|
Name |
Accession |
Description |
Interval |
E-value |
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-228 |
1.14e-105 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 306.27 E-value: 1.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLND 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 81 SLPLNVERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLY 160
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 161 DLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHHHICCSGAPADIKHHPSYIALFGTATQETLAFY 228
Cdd:PRK09544 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVVSLHPEFISMFGPRGAEQLGIY 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
2.08e-80 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 241.92 E-value: 2.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------KAKKLKIGYVPQ 74
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 KLKLNDSLPLNVE-----------RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:COG1121 83 RAEVDWDFPITVRdvvlmgrygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 144 LDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHHHICCSGAPADIKHHPSYIALFGTA 220
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGGP 238
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-202 |
6.86e-72 |
|
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: 218.94 E-value: 6.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 6 QLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK------LKIGYVPQKLKLN 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSLPLNVERFLKLT--------GKFSQ---QEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPA 148
Cdd:cd03235 81 RDFPISVRDVVLMGlyghkglfRRLSKadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 149 QGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICLHHHICCSG 202
Cdd:cd03235 161 AGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-207 |
1.88e-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: 183.71 E-value: 1.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--KIGYV 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslSRRELarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLklNDSLPLNVE------RF--LKLTGKFSQQE---ILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDL 141
Cdd:COG1120 81 PQEP--PAPFGLTVRelvalgRYphLGLFGRPSAEDreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 142 LVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDgRIVAQGPPEEV 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-209 |
2.52e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 174.87 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKlKIGYVP 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpaEVRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKLNDSlpLNVERFLKLTGKF-------SQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:COG1131 80 QEPALYPD--LTVRENLRFFARLyglprkeARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 147 PAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKH 209
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPDELKA 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-193 |
1.38e-49 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 161.63 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 14 FDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLNDSLPLNVERFLKLt 93
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVAM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 94 GKFSQQ------------EILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYD 161
Cdd:NF040873 81 GRWARRglwrrltrddraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180 190
....*....|....*....|....*....|..
gi 873911691 162 LIDTIRHRfGCAVFMVSHDLHLVMAKTDDVIC 193
Cdd:NF040873 161 LLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-196 |
3.01e-49 |
|
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: 160.29 E-value: 3.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 6 QLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--KIGYVPQ 74
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlaslSPKELarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 klklndslplnverflkltgkfsqqeileALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:cd03214 81 -----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 873911691 155 GQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-207 |
5.75e-47 |
|
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: 155.95 E-value: 5.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------TKAKKL-----KIGYV 72
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkdITKKNLrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQklklN--DSL------------PLNverfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRR 138
Cdd:COG1122 81 FQ----NpdDQLfaptveedvafgPEN----LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 139 PDLLVLDEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICLHHH-ICCSGAPADI 207
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGrIVADGTPREV 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-196 |
2.97e-46 |
|
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: 152.17 E-value: 2.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----------KAKKLKIGYVPQ 74
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkepEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 klklNDSLPLNverflkLTGKfsqqeilealklvgaEHLqksnmhQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:cd03230 81 ----EPSLYEN------LTVR---------------ENL------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 873911691 155 GQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03230 130 SRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNN 170
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-211 |
8.59e-46 |
|
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: 160.07 E-value: 8.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGR-----KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKLK- 68
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltklSRRSLRe 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 ----IGYVPQ--------KLKLNDSlplnVERFLKLTGKFSQQE----ILEALKLVG--AEHLQKSNmHQLSGGENQRVL 130
Cdd:COG1123 340 lrrrVQMVFQdpysslnpRMTVGDI----IAEPLRLHGLLSRAErrerVAELLERVGlpPDLADRYP-HELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 131 IARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKH 209
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDgRIVEDGPTEEVFA 494
|
..
