPGTVVAVTHD 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-192 |
9.08e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.08 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 15 GQRRV--LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTTLPLTV--SRFM 90
Cdd:PRK11308 24 PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVfqNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 91 RLRPGTKKEDIL----------PALKRVQAGHLMnapMQKL--------------SGGETQRVLLARALLNKPQLLVLDE 146
Cdd:PRK11308 104 SLNPRKKVGQILeepllintslSAAERREKALAM---MAKVglrpehydryphmfSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-194 |
1.02e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQR---RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL---------- 67
Cdd:PRK13642 1 MNKILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 68 -RIGYV---PQKLYLDTTLPLTVSRFMRlRPGTKKEDILP----ALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKP 139
Cdd:PRK13642 81 rKIGMVfqnPDNQFVGATVEDDVAFGME-NQGIPREEMIKrvdeALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL 194
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVM 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
1.05e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.15 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEG-VIKRNGQLR----------IGY 71
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsVLIRGEPITkenirevrkfVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYlDTTLPLTVSRFMRLRP-------GTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVL 144
Cdd:PRK13652 83 VFQNPD-DQIFSPTVEQDIAFGPinlgldeETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFIS 215
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIFLQPDLLA 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-181 |
1.50e-16 |
|
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: 78.29 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 27 LRPGKILTLLGPNGAGKSTLVRVV-------LGLVAAD---EGVIKR--------------NGQLRIGYVPQklYLDTtL 82
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILsgelkpnLGDYDEEpswDEVLKRfrgtelqdyfkklaNGEIKVAHKPQ--YVDL-I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 PLTVSrfmrlrpGTKKEdilpALKRV-QAG------------HLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:COG1245 173 PKVFK-------GTVRE----LLEKVdERGkldelaeklgleNILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|..
gi 489125078 150 GVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-194 |
1.82e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------RIGY 71
Cdd:PRK10575 10 TTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLylDTTLPLTVSRFMRL----------RPG-TKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQ 140
Cdd:PRK10575 90 LPQQL--PAAEGMTVRELVAIgrypwhgalgRFGaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVAL 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-180 |
2.06e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.85 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQklyldttlpltvS 87
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQ------------S 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 88 RfMRLRPG-TKKEDILPALKRVQAG-HLMN------------APMQK----LSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:PRK11819 396 R-DALDPNkTVWEEISGGLDIIKVGnREIPsrayvgrfnfkgGDQQKkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTN 474
|
170 180 190
....*....|....*....|....*....|....
gi 489125078 150 GVDVNGQVALYDLIdqlrreLD---CAVLmVSHD 180
Cdd:PRK11819 475 DLDVETLRALEEAL------LEfpgCAVV-ISHD 501
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
7-179 |
2.36e-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: 75.76 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLG--LVAADEGVIKRNGQLRIGYVPQK-----LYLD 79
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDEraragLFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 80 TTLP-----LTVSRFMR----LRPGTKKEDILPA------LKRVQAGHLMNAPMQK------LSGGETQRVLLARALLNK 138
Cdd:TIGR01978 83 FQYPeeipgVSNLEFLRsalnARRSARGEEPLDLldfeklLKEKLALLDMDEEFLNrsvnegFSGGEKKRNEILQMALLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489125078 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
Cdd:TIGR01978 163 PKLAILDEIDSGLDIDALKIVAEGINRLREP-DRSFLIITH 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-183 |
2.41e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.59 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 16 QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR---IGYVPQKLYLDT 80
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeearakLRakhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 81 TLpltvsrfmrlrpgTKKEDI-LPAL--------KRVQAGHLM----------NAPMQkLSGGETQRVLLARALLNKPQL 141
Cdd:PRK10584 102 TL-------------NALENVeLPALlrgessrqSRNGAKALLeqlglgkrldHLPAQ-LSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-208 |
2.43e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.31 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQ-RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL-----------R 68
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 IGYVPQKLYlDTTLPLTV-------SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQL 141
Cdd:PRK13647 81 VGLVFQDPD-DQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVS 208
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEgRVLAEGDKSLLT 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-232 |
3.03e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYG-----QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK--------RNGQLRIG 70
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvssTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKLYLDTTLPL------TVSRFMRLRP---GTKKEDIlpalKRVQAGHLMNAPMQK---------LSGGETQRVLLA 132
Cdd:PRK13643 81 PVRKKVGVVFQFPEsqlfeeTVLKDVAFGPqnfGIPKEKA----EKIAAEKLEMVGLADefwekspfeLSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 133 RALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHP 211
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKgHIISCGTPSDVFQEV 235
|
250 260
....*....|....*....|.
gi 489125078 212 EFISmfgqrgAEQLGIYRHNH 232
Cdd:PRK13643 236 DFLK------AHELGVPKATH 250
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-194 |
3.64e-16 |
|
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: 75.48 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 28 RPGKILTLLGPNGAGKSTLVRVVLGLVAADEG----------VIK--------------RNGQLRIGYVPQklYLDTtLP 83
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeILDefrgselqnyftklLEGDVKVIVKPQ--YVDL-IP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 L----TVSRFMRLRPGTKKEDILpaLKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVAL 159
Cdd:cd03236 101 KavkgKVGELLKKKDERGKLDEL--VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190
....*....|....*....|....*....|....*
gi 489125078 160 YDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:cd03236 179 ARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-181 |
5.71e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.81 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVV-----LGLVAADEGVIKRNG---------- 65
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGhniysprtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 -QLR--IGYVPQKlylDTTLPLT----VSRFMRLRpGTKKEDIL-PALKRVQAG---------HLMNAPMqKLSGGETQR 128
Cdd:PRK14239 82 vDLRkeIGMVFQQ---PNPFPMSiyenVVYGLRLK-GIKDKQVLdEAVEKSLKGasiwdevkdRLHDSAL-GLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 129 VLLARALLNKPQLLVLDEPTQGVD--VNGQV--ALYDLIDqlrrelDCAVLMVSHDL 181
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDpiSAGKIeeTLLGLKD------DYTMLLVTRSM 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-181 |
6.11e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 24 SLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK-----LYLDTTL--PLTVSR--FMRLRP 94
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvsmLFQENNLfsHLTVAQniGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 95 GTK-----KEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
Cdd:PRK10771 99 GLKlnaaqREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170
....*....|..
gi 489125078 170 LDCAVLMVSHDL 181
Cdd:PRK10771 179 RQLTLLMVSHSL 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-207 |
7.65e-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: 76.38 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEG------------VIKRNGQLR---- 68
Cdd:TIGR03269 285 VSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvdMTKPGPDGRgrak 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 --IGYVPQK--LYLDTTL--PLTVSRFMRLRPGTKKEDILPALKRV-----QAGHLMNAPMQKLSGGETQRVLLARALLN 137
Cdd:TIGR03269 365 ryIGILHQEydLYPHRTVldNLTEAIGLELPDELARMKAVITLKMVgfdeeKAEEILDKYPDELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV-LCLNHHICCSGAPEVV 207
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAaLMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-195 |
9.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.82 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQ-----RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG-------------- 65
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 -QLRIGYVPQ----KLYLDTtlpltVSRFMRLRPGTKKEDILPALKR-----VQAGHLMN----APMQkLSGGETQRVLL 131
Cdd:PRK13646 83 vRKRIGMVFQfpesQLFEDT-----VEREIIFGPKNFKMNLDEVKNYahrllMDLGFSRDvmsqSPFQ-MSGGQMRKIAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 132 ARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMK 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-152 |
1.05e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 15 GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAD---EGVIKRNG--------QLRIGYVPQKLYLDTTLP 83
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 ----LTVSRFMRL-RPGTKKE------DILPALKRVQAGH-LMNAP--MQKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:TIGR00955 116 vrehLMFQAHLRMpRRVTKKEkrervdEVLQALGLRKCANtRIGVPgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
...
gi 489125078 150 GVD 152
Cdd:TIGR00955 196 GLD 198
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-187 |
1.31e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 75.65 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 23 VSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAdEGVIKRNGQ-LR----------IGYVPQklylDTTLPL-TVSRFM 90
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIeLReldpeswrkhLSWVGQ----NPQLPHgTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 91 RL-RPGTKKEDILPALKRVQAGHLMNAPMQ-----------KLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVA 158
Cdd:PRK11174 444 LLgNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190
....*....|....*....|....*....|....*..
gi 489125078 159 LYDLIDQLRRELDCavLMVSH---DLH-----LVMAK 187
Cdd:PRK11174 524 VMQALNAASRRQTT--LMVTHqleDLAqwdqiWVMQD 558
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-196 |
1.76e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.58 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVsYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAdeGVIKRNGQLRIG---YVPQKL- 76
Cdd:PRK10418 1 MPQQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDgkpVAPCALr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 77 --YLDTTLPLTVSRFMRLRP-GTKKEDILPALKRVQAGHLMNAPMQ----------------KLSGGETQRVLLARALLN 137
Cdd:PRK10418 78 grKIATIMQNPRSAFNPLHTmHTHARETCLALGKPADDATLTAALEavglenaarvlklypfEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-192 |
2.95e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.79 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 15 GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL------VAAD-----------------EGVIKRNgqlrIGY 71
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhVTADrfrwngidllklsprerRKIIGRE----IAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQ--KLYLDTTLPL-----------TVS-RFMRlRPGTKKEDILPALKRV---QAGHLMNAPMQKLSGGETQRVLLARA 134
Cdd:COG4170 94 IFQepSSCLDPSAKIgdqlieaipswTFKgKWWQ-RFKWRKKRAIELLHRVgikDHKDIMNSYPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 135 LLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV--MAKTDEVL 192
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESIsqWADTITVL 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-179 |
3.04e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.95 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVR-----VVLGLVAADEGVIKRNG---------- 65
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGrniyspdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 ---QLRIGYVPQ--------KLYLDTTLPLTVSRFMRLRpGTKKEDILPALKRV----QAGHLMNAPMQKLSGGETQRVL 130
Cdd:PRK14267 81 ievRREVGMVFQypnpfphlTIYDNVAIGVKLNGLVKSK-KELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489125078 131 LARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSH 179
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-180 |
3.10e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.76 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY----GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------- 66
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 67 --LR---IGYVPQKLYLdttLP-LTVSR-------FMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLAR 133
Cdd:PRK10535 81 aqLRrehFGFIFQRYHL---LShLTAAQnvevpavYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHD 180
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-166 |
4.01e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 16 QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAD--EGVIKRNGQ-------LRIGYVPQK--LYLDTTL-- 82
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRkptkqilKRTGFVTQDdiLYPHLTVre 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 PLTVSRFMRL-RPGTKKEDILPA--------LKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDV 153
Cdd:PLN03211 160 TLVFCSLLRLpKSLTKQEKILVAesviselgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170
....*....|...
gi 489125078 154 ngqVALYDLIDQL 166
Cdd:PLN03211 240 ---TAAYRLVLTL 249
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
5.57e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.96 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 19 VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIkRNGQLRIG-YVPQKLYLDTTLPLTVSRFMRLR---- 93
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDIYIGdKKNNHELITNPYSKKIKNFKELRrrvs 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 94 -----------PGTKKEDIL--P-ALK------RVQAGHLMN-----------APMQkLSGGETQRVLLARALLNKPQLL 142
Cdd:PRK13631 120 mvfqfpeyqlfKDTIEKDIMfgPvALGvkkseaKKLAKFYLNkmglddsylerSPFG-LSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEFIS 215
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKgKILKTGTPYEIFTDQHIIN 271
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-192 |
6.81e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 6.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 17 RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-LRIGYVPQklyldttlplTVSRFMRLRPG 95
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpIDIRSPRD----------AIRAGIMLCPE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 96 TKKEDILPALKRVQ-------------AGHLMNA-----------------------PMQKLSGGETQRVLLARALLNKP 139
Cdd:PRK11288 336 DRKAEGIIPVHSVAdninisarrhhlrAGCLINNrweaenadrfirslniktpsreqLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-192 |
1.66e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.45 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKL-------------------YLDT 80
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvteerrstgiyaYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 81 TLPLTVSRF------MRLRPGTK-KED---ILPALKRVQAGHlmNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQG 150
Cdd:PRK10982 344 GFNSLISNIrnyknkVGLLDNSRmKSDtqwVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489125078 151 VDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRIL 462
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-224 |
1.71e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.31 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYG-----QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL--------RIGY 71
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLDTTLPL------TVSRFMRLRP---GTKKEDIlPALKRVQ------AGHLMNAPMQKLSGGETQRVLLARALL 136
Cdd:PRK13649 83 IRKKVGLVFQFPEsqlfeeTVLKDVAFGPqnfGVSQEEA-EALAREKlalvgiSESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPEF-- 213
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDIFQDVDFle 240
|
250
....*....|....*....
gi 489125078 214 --------ISMFGQRGAEQ 224
Cdd:PRK13649 241 ekqlgvpkITKFAQRLADR 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-184 |
2.14e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 22 DVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ------------LR--IGYVPQKLY--LDTTL--- 82
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklqaLRrdIQFIFQDPYasLDPRQtvg 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 -----PLTVSRFMRLRPGTKKEDILpaLKRV--QAGHLMNAPmQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNG 155
Cdd:PRK10261 422 dsimePLRVHGLLPGKAAAARVAWL--LERVglLPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180
....*....|....*....|....*....