gi 873911691 210 HP 211
Cdd:COG1123 495 NP 496
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-211 |
1.07e-44 |
|
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: 150.51 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------------KAKK 66
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqditglsekelYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 67 LKIGYVPQKLKLNDSLPL--NVERFLKLTGKFSQQEI----LEALKLVG---AEHLQKSnmhQLSGGENQRVLIARSLLR 137
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVfeNVAFPLREHTDLSEAEIrelvLEKLELVGlpgAADKMPS---ELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 138 RPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADgKIIAEGTPEELLASD 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-184 |
9.60e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.51 E-value: 9.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL-----KI 69
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIpylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 70 GYVPQKLKLNDSLPL--NVERFLKLTG---KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:COG2884 82 GVVFQDFRLLPDRTVyeNVALPLRVTGksrKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 873911691 145 DEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLV 184
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELV 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-211 |
1.31e-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: 154.29 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDG--RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL---QTKFSGTITKAKK--------- 66
Cdd:COG1123 1 MTPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 67 --LKIGYVPQ--KLKLNdslPLNVE-------RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSL 135
Cdd:COG1123 81 rgRRIGMVFQdpMTQLN---PVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 136 LRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEILAAP 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-196 |
2.46e-43 |
|
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: 146.50 E-value: 2.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGR----KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------------KAK 65
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllklsrrlrKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 66 KLKIGYVPQ--------KLKLNDSL--PLnveRFLKLTGKFSQQEILEALKLVG---AEHLQKSNMHQLSGGENQRVLIA 132
Cdd:cd03257 81 RKEIQMVFQdpmsslnpRMTIGEQIaePL---RIHGKLSKKEARKEAVLLLLVGvglPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 133 RSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-196 |
4.53e-43 |
|
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: 146.49 E-value: 4.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEF----DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLK 68
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQ--------KLKLNDSL--PLNVERFLKltgkfSQQEILEALKLVG-AEHLQKSNMHQLSGGENQRVLIARSLLR 137
Cdd:COG1124 81 VQMVFQdpyaslhpRHTVDRILaePLRIHGLPD-----REERIAELLEQVGlPPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 138 RPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-212 |
2.27e-41 |
|
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: 141.87 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------------KAKKLKIG 70
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglseaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKLNDSLPL--NVERFLKLTGKFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:cd03261 81 MLFQSGALFDSLTVfeNVAFPLREHTRLSEEEIreivLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 145 DEPAQGVD--VQGQIDlyDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLH-HHICCSGAPADIKHHPS 212
Cdd:cd03261 161 DEPTAGLDpiASGVID--DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYdGKIVAEGTPEELRASDD 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-181 |
6.34e-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: 141.38 E-value: 6.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRK----VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------KAKKLKIG 70
Cdd:COG1116 4 AAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQklklNDSL-P-LNVE-------RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDL 141
Cdd:COG1116 84 VVFQ----EPALlPwLTVLdnvalglELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 873911691 142 LVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDL 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 |
7.30e-41 |
|
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: 139.52 E-value: 7.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 6 QLDSVSVEFDG--RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYV 72
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdltklslKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKlklndslP------LNVE-------RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRP 139
Cdd:cd03225 81 FQN-------PddqffgPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 140 DLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHHH 197
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-211 |
1.61e-40 |
|
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: 140.17 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGT-------ITKAK-----KLK 68
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRilfdgrdITGLPphriaRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IG------------------YVPQKLKLNDSLPLNVERFLKLTGKFSQ--QEILEALKLVGAEHLQKSNMHQLSGGENQR 128
Cdd:COG0411 81 IArtfqnprlfpeltvlenvLVAAHARLGRGLLAALLRLPRARREEREarERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 129 VLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFgRVIAEGTPAEV 240
|
....
gi 873911691 208 KHHP 211
Cdd:COG0411 241 RADP 244
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-209 |
2.33e-40 |
|
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: 138.76 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGR----KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------KAKKLKIGYVPQ 74
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 KLKL--------NDSLPLNVERflkLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:cd03293 81 QDALlpwltvldNVALGLELQG---VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 147 PAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLH--LVMAktDDVICLhhhiccSGAPADIKH 209
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeaVFLA--DRVVVL------SARPGRIVA 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-211 |
5.48e-40 |
|
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: 138.34 E-value: 5.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------------TKAKKLKIGYV 72
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditglppHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLNDSLPL--NV---------ERFLKLTGKFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLR 137
Cdd:cd03219 81 FQIPRLFPELTVleNVmvaaqartgSGLLLARARREEREAreraEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 138 RPDLLVLDEPAQGVDVQGQIDLYDLIDTIRhRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQgRVIAEGTPDEVRNNP 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-194 |
1.66e-39 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 137.52 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSG-------------TITKAKKlK 68
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggeDVWELRK-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSLPLNVERFLkLTGKFS------------QQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLL 136
Cdd:COG1119 80 IGLVSPALQLRFPRDETVLDVV-LSGFFDsiglyreptdeqRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-217 |
9.86e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.92 E-value: 9.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------TKAKKLKIGY 71
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldgrdvtgLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQklklNDSL-P-LNVE-------RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLL 142
Cdd:COG3842 82 VFQ----DYALfPhLTVAenvafglRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 143 VLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLH--LVMAktDDVICLHH-HICCSGAPADIKHHPS--YIALF 217
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLALA--DRIAVMNDgRIEQVGTPEEIYERPAtrFVADF 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-196 |
2.37e-38 |
|
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: 132.31 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-------------KAKKLKIGY 71
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILidgedltdledelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKLndslplnverflkltgkFSQQEILEALklvgaehlqksnMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGV 151
Cdd:cd03229 81 VFQDFAL-----------------FPHLTVLENI------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 873911691 152 DVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-196 |
2.42e-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: 133.41 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------TKAKKLKIGYVPQk 75
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgVPPERRNIGMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 lklNDSL--PLNVE-------RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:cd03259 80 ---DYALfpHLTVAeniafglKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 873911691 147 PAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-180 |
5.12e-38 |
|
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: 132.22 E-value: 5.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----------KAKKLKIGYVP 73
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngepirdarEDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKLNDSLPL--NVERFLKLTG-KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQG 150
Cdd:COG4133 82 HADGLKPELTVreNLRFWAALYGlRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|
gi 873911691 151 VDVQGQIDLYDLIDTIRHRfGCAVFMVSHD 180
Cdd:COG4133 162 LDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-208 |
1.66e-37 |
|
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: 131.90 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKlKIGYV 72
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkeprEARR-QIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLNDSLPL--NVERFLKLTGKFSQQ---EILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:COG4555 80 PDERGLYDRLTVreNIRYFAELYGLFDEElkkRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 148 AQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIK 208
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKgKVVAQGSLDELR 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-195 |
1.29e-36 |
|
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: 126.98 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 6 QLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITkakklkigyvpqklklndslpln 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 86 verflkLTGK-FSQQEILEALKLVGAehlqksnMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLID 164
Cdd:cd00267 58 ------IDGKdIAKLPLEELRRRIGY-------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|.