gi 489125078 156 QVALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVV 527
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-196 |
2.68e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.97 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRV--LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGY 71
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlasLRnqVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYL--DTtlpltVSRFMRLRPGTK--KEDILPALKrvqAGHLMN--APMQK------------LSGGETQRVLLAR 133
Cdd:PRK11176 422 VSQNVHLfnDT-----IANNIAYARTEQysREQIEEAAR---MAYAMDfiNKMDNgldtvigengvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH 196
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEILVVED 553
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-212 |
4.09e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.00 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 14 YGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRN-----------GQLRIGYVPQKLYLDTTL 82
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkdGQLKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 PLTVSRFMRLRPGTKKEDILPA------LKRVQAGHLMNAPMQK--------------LSGGETQRVLLARALLNKPQLL 142
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEApiqvlgLSKQEARERAVKYLAKvgideraqgkypvhLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLmVSHDLHLVMAKTDEVLCLNH-HICCSGAPEVVSMHPE 212
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQgKIEEEGAPEQLFGNPQ 244
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-224 |
5.47e-14 |
|
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: 69.89 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 19 VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGqlRIGYVPQklyldttlpltVSRFMrlrPGTKK 98
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQ-----------FSWIM---PGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 99 EDILPALKR--------VQAGHLM----------NAPMQK----LSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQ 156
Cdd:cd03291 116 ENIIFGVSYdeyryksvVKACQLEeditkfpekdNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 157 VALYD-----LIDQLRReldcaVLMVSHDLHLvmAKTDEVLCLNHHIC--CSGAPEVVSMHPEFISM------FGQRGAE 223
Cdd:cd03291 196 KEIFEscvckLMANKTR-----ILVTSKMEHL--KKADKILILHEGSSyfYGTFSELQSLRPDFSSKlmgydtFDQFSAE 268
|
.
gi 489125078 224 Q 224
Cdd:cd03291 269 R 269
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-152 |
6.54e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.04 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 10 VSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVV-----LGLVaadEGVIKRNGQLR-------IGYVPQkly 77
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPLdknfqrsTGYVEQ--- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 78 LDTTLP-LTVSRFMRLrpgtkkedilpalkrvqaghlmNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:cd03232 87 QDVHSPnLTVREALRF----------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-190 |
9.06e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.05 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 9 NVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----------QLRIGYVPQKLYL 78
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlctyQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 DTTLPLTVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDvngQVA 158
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELS 162
|
170 180 190
....*....|....*....|....*....|....*
gi 489125078 159 LYDLIDQLR--RELDCAVLMVSH-DLHLVMAKTDE 190
Cdd:PRK13540 163 LLTIITKIQehRAKGGAVLLTSHqDLPLNKADYEE 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-194 |
1.02e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRR----VLSDVSLELRPGKILTLLGPNGAGKS----TLVRVVL---GLVAADEGVIKRNGQLRIGYV 72
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQK-----------LYLDTTLPLT-----------VSRFMRLRPGTKKEDILPALKRV-------QAGHLMNAPMQKLSG 123
Cdd:PRK10261 92 EQSaaqmrhvrgadMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMldqvripEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 124 GETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-152 |
1.26e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 9 NVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAadegviKRNGQLRIGYVPQKLYLDTTLpltVSR 88
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK------GTPVAGCVDVPDNQFGREASL---IDA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 89 FMRLRPGTKKEDILPALKRVQAgHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:COG2401 106 IGRKGDFKDAVELLNAVGLSDA-VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-191 |
1.53e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL--VAADEGVIKRNGQ-LR--------- 68
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEeLQasnirdter 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 --IGYVPQKLYLDTTLPLTVSRFM--RLRPG--------TKKEDILpaLKRVQAGHLMNAPMQKLSGGETQRVLLARALL 136
Cdd:PRK13549 82 agIAIIHQELALVKELSVLENIFLgnEITPGgimdydamYLRAQKL--LAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 137 NKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTI 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-152 |
1.66e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 22 DVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LRIGYVPQ--KLYLDttlpLTV--- 86
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagdiatrRRVGYMSQafSLYGE----LTVrqn 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 87 ----SRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:NF033858 360 lelhARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-191 |
2.03e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.08 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAD--EGVIKRNGQ------LR------I 69
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSplkasnIRdteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 70 GYVPQKLYLDTTLPLTVSRFMR---LRPGTKKED---ILPA---LKRVQAGHLMNA-PMQKLSGGETQRVLLARALLNKP 139
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneiTLPGGRMAYnamYLRAknlLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489125078 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTI 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-231 |
2.91e-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: 69.17 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 19 VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGqlRIGYVPQklyldttlpltVSRFMrlrPGTKK 98
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQ-----------TSWIM---PGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 99 EDILPALKR--------VQAGHLM----------NAPMQK----LSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQ 156
Cdd:TIGR01271 505 DNIIFGLSYdeyrytsvIKACQLEedialfpekdKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 157 VALYD------LIDQLRreldcaVLMVSHDLHLvmAKTDEVLCLNHHIC--CSGAPEVVSMHPEFIS-MFGQRGAEQLGI 227
Cdd:TIGR01271 585 KEIFEsclcklMSNKTR------ILVTSKLEHL--KKADKILLLHEGVCyfYGTFSELQAKRPDFSSlLLGLEAFDNFSA 656
|
....
gi 489125078 228 YRHN 231
Cdd:TIGR01271 657 ERRN 660
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-152 |
3.14e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK--------------RNGQLR 68
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslsqQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 -----IGYV-------PQKLYLDTTL--PLTVSrfmrlrpGTKKEDILPA----LKRVQAGHLMNAPMQKLSGGETQRVL 130
Cdd:PRK11264 82 qlrqhVGFVfqnfnlfPHRTVLENIIegPVIVK-------GEPKEEATARarelLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180
....*....|....*....|..
gi 489125078 131 LARALLNKPQLLVLDEPTQGVD 152
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALD 176
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-216 |
4.25e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG-----------QLRIGY 71
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQklylDTTLpLTVSRFMRLRPGTK--KEDILPALKRVQAGHLMNAPMQKL-----------SGGETQRVLLARALLNK 138
Cdd:TIGR00957 1365 IPQ----DPVL-FSGSLRMNLDPFSQysDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 139 PQLLVLDEPTQGVDVNGQvalyDLIDQLRREL--DCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGAP-EVVSMHPEFIS 215
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPsNLLQQRGIFYS 1515
|
.