gi 873911691 165 TIRHRfGCAVFMVSHDLHLVMAKTDDVICLH 195
Cdd:cd00267 125 ELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-206 |
1.88e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 129.47 E-value: 1.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--KIGYV 72
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawSPWELarRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLNdsLPLNVERFLKL-------TGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSL--LRRPD--- 140
Cdd:COG4559 81 PQHSSLA--FPFTVEEVVALgraphgsSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdgg 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 141 --LLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPAD 206
Cdd:COG4559 159 prWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQgRLVAQGTPEE 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-195 |
2.52e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 128.24 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFD----GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL 67
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 ------KIGYVPQKLKLNDSLPL--NVE---RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLL 136
Cdd:COG1136 81 arlrrrHIGFVFQFFNLLPELTAleNVAlplLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLvMAKTDDVICLH 195
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLR 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-217 |
5.48e-36 |
|
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: 127.74 E-value: 5.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKLKIGYVPQK 75
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILldgkditnlPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKLndsLP-LNVE-------RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:cd03300 81 YAL---FPhLTVFeniafglRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873911691 148 AQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP--SYIALF 217
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKgKIQQIGTPEEIYEEPanRFVADF 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-180 |
2.29e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 132.11 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 7 LDSVSVEFDGRKVLDNISLNLERG-RITtLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLNDSLPL- 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRIG-LVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 -----------------------------NVERFLKLTGKFSQQ----------EILEALKLVGAEHLQKsnMHQLSGGE 125
Cdd:COG0488 80 dtvldgdaelraleaeleeleaklaepdeDLERLAELQEEFEALggweaearaeEILSGLGFPEEDLDRP--VSELSGGW 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 126 NQRVLIARSLLRRPDLLVLDEPAQGVDvqgqidlydlIDTIR------HRFGCAVFMVSHD 180
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLD----------LESIEwleeflKNYPGTVLVVSHD 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-180 |
2.70e-35 |
|
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: 125.68 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRK----VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL---- 67
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisklSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 --KIGYVPQKLKLNDSLPL--NVERFLKLTGKFSQQ---EILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPD 140
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTAleNVELPLLLAGVPKKErreRAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 873911691 141 LLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHD 180
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD 200
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-210 |
7.73e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 131.03 E-value: 7.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYV 72
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdldpASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKL-NDSLPLNVeRFLKltGKFSQQEILEALKLVGAEHLQKS-----------NMHQLSGGENQRVLIARSLLRRPD 140
Cdd:COG4988 417 PQNPYLfAGTIRENL-RLGR--PDASDEELEAALEAAGLDEFVAAlpdgldtplgeGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 141 LLVLDEPAQGVDVQGQIDLYDLIDTIRHrfGCAVFMVSHDLHLvMAKTDDVICLHH-HICCSGAPADIKHH 210
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL-LAQADRILVLDDgRIVEQGTHEELLAK 561
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-197 |
9.88e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 9.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKL-----------KIGYVP 73
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKLndsLPLNVERFLKLT-----GKFSQQEILEALKLVG-AEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:COG4619 81 QEPAL---WGGTVRDNLPFPfqlreRKFDRERALELLERLGlPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 873911691 148 AQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHHH 197
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-196 |
9.94e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.78 E-value: 9.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL-----K 68
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgqdvtalRGRALrrlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSLP---------LNVERFLK-LTGKFSQQEI---LEALKLVG-AEHLQKSnMHQLSGGENQRVLIARS 134
Cdd:COG3638 82 IGMIFQQFNLVPRLSvltnvlagrLGRTSTWRsLLGLFPPEDReraLEALERVGlADKAYQR-ADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 135 LLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-196 |
1.04e-33 |
|
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: 119.80 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGR--KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGY 71
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdldlESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKL-NDSLplnverflkltgkfsqqeilealklvgaehlqKSNMhqLSGGENQRVLIARSLLRRPDLLVLDEPAQG 150
Cdd:cd03228 81 VPQDPFLfSGTI--------------------------------RENI--LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 873911691 151 VDVQGQIDLYDLIDTIRHrfGCAVFMVSHDLHLVMaKTDDVICLHH 196
Cdd:cd03228 127 LDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-196 |
1.30e-33 |
|
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: 121.53 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGR----KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--- 67
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 --KIGYVPQKLKLNDSLPL--NVERFLKLTG---KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPD 140
Cdd:cd03258 81 rrRIGMIFQHFNLLSSRTVfeNVALPLEIAGvpkAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 141 LLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-227 |
1.42e-33 |
|
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: 122.56 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDG-----RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--- 67
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTidgrditakKKKKLkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 --KIGYVPQ--------KLKLNDSL--PLNVerflkltgKFSQQEIL----EALKLVG-AEHLQKSNMHQLSGGENQRVL 130
Cdd:TIGR04521 81 rkKVGLVFQfpehqlfeETVYKDIAfgPKNL--------GLSEEEAEervkEALELVGlDEEYLERSPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 131 IARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKH 209
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDGTPREVFS 232
|
250
....*....|....*...
gi 873911691 210 HPSYIALFGTATQETLAF 227
Cdd:TIGR04521 233 DVDELEKIGLDVPEITEL 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-184 |
1.53e-33 |
|
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: 123.62 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGR----KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL---QTKFSGTIT---------KAKKL 67
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILfdgedllklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 ------KIGYVPQ--------KLKLNDSL--PLnvERFLKLTGKFSQQEILEALKLVG----AEHLqksNM--HQLSGGE 125
Cdd:COG0444 81 rkirgrEIQMIFQdpmtslnpVMTVGDQIaePL--RIHGGLSKAEARERAIELLERVGlpdpERRL---DRypHELSGGM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 126 NQRVLIARSLLRRPDLLVLDEPAQGVDV--QGQIdLyDLIDTIRHRFGCAVFMVSHDLHLV 184
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVtiQAQI-L-NLLKDLQRELGLAILFITHDLGVV 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-194 |
1.61e-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: 120.44 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 6 QLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------TKAKKL--KIGYVPQKL 76
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpIKAKERrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 77 KLN---DSLPLNVERFLKLTGKfSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDV 153
Cdd:cd03226 81 DYQlftDSVREELLLGLKELDA-GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 873911691 154 QGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:cd03226 160 KNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-192 |
3.89e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.95 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQK---LKL 78
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHqeeLDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 79 NDSLPLNVERFLKLTGKFSQQEILEALKLVGAEHLQKsnMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQgvdvqgqid 158
Cdd:COG0488 393 DKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKP--VGVLSGGEKARLALAKLLLSPPNVLLLDEPTN--------- 461
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 873911691 159 lyDL-IDTIR------HRFGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:COG0488 462 --HLdIETLEaleealDDFPGTVLLVSHDRYFLDRVATRIL 500
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-147 |
4.98e-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: 117.36 E-value: 4.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYVPQKLKLNDSLP----- 83
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQDPQLFPRLTvrenl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 84 LNVERFLKLTGKFSQQEILEALKLVGAEHL----QKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-206 |
7.07e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 120.26 E-value: 7.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--KIGYV 72
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladwSPAELarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLndSLPLNVE---RFLKLTGKFSQQE----ILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSL--LRRPD--- 140
Cdd:PRK13548 82 PQHSSL--SFPFTVEevvAMGRAPHGLSRAEddalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqLWEPDgpp 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 141 -LLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPAD 206
Cdd:PRK13548 160 rWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQgRLVADGTPAE 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-207 |
1.57e-32 |
|
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: 118.82 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL-----KI 69
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklKGKALrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 70 GYVPQKLKLNDSLP---------LNVERFLK-LTGKFSQQEI---LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLL 136
Cdd:cd03256 81 GMIFQQFNLIERLSvlenvlsgrLGRRSTWRsLFGLFPKEEKqraLAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDgRIVFDGPPAEL 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-209 |
4.36e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 117.15 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-------TKAK-----KLKIGYV 72
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrdiTGLPpheraRAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQklklndslplnvERFLkltgkFSQQEILEALkLVGAEHLQKSN------------------MHQ----LSGGENQRVL 130
Cdd:cd03224 81 PE------------GRRI-----FPELTVEENL-LLGAYARRRAKrkarlervyelfprlkerRKQlagtLSGGEQQMLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 131 IARSLLRRPDLLVLDEPAQG-----VDvqgqiDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAP 204
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGlapkiVE-----EIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERgRVVLEGTA 216
|
....*
gi 873911691 205 ADIKH 209
Cdd:cd03224 217 AELLA 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-208 |
1.04e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 118.29 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-------KAKKLKIGYVP---- 73
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldPEDRRRIGYLPeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 --QKLKLNDSLplnvERFLKLTG---KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPA 148
Cdd:COG4152 82 lyPKMKVGEQL----VYLARLKGlskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 149 QGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIK 208
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKgRKVLSGSVDEIR 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-197 |
1.92e-31 |
|
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: 113.31 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPqklklndslpl 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 nverflkltgkfsqqeilealklvgaehlqksnmhQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLID 164
Cdd:cd03221 70 -----------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|...