gi 489125078 216 M 216
Cdd:TIGR00957 1516 M 1516
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-207 |
5.89e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQR----RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL------VAADEGVIKRNGQLRIGYVP 73
Cdd:PRK11022 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 QKLYLDTTLPLTVSRFM-RLRPG-TKKEDILPALKRVQAGH-----------------------LMNAPMQkLSGGETQR 128
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMtSLNPCyTVGFQIMEAIKVHQGGNkktrrqraidllnqvgipdpasrLDVYPHQ-LSGGMSQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 129 VLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTdevlclnHHICCSGAPEVV 207
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAA-------HKIIVMYAGQVV 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-180 |
6.80e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQ--------- 74
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 ----------------KLYLDttlpltVSRFMRLRPgtkKEDILPALKRVQA--GHL-------------------MNAP 117
Cdd:PRK11147 83 vydfvaegieeqaeylKRYHD------ISHLVETDP---SEKNLNELAKLQEqlDHHnlwqlenrinevlaqlgldPDAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489125078 118 MQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVngqvalyDLIDQLR---RELDCAVLMVSHD 180
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI-------ETIEWLEgflKTFQGSIIFISHD 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-180 |
7.27e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQL--------R-IGYVPQ 74
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadRdIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 K--LYldttlP-LTVSRFM----RLRpGTKKEDIlpaLKRVQ--AGHLMNAPM-----QKLSGGETQRVLLARALLNKPQ 140
Cdd:PRK11650 84 NyaLY-----PhMSVRENMayglKIR-GMPKAEI---EERVAeaARILELEPLldrkpRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD 194
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-211 |
7.31e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.43 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 16 QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----QLRIGYVPQKLYLDTTLPL----TVS 87
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltKLQLDSWRSRLAVVSQTPFlfsdTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 88 RFMRL-RPGTKKEDI---------------LPALKRVQAGH--LMnapmqkLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:PRK10789 407 NNIALgRPDATQQEIehvarlasvhddilrLPQGYDTEVGErgVM------LSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 150 GVDvnGQVAlYDLIDQLRRELDCAVLMVS-HDLHlVMAKTDEVLCLNH-HICCSGAPEVVSMHP 211
Cdd:PRK10789 481 AVD--GRTE-HQILHNLRQWGEGRTVIISaHRLS-ALTEASEILVMQHgHIAQRGNHDQLAQQS 540
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-191 |
1.27e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 3 TLVSLENVSvSYGQRRVlSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG------------QLRIG 70
Cdd:PRK09700 264 TVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprspldavKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKLYLDTTLP-------LTVSRFMRL---------------RPGTKKEDILPALKrvqaGHLMNAPMQKLSGGETQR 128
Cdd:PRK09700 342 YITESRRDNGFFPnfsiaqnMAISRSLKDggykgamglfhevdeQRTAENQRELLALK----CHSVNQNITELSGGNQQK 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489125078 129 VLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRI 479
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-181 |
1.94e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 63.75 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSlELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGqLRIGYVPQKLyldttlpl 84
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 tvsrfmrlrpgtkkedilpalkrvqaghlmnapmqKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLID 164
Cdd:cd03222 71 -----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170
....*....|....*..
gi 489125078 165 QLRRELDCAVLMVSHDL 181
Cdd:cd03222 116 RLSEEGKKTALVVEHDL 132
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-169 |
2.24e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 16 QRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGviKRNGQLRigyVPQKLYLDTTLPLTVSRFMR---- 91
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--ERQSQFS---HITRLSFEQLQKLVSDEWQRnntd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 92 -LRPG------TKKEDIL-----PAL-----KRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVN 154
Cdd:PRK10938 90 mLSPGeddtgrTTAEIIQdevkdPARceqlaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170
....*....|....*
gi 489125078 155 GQVALYDLIDQLRRE 169
Cdd:PRK10938 170 SRQQLAELLASLHQS 184
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-181 |
3.09e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.42 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVikrNGQLRIGYVPQKLYLDTT 81
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF---RVEGKVTFHGKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 82 LPLTVSR-----FMRLRP-------------------GTKKEDILPALKRV----QAGHLMNAPMQKLSGGETQRVLLAR 133
Cdd:PRK14243 85 DPVEVRRrigmvFQKPNPfpksiydniaygaringykGDMDELVERSLRQAalwdEVKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-179 |
6.66e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.95 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSY------GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG--------- 65
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 66 ---QLRIGYVPQKLylDTTLPLT-VSRFMRLRP---GTKKEDILP----ALKRVQAGHLMNAPMQKLSGGETQRVLLARA 134
Cdd:PRK13633 81 wdiRNKAGMVFQNP--DNQIVATiVEEDVAFGPenlGIPPEEIRErvdeSLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489125078 135 LLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-196 |
1.07e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 1 MTTLVSLENVSVSYGQR---------RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG-QLRIG 70
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 ---YVPQKL-------------------YLDTTLPLTVSrfmrLRPGTKKEDILPALKRV--QAGHLMNAPmQKLSGGET 126
Cdd:PRK15112 81 dysYRSQRIrmifqdpstslnprqrisqILDFPLRLNTD----LEPEQREKQIIETLRQVglLPDHASYYP-HMLAPGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 127 QRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHdlHLVMAK--TDEVLCLNH 196
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQ--HLGMMKhiSDQVLVMHQ 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-195 |
1.11e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.57 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 18 RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIK---RNGQLRIGYVPQKLYLDT-TLPLTVSRF---- 89
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifKDEKNKKKTKEKEKVLEKlVIQKTRFKKikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 90 --MRLRPG-------------TKKEDIL-----------PALKRVQA---------GHLMNAPMQkLSGGETQRVLLARA 134
Cdd:PRK13651 101 keIRRRVGvvfqfaeyqlfeqTIEKDIIfgpvsmgvskeEAKKRAAKyielvgldeSYLQRSPFE-LSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 135 LLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLN 195
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-179 |
1.35e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLvAADEGVIKRNG---------QLR--IGY 71
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGvswnsvtlqTWRkaFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLdttlpLTVSRFMRLRPGTK--KEDILPALKRVQAGHLMNAPMQK-----------LSGGETQRVLLARALLNK 138
Cdd:TIGR01271 1297 IPQKVFI-----FSGTFRKNLDPYEQwsDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSK 1371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489125078 139 PQLLVLDEPTQGVD-VNGQValydlidqLRREL-----DCAVLMVSH 179
Cdd:TIGR01271 1372 AKILLLDEPSAHLDpVTLQI--------IRKTLkqsfsNCTVILSEH 1410
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-211 |
1.37e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.51 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGqrrvLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--------- 68
Cdd:PRK10070 35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaELRevrrkkiam 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 69 ----IGYVPQKLYLDTTLplTVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVL 144
Cdd:PRK10070 111 vfqsFALMPHMTVLDNTA--FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGAPEVVSMHP 211
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILNNP 256
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-152 |
1.98e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 10 VSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLV-----RVVLGLVAADEGVIkrNG-------QLRIGYVPQK-L 76
Cdd:TIGR00956 769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVITGGDRLV--NGrpldssfQRSIGYVQQQdL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 77 YLDTTL---PLTVSRFMRlRPG--TKKE---------DILPALKRVQAghLMNAPMQKLSGGETQRVLLARALLNKPQLL 142
Cdd:TIGR00956 847 HLPTSTvreSLRFSAYLR-QPKsvSKSEkmeyveeviKLLEMESYADA--VVGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170
....*....|.