gi 873911691 165 TirhrFGCAVFMVSHDLHLVMAKTDDVICLHHH 197
Cdd:cd03221 115 E----YPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-208 |
4.99e-31 |
|
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: 114.39 E-value: 4.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAK----------KLKIGYVPQ 74
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 KLKLNDSLPL--NVERFLKLTG---KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQ 149
Cdd:cd03265 81 DLSVDDELTGweNLYIHARLYGvpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 150 GVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIK 208
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEGTPEELK 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-194 |
7.41e-31 |
|
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: 112.14 E-value: 7.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLKIGYV 72
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILvdgkevsfasprDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 pqklklndslplnverflkltgkfsqqeilealklvgaehlqksnmHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVD 152
Cdd:cd03216 81 ----------------------------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 873911691 153 VQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:cd03216 115 PAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-195 |
1.65e-30 |
|
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: 112.70 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITkakklkigyVPQKLKLNDSLPL 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT---------FDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 NV----------------ERFLKLTGK---FSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLD 145
Cdd:cd03268 72 RRigalieapgfypnltaRENLRLLARllgIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 873911691 146 EPAQGVDVQGQIDLYDLIDTIRhRFGCAVFMVSHDLHLVMAKTDDVICLH 195
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-195 |
1.70e-30 |
|
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: 112.76 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-------TKAKKLKIGYVP---- 73
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYLPeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 --QKLKLNDSLpLNVERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGV 151
Cdd:cd03269 81 lyPKMKVIDQL-VYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 873911691 152 DVQGQIDLYDLIDTIRhRFGCAVFMVSHDLHLVMAKTDDVICLH 195
Cdd:cd03269 160 DPVNVELLKDVIRELA-RAGKTVILSTHQMELVEELCDRVLLLN 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-152 |
3.24e-30 |
|
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: 111.90 E-value: 3.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGrITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------KAKKL--KIGYVPQ 74
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQKLrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 KLKLNDSLPlnVERFLK-------LTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:cd03264 80 EFGVYPNFT--VREFLDyiawlkgIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
....*
gi 873911691 148 AQGVD 152
Cdd:cd03264 158 TAGLD 162
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-217 |
4.43e-30 |
|
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: 112.38 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-------TKAK-----KLKI 69
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrfdgediTGLPphriaRLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 70 GYVPQklklndslplnvER--FLKLT-------------GKFSQQEILEAL-----KLvgAEHL-QKSNmhQLSGGENQR 128
Cdd:COG0410 81 GYVPE------------GRriFPSLTveenlllgayarrDRAEVRADLERVyelfpRL--KERRrQRAG--TLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 129 VLIARSLLRRPDLLVLDEPAQG-----VDvqgqiDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSG 202
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERgRIVLEG 218
|
250
....*....|....*
gi 873911691 203 APADIKHHPSYIALF 217
Cdd:COG0410 219 TAAELLADPEVREAY 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-194 |
4.48e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLK 68
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrsprDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLndsLP-LNVE------RFLKLTGKFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLR 137
Cdd:COG1129 81 IAIIHQELNL---VPnLSVAeniflgREPRRGGLIDWRAMrrraRELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 138 RPDLLVLDEP-----AQGVDVqgqidLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:COG1129 158 DARVLILDEPtasltEREVER-----LFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-196 |
4.83e-30 |
|
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: 118.01 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSveF----DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----KAKKL-------KI 69
Cdd:COG2274 474 IELENVS--FrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgiDLRQIdpaslrrQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 70 GYVPQKLKL-NDSLPLNverfLKLTGK-FSQQEILEALKLVGAE----------HLQKSNM-HQLSGGENQRVLIARSLL 136
Cdd:COG2274 552 GVVLQDVFLfSGTIREN----ITLGDPdATDEEIIEAARLAGLHdfiealpmgyDTVVGEGgSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHrfGCAVFMVSHDLHLVmAKTDDVICLHH 196
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDK 684
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-210 |
5.06e-30 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 112.39 E-value: 5.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL-----K 68
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtditklRGKKLrklrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSLP---------LNVERFLK-LTGKFSQQEI---LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSL 135
Cdd:TIGR02315 81 IGMIFQHYNLIERLTvlenvlhgrLGYKPTWRsLLGRFSEEDKeraLSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 136 LRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHH 210
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAgEIVFDGAPSELDDE 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-212 |
5.92e-30 |
|
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: 112.04 E-value: 5.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 19 VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKLKIGYVPQKLKL--NDSLPLNVE 87
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnlPPEKRDISYVPQNYALfpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 88 ---RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLID 164
Cdd:cd03299 94 yglKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 873911691 165 TIRHRFGCAVFMVSHDLHLVMAKTDDV-ICLHHHICCSGAPADIKHHPS 212
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVaIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-207 |
1.67e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 111.75 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDG--RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-------KAKKL-----KIG 70
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgldtlDEENLweirkKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQklklNdslPLN------VER---FlkltG----KFSQQEIL----EALKLVGAEHLQKSNMHQLSGGENQRVLIAR 133
Cdd:TIGR04520 81 MVFQ----N---PDNqfvgatVEDdvaF----GlenlGVPREEMRkrvdEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 134 SLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDL-HLVMAktDDVICLHH-HICCSGAPADI 207
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeEAVLA--DRVIVMNKgKIVAEGTPREI 223
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-194 |
2.35e-29 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 109.63 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 7 LDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSG----------TITKAKKL-----KIGY 71
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGqvylngqetpPLNSKKASkfrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKL--------NDSLPLnveRFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:TIGR03608 81 LFQNFALienetveeNLDLGL---KYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 873911691 144 LDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLhLVMAKTDDVICL 194
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-208 |
3.55e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 109.52 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 13 EFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----------KAKKLKIGYVPQKlklnDSL 82
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrKAARQSLGYCPQF----DAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 P--LNVER----FLKLTGKFSQQEILEA---LKLVGAEHLQKSNMHQLSGGeNQRVL-IARSLLRRPDLLVLDEPAQGVD 152
Cdd:cd03263 87 FdeLTVREhlrfYARLKGLPKSEIKEEVellLRVLGLTDKANKRARTLSGG-MKRKLsLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 153 VQGQIDLYDLIDTIRHrfGCAVFMVSHDLHLVmaktdDVICLHHHI------CCSGAPADIK 208
Cdd:cd03263 166 PASRRAIWDLILEVRK--GRSIILTTHSMDEA-----EALCDRIAImsdgklRCIGSPQELK 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-225 |
1.24e-28 |
|
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: 111.35 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 22 NISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------------KAKKLKIGYVPQklklNDSL-P-L 84
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflPPHRRRIGYVFQ----EARLfPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 NVERFLKLTGKFS-----QQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDL 159
Cdd:COG4148 93 SVRGNLLYGRKRApraerRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 160 YDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPSYIALFGTATQETL 225
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQgRVVASGPLAEVLSRPDLLPLAGGEEAGSV 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-211 |
1.34e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.93 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------TKAKKLKIGYVPQk 75
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrdvtdLPPKDRNIAMVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 lklNDSL-P-LNVER---F-LKLTgKFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLD 145
Cdd:COG3839 83 ---SYALyPhMTVYEniaFpLKLR-KVPKAEIdrrvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 146 EPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDgRIQQVGTPEELYDRP 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-212 |
1.74e-28 |
|
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: 108.20 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKLKIGYVPQK 75
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedatdvPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKLNDSLPL--NVE---RFLKLTGKFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:cd03296 83 YALFRHMTVfdNVAfglRVKPRSERPPEAEIrakvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 147 PAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPS 212
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKgRIEQVGTPDEVYDHPA 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-196 |
1.86e-28 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 107.72 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFD-GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKL--------------K 68
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvnrlrgrqlpllrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKL--------NDSLPLNVERflkLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPD 140
Cdd:TIGR02673 81 IGVVFQDFRLlpdrtvyeNVALPLEVRG---KKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 141 LLVLDEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-213 |
2.48e-28 |
|
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: 112.94 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDG--RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----KAKKL-------KIGY 71
Cdd:COG4987 334 LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvDLRDLdeddlrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKL-NDSLPLNverfLKLT-GKFSQQEILEALKLVGAEHLQKSNMH-----------QLSGGENQRVLIARSLLRR 138
Cdd:COG4987 414 VPQRPHLfDTTLREN----LRLArPDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 139 PDLLVLDEPAQGVDVQ--GQIdLYDLIDTIRHRfgcAVFMVSHDLHLvMAKTDDVICL-HHHICCSGAPADIKHHPSY 213
Cdd:COG4987 490 APILLLDEPTEGLDAAteQAL-LADLLEALAGR---TVLLITHRLAG-LERMDRILVLeDGRIVEQGTHEELLAQNGR 562
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-181 |
2.81e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 108.25 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK------LKIGYVPQKLK 77
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 78 LndsLPL-----NVERFLKLTGKFSQQEI---LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQ 149
Cdd:PRK11248 81 L---LPWrnvqdNVAFGLQLAGVEKMQRLeiaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|..