gi 489125078 143 V-LDEPTQGVD 152
Cdd:TIGR00956 924 LfLDEPTSGLD 934
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-218 |
2.09e-11 |
|
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: 63.49 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 27 LRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LRIGYVPQklyLDTTLPLTVSR-----FMR 91
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisdvhQNMGYCPQ---FDAIDDLLTGRehlylYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 92 LRpGTKKEDIlpalKRVQaghlmNAPMQKL-------------SGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVA 158
Cdd:TIGR01257 2039 LR-GVPAEEI----EKVA-----NWSIQSLglslyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 159 LYDLIDQLRRElDCAVLMVSHDLhlvmaKTDEVLCLNHHICCSGAPEVVSMHPEFISMFG 218
Cdd:TIGR01257 2109 LWNTIVSIIRE-GRAVVLTSHSM-----EECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-197 |
5.03e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 2 TTLVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAD--EGVIKRNGQLRIGYVPQK---- 75
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEErahl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 76 -LYLDTTLPLTV-----SRFMRLRPGTKK--------------EDILPALKRV--QAGHLMNAPMQKLSGGETQR-VLLA 132
Cdd:CHL00131 85 gIFLAFQYPIEIpgvsnADFLRLAYNSKRkfqglpeldpleflEIINEKLKLVgmDPSFLSRNVNEGFSGGEKKRnEILQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 133 RALLNkPQLLVLDEPTQGVDvngqvalydlIDQLRreldcavlMVSHDLHLVMAKTDEVLCLNHH 197
Cdd:CHL00131 165 MALLD-SELAILDETDSGLD----------IDALK--------IIAEGINKLMTSENSIILITHY 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-192 |
8.58e-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: 8.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLglvaadegviKRNGQLRIGYVPQKLYLDTTLPLtvsrfmrlrpgtkke 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------YASGKARLISFLPKFSRNKLIFI--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 100 DILPALKRVQAGHL-MNAPMQKLSGGETQRVLLARALL--NKPQLLVLDEPTQGVDvngQVALYDLIDQLRRELDC--AV 174
Cdd:cd03238 66 DQLQFLIDVGLGYLtLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLH---QQDINQLLEVIKGLIDLgnTV 142
|
170
....*....|....*...
gi 489125078 175 LMVSHDLHlVMAKTDEVL 192
Cdd:cd03238 143 ILIEHNLD-VLSSADWII 159
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-204 |
1.05e-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: 61.57 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 17 RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LRIGYVPQK--LYLDTTLPL 84
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrQSLGMCPQHniLFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 TVSRFMRLRPGTKKE---DILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYD 161
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489125078 162 LIDQLRRELdcAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGAP 204
Cdd:TIGR01257 1103 LLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQgRLYCSGTP 1144
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-196 |
1.72e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY-GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ---------LR--IGYV 72
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvLRqgVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQ-------KLYLDTTLPLTVSrfmrlrpgtkKEDILPALKRVQAGHL-------MNAPM----QKLSGGETQRVLLARA 134
Cdd:PRK10790 421 QQdpvvladTFLANVTLGRDIS----------EEQVWQALETVQLAELarslpdgLYTPLgeqgNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 135 LLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDLHLVMaKTDEVLCLNH 196
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIV-EADTILVLHR 549
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-207 |
8.43e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.69 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQ-RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----------QLR--IG 70
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqGIRklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YV---PQKLYLDTTLPLTVS---RFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVL 144
Cdd:PRK13644 81 IVfqnPETQFVGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAkTDEVLCLNH-HICCSGAPEVV 207
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRgKIVLEGEPENV 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
120-181 |
1.13e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.13e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 120 KLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSEL 464
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-191 |
1.14e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 18 RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAD--EGVIKRNGQLR------------IGYVPQKLYLDTTLP 83
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCrfkdirdsealgIVIIHQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 LTVSRFMRLRPGTK-----KEDILPA---LKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNG 155
Cdd:NF040905 95 IAENIFLGNERAKRgvidwNETNRRArelLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEED 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 489125078 156 QVALYDLIDQLRRE-LDCavLMVSHDLHLVMAKTDEV 191
Cdd:NF040905 175 SAALLDLLLELKAQgITS--IIISHKLNEIRRVADSI 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-195 |
1.57e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQR--RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IGY 71
Cdd:PLN03130 1238 IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmDLRkvLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKlyldttlPLTVSRFMR--LRPGTKKED--ILPALKRvqaGHLMNA--------PMQKLSGGET----QRVL--LAR 133
Cdd:PLN03130 1318 IPQA-------PVLFSGTVRfnLDPFNEHNDadLWESLER---AHLKDVirrnslglDAEVSEAGENfsvgQRQLlsLAR 1387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQValydLIDQLRRE--LDCAVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTII-DCDRILVLD 1446
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
120-197 |
1.81e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 120 KLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL---------VM----- 185
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMlsqwadkinVLycgqt 237
|
90
....*....|....*
gi 489125078 186 ---AKTDEVLCLNHH 197
Cdd:PRK15093 238 vetAPSKELVTTPHH 252
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-152 |
2.27e-09 |
|
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: 57.65 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQlrIGYVPQKLYL-DTTLPLTVSRFMRLRPGTKK 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQAWIqNDSLRENILFGKALNEKYYQ 731
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 99 E-----------DILPALKRVQAGHlmnaPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:TIGR00957 732 QvleacallpdlEILPSGDRTEIGE----KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-194 |
3.16e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 7 LENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ----------LR--IGYVPQ 74
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskeaLEngISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYLdtTLPLTVSRFMRL-RPGTK-----------------KE---DILPALKrvqaghlmnapMQKLSGGETQRVLLAR 133
Cdd:PRK10982 81 ELNL--VLQRSVMDNMWLgRYPTKgmfvdqdkmyrdtkaifDEldiDIDPRAK-----------VATLSVSQMQMIEIAK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489125078 134 ALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMAKTDEVLCL 194
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-180 |
3.81e-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: 53.92 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 29 PGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIkrngqlrigyvpqkLYLDTtlpltvsrfmrlrpgtkkEDILPALKRV 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------IYIDG------------------EDILEEVLDQ 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 109 QAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLID-----QLRRELDCAVLMVSHD 180
Cdd:smart00382 49 LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTND 125
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-195 |
4.93e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IG 70
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltDLRrvLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 71 YVPQKlyldttlPLTVSRFMR--LRPGTKKED--ILPALKRVQAGHLM-NAPM----QKLSGGET----QRVLL--ARAL 135
Cdd:PLN03232 1314 IIPQS-------PVLFSGTVRfnIDPFSEHNDadLWEALERAHIKDVIdRNPFgldaEVSEGGENfsvgQRQLLslARAL 1386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 136 LNKPQLLVLDEPTQGVDVNGQvalyDLIDQLRRE--LDCAVLMVSHDLHLVMaKTDEVLCLN 195
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTD----SLIQRTIREefKSCTMLVIAHRLNTII-DCDKILVLS 1443
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-181 |
6.74e-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: 55.25 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAdEGVIKRNG---------QLR--IGY 71
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGvswnsvplqKWRkaFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 72 VPQKLYLdttlpLTVSRFMRLRPGTK--KEDILPALKRVQAGHLMNA-PMQ----------KLSGGETQRVLLARALLNK 138
Cdd:cd03289 82 IPQKVFI-----FSGTFRKNLDPYGKwsDEEIWKVAEEVGLKSVIEQfPGQldfvlvdggcVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489125078 139 PQLLVLDEPTQGVD-VNGQValydlidqLRREL-----DCAVLMVSHDL 181
Cdd:cd03289 157 AKILLLDEPSAHLDpITYQV--------IRKTLkqafaDCTVILSEHRI 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-229 |
7.45e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 119 QKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLNHHI 198
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNNPD 1435
|
90 100 110
....*....|....*....|....*....|.