gi 873911691 150 GVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDL 181
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-196 |
4.26e-28 |
|
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: 106.57 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------TKAKKLKIGYVPQK 75
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKL--NDSLPLNVERFLKLTgKFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQ 149
Cdd:cd03301 81 YALypHMTVYDNIAFGLKLR-KVPKDEIdervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 873911691 150 GVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-217 |
4.35e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.04 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLN-- 79
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNtv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 -DSLPL--------NVERFLKLTgKFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:PRK09452 92 fQSYALfphmtvfeNVAFGLRMQ-KTPAAEItprvMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 147 PAQGVD----VQGQIDLYDLIDTIRHRFgcaVFmVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPS--YIALF 217
Cdd:PRK09452 171 SLSALDyklrKQMQNELKALQRKLGITF---VF-VTHDQEEALTMSDRIVVMRDgRIEQDGTPREIYEEPKnlFVARF 244
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-182 |
9.74e-28 |
|
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: 106.11 E-value: 9.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-----QTKFSGTIT-------------KAKK 66
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLldgkdiydldvdvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 67 LKIGYVPQKLKLndsLPL----NVERFLKLTGKFSQQEI----LEALKLVG--AEHLQKSNMHQLSGGENQRVLIARSLL 136
Cdd:cd03260 81 RRVGMVFQKPNP---FPGsiydNVAYGLRLHGIKLKEELdervEEALRKAAlwDEVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFgcAVFMVSHDLH 182
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQ 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-196 |
9.84e-28 |
|
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: 105.57 E-value: 9.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL-----KIGYVPQKLKLNDS 81
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlRGRAIpylrrKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 82 LPL--NVERFLKLTG---KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQ 156
Cdd:cd03292 93 RNVyeNVAFALEVTGvppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 873911691 157 IDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03292 173 WEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-212 |
1.48e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.27 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-------TKA--KKLKIGYV 72
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvTHRsiQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKL--NDSLPLNVERFLKLTGKFS---QQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:PRK11432 84 FQSYALfpHMSLGENVGYGLKMLGVPKeerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 148 AQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPS 212
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKgKIMQIGSPQELYRQPA 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-196 |
1.74e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.25 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSveF---DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--KIG 70
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLESLrrQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKL-NDSLPLNVeRFLKLtgKFSQQEILEALKLVGAEHLQKS-----------NMHQLSGGENQRVLIARSLLRR 138
Cdd:COG1132 418 VVPQDTFLfSGTIRENI-RYGRP--DATDEEVEEAAKAAQAHEFIEAlpdgydtvvgeRGVNLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 139 PDLLVLDEPAQGVDVQGQIDLYDLIDTIRHrfGCAVFMVSHDLHLVMaKTDDVICLHH 196
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-NADRILVLDD 549
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-217 |
1.84e-27 |
|
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: 105.85 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK-----------LKIGYV 72
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdpvelrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLndsLP-----LNVERFLKLTG---KFSQQEILEALKLVGAE--HLQKSNMHQLSGGENQRVLIARSLLRRPDLL 142
Cdd:cd03295 81 IQQIGL---FPhmtveENIALVPKLLKwpkEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 143 VLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLhlvmaktDDVICLHHHICC--------SGAPADIKHHP--S 212
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDI-------DEAFRLADRIAImkngeivqVGTPDEILRSPanD 230
|
....*
gi 873911691 213 YIALF 217
Cdd:cd03295 231 FVAEF 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-191 |
1.99e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 109.73 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLK 68
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvrirsprDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSLP------LNVERflKLTGKFSQQEILEALKlvgaEHLQKSNM--------HQLSGGENQRVLIARS 134
Cdd:COG3845 82 IGMVHQHFMLVPNLTvaenivLGLEP--TKGGRLDRKAARARIR----ELSERYGLdvdpdakvEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 135 LLRRPDLLVLDEP-----AQGVDvqgqidlyDLIDTIRhRF---GCAVFMVSHDLHLVMAKTDDV 191
Cdd:COG3845 156 LYRGARILILDEPtavltPQEAD--------ELFEILR-RLaaeGKSIIFITHKLREVMAIADRV 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-212 |
2.31e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.86 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKLKIGYVPQK 75
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKL--------NDSLPLNV-ERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:PRK10851 83 YALfrhmtvfdNIAFGLTVlPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 147 PAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPS 212
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQgNIEQAGTPDQVWREPA 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-221 |
2.43e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.39 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYVP 73
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKLndSLPLNVERFLKL-----TGKFSQQE------ILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLL 142
Cdd:PRK09536 84 QDTSL--SFEFDVRQVVEMgrtphRSRFDTWTetdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 143 VLDEPAQGVDVQGQID----LYDLIDTirhrfGCAVFMVSHDLHLVmAKTDDVICL--HHHICCSGAPADIKHHPSYIAL 216
Cdd:PRK09536 162 LLDEPTASLDINHQVRtlelVRRLVDD-----GKTAVAAIHDLDLA-ARYCDELVLlaDGRVRAAGPPADVLTADTLRAA 235
|
....*
gi 873911691 217 FGTAT 221
Cdd:PRK09536 236 FDART 240
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1-207 |
3.12e-27 |
|
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: 105.05 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQldsvsvEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLK 68