gi 489125078 199 CCSGAPEVVSMHPEFISMfgqrgaeQLGIYR 229
Cdd:PTZ00265 1436 RTGSFVQAHGTHEELLSV-------QDGVYK 1459
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-181 |
1.23e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.33 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 9 NVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGViKRNGQLRIGYVPQKLYLDTTL------ 82
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGGRSIFNYRDVLEfrrrvg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 -------PLTVSRFMRLRPGTKKEDILP---------------ALKRVQAGHLMNAPMqKLSGGETQRVLLARALLNKPQ 140
Cdd:PRK14271 105 mlfqrpnPFPMSIMDNVLAGVRAHKLVPrkefrgvaqarltevGLWDAVKDRLSDSPF-RLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489125078 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNL 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-184 |
1.99e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRR---VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLV--AADEGVIKRNGqlrIGYVPQKLYL- 78
Cdd:PLN03232 615 ISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELshAETSSVVIRGS---VAYVPQVSWIf 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 DTTLPLTV--------SRFMRLRPGTKKE---DILPALKRVQAGHL-MNapmqkLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:PLN03232 692 NATVRENIlfgsdfesERYWRAIDVTALQhdlDLLPGRDLTEIGERgVN-----ISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489125078 147 PTQGVDVNGQVALYD--LIDQLRREldcAVLMVSHDLHLV 184
Cdd:PLN03232 767 PLSALDAHVAHQVFDscMKDELKGK---TRVLVTNQLHFL 803
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
115-182 |
2.98e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 2.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489125078 115 NAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIdqlrRELDCAVLMVSHDLH 182
Cdd:PRK15064 150 YGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHDRH 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-152 |
3.39e-08 |
|
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: 52.26 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRV----LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVaadEGVIKRNGQLRIGYVPQKlyld 79
Cdd:cd03233 3 TLSWRNISFTTGKGRSkipiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNGIPYK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 80 ttlpltvsRFMRLRPGT----KKEDILPALKRVQagHLM--------NAPMQKLSGGETQRVLLARALLNKPQLLVLDEP 147
Cdd:cd03233 76 --------EFAEKYPGEiiyvSEEDVHFPTLTVR--ETLdfalrckgNEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
....*
gi 489125078 148 TQGVD 152
Cdd:cd03233 146 TRGLD 150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-152 |
4.08e-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: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 17 RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVL----GLVAADEGVIKRNGQLRIGYVPQK----LY---LDTTLP-L 84
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYrgdvVYnaeTDVHFPhL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 TVSRFM----RLR-PGTKKEDIlpaLKRVQAGHLMNAPMQKL------------------SGGETQRVLLARALLNKPQL 141
Cdd:TIGR00956 154 TVGETLdfaaRCKtPQNRPDGV---SREEYAKHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 489125078 142 LVLDEPTQGVD 152
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-182 |
4.71e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSY---GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAA--DEGVIKRNgqlRIGYVPQKLYL- 78
Cdd:PLN03130 615 ISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrsDASVVIRG---TVAYVPQVSWIf 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 -----DTTL---PLTVSRFMRLRPGTKKE---DILPALKRVQAGHL-MNapmqkLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:PLN03130 692 natvrDNILfgsPFDPERYERAIDVTALQhdlDLLPGGDLTEIGERgVN-----ISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190
....*....|....*....|....*....|....*...
gi 489125078 147 PTQGVD--VNGQVALYDLIDQLRREldcAVLMVSHDLH 182
Cdd:PLN03130 767 PLSALDahVGRQVFDKCIKDELRGK---TRVLVTNQLH 801
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-155 |
5.61e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQ-----------LRIGYV 72
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfmAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 73 PQ-KLYLDTTLPLTV-----SRFMRLRPGTkkedilpALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDE 146
Cdd:PRK13543 91 PGlKADLSTLENLHFlcglhGRRAKQMPGS-------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*....
gi 489125078 147 PTQGVDVNG 155
Cdd:PRK13543 164 PYANLDLEG 172
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-154 |
5.61e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVvLGLVAADEgvIKRNGQlrIGYVPQKLYLDTTLPL 84
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRY-MAMHAIDG--IPKNCQ--ILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 85 --------------------------------TVSRFMRLRPGTKKEDILPAL----KRVQ---------------AGHL 113
Cdd:PLN03073 253 qcvlntdiertqlleeeaqlvaqqrelefeteTGKGKGANKDGVDKDAVSQRLeeiyKRLElidaytaearaasilAGLS 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489125078 114 MNAPMQK-----LSGGETQRVLLARALLNKPQLLVLDEPTQGVDVN 154
Cdd:PLN03073 333 FTPEMQVkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-184 |
6.22e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTTlPLTVSRFMRLRPGTKKE 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLT-GIENIEFKMLCMGFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 100 DILPALKRV----QAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEptqGVDVNGQVALYDLIDQLR--RELDCA 173
Cdd:PRK13546 119 EIKAMTPKIiefsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCLDKIYefKEQNKT 195
|
170
....*....|.
gi 489125078 174 VLMVSHDLHLV 184
Cdd:PRK13546 196 IFFVSHNLGQV 206
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-184 |
2.54e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 2.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489125078 117 PMQKLSGGETQRVLLARALLN---KPQLLVLDEPTQGV---DVNGQV-ALYDLIDQLRreldcAVLMVSHDLHLV 184
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIyVLQSLTHQGH-----TVVIIEHNMHVV 875
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-182 |
2.66e-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: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLR---------------IGYVPQKLYL-DTTL- 82
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLlNATVe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 -------PLTVSRFM------RLRPGTkkeDILPALKRVQAGHL-MNapmqkLSGGETQRVLLARALLNKPQLLVLDEPT 148
Cdd:cd03290 97 enitfgsPFNKQRYKavtdacSLQPDI---DLLPFGDQTEIGERgIN-----LSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|....*
gi 489125078 149 QGVDVN-GQVALYDLIDQLRRELDCAVLMVSHDLH 182
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-196 |
3.14e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 19 VLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKrnGQLRIGYVPQKLYL------DTTLPLTVSRFMRL 92
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQQAWImnatvrGNILFFDEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 93 RPGTKKEDILPALKRVQAGhLMNAPMQK---LSGGETQRVLLARALLNKPQLLVLDEPTQGVDVN-GQVALYDLIdqlRR 168
Cdd:PTZ00243 753 ADAVRVSQLEADLAQLGGG-LETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECF---LG 828
|
170 180
....*....|....*....|....*....
gi 489125078 169 ELDCAV-LMVSHDLHLVmAKTDEVLCLNH 196
Cdd:PTZ00243 829 ALAGKTrVLATHQVHVV-PRADYVVALGD 856
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-181 |
5.72e-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: 48.12 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 17 RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIG-YVPQklyldttlpltvsrfmrlrpg 95
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGcIVAA--------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 96 tkkEDILPALKRVQaghlmnapmqkLSGGETQRV----LLARALLNKPQLLVLDEPTQGVD-VNGQVALYDLIDQLRRel 170
Cdd:cd03227 67 ---VSAELIFTRLQ-----------LSGGEKELSalalILALASLKPRPLYILDEIDRGLDpRDGQALAEAILEHLVK-- 130
|
170
....*....|.
gi 489125078 171 DCAVLMVSHDL 181
Cdd:cd03227 131 GAQVIVITHLP 141
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
113-181 |
5.90e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 5.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489125078 113 LMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-182 |
6.62e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQRRV-LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQK-LYLDTTL 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 83 PLTVSRFMRLRpGTKKEDILPA-----LKRVQAGH--------LMNApmqKLSGGETQRVLLARALLNKPQLLVLDEPTQ 149
Cdd:PRK10522 403 FTDFHLFDQLL-GPEGKPANPAlvekwLERLKMAHkleledgrISNL---KLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190
....*....|....*....|....*....|...
gi 489125078 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLH 182
Cdd:PRK10522 479 DQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH 511
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-179 |
9.17e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGL--VAADEGVIKRNGQLRIGYVPQK-----L 76
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDragegI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 77 YLDTTLPLTVsrfmrlrPGTKKEDIL-------------PALKRVQAGHLMNAPMQKL---------------SGGETQR 128
Cdd:PRK09580 81 FMAFQYPVEI-------PGVSNQFFLqtalnavrsyrgqEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489125078 129 V-LLARALLnKPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
Cdd:PRK09580 154 NdILQMAVL-EPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTH 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-224 |
1.07e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKLYLDTTlPLTVSRFMRLRPGTKKE 99
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLT-GIENIELKGLMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 100 DILPALKRV----QAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEptqGVDVNGQVALYDLIDQLR--RELDCA 173
Cdd:PRK13545 119 KIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMNefKEQGKT 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489125078 174 VLMVSHDLHLVMAKTDEVLCLNH-HICCSG-APEVVSMHPEFISMFGQRGAEQ 224
Cdd:PRK13545 196 IFFISHSLSQVKSFCTKALWLHYgQVKEYGdIKEVVDHYDEFLKKYNQMSVEE 248
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-242 |
1.15e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 15 GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNGQLRIGYVPQKlyldtTLPLTVS------- 87
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQE-----TPALPQPaleyvid 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 88 --RFMR-----LRPGTKKED---------ILPALK----RVQAGHLMNA----------PMQKLSGGETQRVLLARALLN 137
Cdd:PRK10636 87 gdREYRqleaqLHDANERNDghaiatihgKLDAIDawtiRSRAASLLHGlgfsneqlerPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 138 KPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHDLHLVMAKTDEVLclnhHICCSGAPEVVSMHPEFISMF 217
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWL----EKWLKSYQGTLILISHDRDFLDPIVDKII----HIEQQSLFEYTGNYSSFEVQR 238
|
250 260
....*....|....*....|....*
gi 489125078 218 GQRGAEQLGIYRHNHNHRHDLQGRI 242
Cdd:PRK10636 239 ATRLAQQQAMYESQQERVAHLQSYI 263
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
121-184 |
1.45e-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: 47.99 E-value: 1.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489125078 121 LSGGETQRVLLARALLNK---PQLLVLDEPTQGV---DVNgqvalyDLIDQLRRELDC--AVLMVSHDLHLV 184
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVK------KLLEVLQRLVDKgnTVVVIEHNLDVI 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-152 |
1.71e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 18 RVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAAD--EGVIKRNGQ-------LRI-GYVPQKlylDTTLP---- 83
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFpkkqetfARIsGYCEQN---DIHSPqvtv 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 84 ---LTVSRFMRLRPGTKKEDIL----PALKRVQAGHLMNA-----PMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGV 151
Cdd:PLN03140 971 resLIYSAFLRLPKEVSKEEKMmfvdEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
.
gi 489125078 152 D 152
Cdd:PLN03140 1051 D 1051
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-163 |
1.79e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 4 LVSLENVSVSYGQRrVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEG-VIKRNGQLR------IGYVPQKL 76
Cdd:PRK13541 1 MLSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGnIYYKNCNINniakpyCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 77 YLdtTLPLTVsrFMRLRPGTK----KEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGVD 152
Cdd:PRK13541 80 GL--KLEMTV--FENLKFWSEiynsAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
170
....*....|.
gi 489125078 153 VNGQVALYDLI 163
Cdd:PRK13541 156 KENRDLLNNLI 166
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
117-208 |
2.06e-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: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 117 PMQKLSGGETQRVLLARALLNK---PQLLVLDEPTQGV---DVNgqvalyDLIDQLRRELDC--AVLMVSHDLHlVMAKT 188
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIK------KLLEVLQRLVDKgnTVVVIEHNLD-VIKTA 898
|
90 100
....*....|....*....|....*..
gi 489125078 189 DEVLCL-------NHHICCSGAPEVVS 208
Cdd:TIGR00630 899 DYIIDLgpeggdgGGTVVASGTPEEVA 925
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-169 |
1.43e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 14 YGQRRVLSDVSLELRPGKILTLLGPNGAG--KSTLVRVVLGLVA-----------ADEGVIKR----NGQLRIGYVP--- 73
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrpwrf*twcANRRALRRtig*HRPVR*GRREsfs 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 74 --QKLYLdttlpltVSRFMRLRPGTKKEDILPALKRVQAGHLMNAPMQKLSGGETQRVLLARALLNKPQLLVLDEPTQGV 151
Cdd:NF000106 103 grENLYM-------IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170
....*....|....*...
gi 489125078 152 DVNGQVALYDLIDQLRRE 169
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRD 193
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-222 |
2.15e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 8 ENVSVSY--GQRRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG---------QLR--IGYVPQ 74
Cdd:PTZ00243 1312 EGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreigayglrELRrqFSMIPQ 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYL-DTTLPLTVSRF----------------MRLRPGTKKEDIlpaLKRVQAGHLmnapmqKLSGGETQRVLLARALLN 137
Cdd:PTZ00243 1392 DPVLfDGTVRQNVDPFleassaevwaalelvgLRERVASESEGI---DSRVLEGGS------NYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 138 KPQLLVL-DEPTQGVDvngqVALYDLIDQLRRELDCA--VLMVSHDLHLVmAKTDEVLCLNHHICCS-GAPEVVSMHPE- 212
Cdd:PTZ00243 1463 KGSGFILmDEATANID----PALDRQIQATVMSAFSAytVITIAHRLHTV-AQYDKIIVMDHGAVAEmGSPRELVMNRQs 1537
|
250
....*....|....
gi 489125078 213 -FISM---FGQRGA 222
Cdd:PTZ00243 1538 iFHSMveaLGRSEA 1551
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
5-152 |
6.97e-05 |
|
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: 42.58 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVsVSYGqrrvlsdvSLELRPGKILTL-LGPNGAGKSTLV-RVVLGLvAADEGVIKRNGQL--------RIGYVPQ 74
Cdd:cd03277 6 IKLENF-VTYD--------ETEFRPGPSLNMiIGPNGSGKSSIVcAICLGL-GGKPKLLGRAKKVgefvkrgcDEGTIEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 75 KLYLDTT----------LPLT-VSRFMRLRPgtkkEDILPALKRvqaghlmNAPMQKL-----SGGE----TQRVLLARA 134
Cdd:cd03277 76 ELYGNPGniqvdnlcqfLPQDrVGEFAKLSP----IELLVKFRE-------GEQLQELdphhqSGGErsvsTMLYLLSLQ 144
|
170
....*....|....*...
gi 489125078 135 LLNKPQLLVLDEPTQGVD 152
Cdd:cd03277 145 ELTRCPFRVVDEINQGMD 162
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-194 |
8.47e-05 |
|
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: 42.59 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 5 VSLENVSVSYGQ--RRVLSDVSLELRPGKILTLLGPNGAGKSTLVRVVLGLVAADEGVIKRNG----QLRIGYVPQKLYL 78
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 79 DTTLPLTVSRFMR--LRPGTKKED--ILPALKRVQAGHLMNAPMQKL-----SGGET----QRVL--LARALLNKPQLLV 143
Cdd:cd03288 100 ILQDPILFSGSIRfnLDPECKCTDdrLWEALEIAQLKNMVKSLPGGLdavvtEGGENfsvgQRQLfcLARAFVRKSSILI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489125078 144 LDEPTQGVDVNGQVALYDLIdqLRRELDCAVLMVSHDLHLVMaKTDEVLCL 194
Cdd:cd03288 180 MDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTIL-DADLVLVL 227
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-184 |
1.05e-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: 42.21 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 21 SDVSLELRPGkiLTLL-GPNGAGKSTL---VRVVL--------GLVAADEGVIKRNGqlRIGYVPQKLYLDTTLPLTVSR 88
Cdd:cd03240 14 ERSEIEFFSP--LTLIvGQNGAGKTTIieaLKYALtgelppnsKGGAHDPKLIREGE--VRAQVKLAFENANGKKYTITR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 89 FMRLRPG---TKKEDILPALKRvqaghlmnaPMQKLSGGetQRVL--------LARALLNKPQLLVLDEPTQGVDV-NGQ 156
Cdd:cd03240 90 SLAILENvifCHQGESNWPLLD---------MRGRCSGG--EKVLasliirlaLAETFGSNCGILALDEPTTNLDEeNIE 158
|
170 180
....*....|....*....|....*...
gi 489125078 157 VALYDLIDQLRRELDCAVLMVSHDLHLV 184
Cdd:cd03240 159 ESLAEIIEERKSQKNFQLIVITHDEELV 186
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-186 |
1.20e-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: 42.24 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPGKILTLLGPNGAGKSTL--------------------------------VRVVLGL---VAADEGVIKRN 64
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayarqflgqmdkpdVDSIEGLspaIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 65 GQLRIGYVPqklyldttlplTVSRFMRL---RPGTKKEdiLPALKRVQAGHL-MNAPMQKLSGGETQRVLLARALLNKPQ 140
Cdd:cd03270 91 PRSTVGTVT-----------EIYDYLRLlfaRVGIRER--LGFLVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489125078 141 --LLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLVMA 186
Cdd:cd03270 158 gvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA 204
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-150 |
4.41e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 4.41e-04
10 20 30
....*....|....*....|....*....|...
gi 489125078 121 LSGGETQRVLLARALLNKPQ---LLVLDEPTQG 150
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTG 863
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-150 |
4.72e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 4.72e-04
10 20 30
....*....|....*....|....*....|...
gi 489125078 121 LSGGETQRVLLARALLNKPQ---LLVLDEPTQG 150
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTG 859
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
18-56 |
5.27e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 5.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489125078 18 RVLSDVSLELRPgkiLTLL-GPNGAGKSTLVRvVLGLVAA 56
Cdd:COG4637 11 KSLRDLELPLGP---LTVLiGANGSGKSNLLD-ALRFLSD 46
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
20-185 |
5.50e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.34 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 20 LSDVSLELRPgkiLTLL-GPNGAGKSTLVRVVLGLVaadegvikrngQLRIGYVP-QKLYLDTTLPLTVSRFMRLrpGTK 97
Cdd:COG4938 12 FKEAELELKP---LTLLiGPNGSGKSTLIQALLLLL-----------QSNFIYLPaERSGPARLYPSLVRELSDL--GSR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 98 KEDILPALKRVQAG-----------HLMNAPMQKLSGGET------------------------------QR-----VLL 131
Cdd:COG4938 76 GEYTADFLAELENLeilddkskellEQVEEWLEKIFPGKVevdassdlvrlvfrpsgngkriplsnvgsgVSellpiLLA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489125078 132 ARALLNKPQLLVLDEPTQGVDVNGQVALYDLIdqlrreldcaVLMVSHDLHLVM 185
Cdd:COG4938 156 LLSAAKPGSLLIIEEPEAHLHPKAQSALAELL----------AELANSGVQVII 199
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
27-179 |
2.00e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 38.73 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 27 LRPGKILTLLGPNGAGKSTL-----VRVVLGLVAADEGVIKRNgqlrigyVpqkLYLDTTLPL--TVSRFMRLR--PGTK 97
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLalqlaAAVAAGGPWLGRRVPPGK-------V---LYLAAEDDRgeLRRRLKALGadLGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489125078 98 KEDILPALkrvqagHLMNAPMQKLSGGETQRvLLARALLNKPQLLVLDePTQ---GVDVN--GQV-ALYDLIDQLRRELD 171
Cdd:COG3598 80 FADLDGRL------RLLSLAGDLDDTDDLEA-LERAIEEEGPDLVVID-PLArvfGGDENdaEEMrAFLNPLDRLAERTG 151
|
....*...
gi 489125078 172 CAVLMVSH 179
Cdd:COG3598 152 AAVLLVHH 159
|
|
| TsaE |
pfam02367 |
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ... |
27-56 |
2.65e-03 |
|
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).
Pssm-ID: 460540 Cd Length: 127 Bit Score: 37.03 E-value: 2.65e-03
10 20 30
....*....|....*....|....*....|
gi 489125078 27 LRPGKILTLLGPNGAGKSTLVRvvlGLVAA 56
Cdd:pfam02367 18 LKPGDVILLSGDLGAGKTTFTR---GLARG 44
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
121-179 |
2.75e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 2.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489125078 121 LSGGETQ------RVLLARALLNKPQLLVLDEPTQGVDVNGQVALYDLID-QLRRELDC-AVLMVSH 179
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDIpQVIMISH 868
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
27-52 |
3.97e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.99 E-value: 3.97e-03
10 20
....*....|....*....|....*.
gi 489125078 27 LRPGKILTLLGPNGAGKSTLVRVVLG 52
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-47 |
5.16e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.09 E-value: 5.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489125078 5 VSLENVsvsygqrRVLSDVSLELRPGkiLTLL-GPNGAGKSTLV 47
Cdd:pfam13476 1 LTIENF-------RSFRDQTIDFSKG--LTLItGPNGSGKTTIL 35
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
5-48 |
6.16e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.28 E-value: 6.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489125078 5 VSLENVsvsygqrRVLSDVSLELRPGKILTLL-GPNGAGKSTLVR 48
Cdd:COG3950 6 LTIENF-------RGFEDLEIDFDNPPRLTVLvGENGSGKTTLLE 43
|
|
| PrkA |
COG2766 |
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]; |
31-48 |
8.14e-03 |
|
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
Pssm-ID: 442049 [Multi-domain] Cd Length: 675 Bit Score: 37.12 E-value: 8.14e-03
|
| |