Cdd:TIGR04406 4 AENLIK------SYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILidgqdithlpmhERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQ------KLKLNDSLPLNVERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLL 142
Cdd:TIGR04406 78 IGYLPQeasifrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 143 VLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDgKVLAEGTPAEI 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-211 |
4.96e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.77 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----------TKAKKLKIGYVPQ 74
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngrdlftnLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 klklNDSL-P-LNVE-------RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLD 145
Cdd:COG1118 83 ----HYALfPhMTVAeniafglRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 146 EPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQgRIEQVGTPDEVYDRP 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-194 |
5.44e-27 |
|
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: 108.91 E-value: 5.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGR-KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-----------TKAKKLKIGYV 72
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQK-LKLNDSLPLNVeRFLKLTGkfSQQEILEALKLVGAEHLQK-----------SNMHQLSGGENQRVLIARSLLRRPD 140
Cdd:TIGR02857 402 PQHpFLFAGTIAENI-RLARPDA--SDAEIREALERAGLDEFVAalpqgldtpigEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 141 LLVLDEPAQGVDVQGQIDLYDLIDTIRHrfGCAVFMVSHDLHLvMAKTDDVICL 194
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-196 |
5.73e-27 |
|
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: 104.34 E-value: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 19 VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAkklkiGYVP----------------QK------L 76
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-----GLVPwkrrkkflrrigvvfgQKtqlwwdL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 77 KLNDSLPLNVERFLKLTGKFSQ--QEILEALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKrlDELSELLDL---EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 873911691 155 GQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-196 |
7.47e-27 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 102.51 E-value: 7.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLKIGYVPQklklndslp 83
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgkpvtrrsprDAIRAGIAYVPE--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 lnvERflKLTGKFSQQEILEalklvgaehlqksNM---HQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLY 160
Cdd:cd03215 83 ---DR--KREGLVLDLSVAE-------------NIalsSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 873911691 161 DLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03215 145 RLIRELADA-GKAVLLISSELDELLGLCDRILVMYE 179
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-179 |
1.25e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.97 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKL-N 79
Cdd:COG4178 360 DGALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLpL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSL------PLNVERFlkltgkfSQQEILEALKLVGAEHL-----QKSN-MHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:COG4178 440 GTLreallyPATAEAF-------SDAELREALEAVGLGHLaerldEEADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|..
gi 873911691 148 AQGVDVQGQIDLYDLIdtIRHRFGCAVFMVSH 179
Cdd:COG4178 513 TSALDEENEAALYQLL--REELPGTTVISVGH 542
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-211 |
1.26e-26 |
|
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: 103.39 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 14 FDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLKIGYVPQ------K 75
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditklpmhKRARLGIGYLPQeasifrK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKLNDSLpLNVERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQG 155
Cdd:cd03218 90 LTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 156 QIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:cd03218 169 VQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEgKVLAEGTPEEIAANE 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-181 |
2.04e-26 |
|
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: 102.37 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 12 VEFDGRKVLDNISLNLE---RGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------------TKAKKLKIGYVP 73
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKL--NDSLPLNVERFLKLTG----KFSQQEILEALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:cd03297 82 QQYALfpHLNVRENLAFGLKRKRnredRISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190
....*....|....*....|....*....|....
gi 873911691 148 AQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDL 181
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDL 192
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-184 |
2.10e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.77 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRK----VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL---- 67
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltalSERELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 -KIGYVPQklklNDSLpL-------NVERFLKLTGKfSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSL 135
Cdd:COG1135 82 rKIGMIFQ----HFNL-LssrtvaeNVALPLEIAGV-PKAEIrkrvAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 873911691 136 LRRPDLLVLDEPAQGVDVQ--GQIdLyDLIDTIRHRFGCAVFMVSHDLHLV 184
Cdd:COG1135 156 ANNPKVLLCDEATSALDPEttRSI-L-DLLKDINRELGLTIVLITHEMDVV 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-196 |
2.13e-26 |
|
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: 102.45 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRK----VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----------KAKKLKI 69
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkepAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 70 GYVPQKLKLNDSLPL--NVERFLKLTGkFSQQEILEALK----LVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:cd03266 81 GFVSDSTGLYDRLTAreNLEYFAGLYG-LKGDELTARLEeladRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 873911691 144 LDEPAQGVDVQGQIDLYDLIDTIRhRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-214 |
2.71e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-KAKKL---------KIGYVP 73
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlRGQHIeglpghqiaRMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 --QKLKLNDSLPLnVE-------RFLK---LTGKF-------SQQEILEA----LKLVGAEHLQKSNMHQLSGGENQRVL 130
Cdd:PRK11300 85 tfQHVRLFREMTV-IEnllvaqhQQLKtglFSGLLktpafrrAESEALDRaatwLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 131 IARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHHHI-CCSGAPADIKH 209
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTpLANGTPEEIRN 243
|
....*
gi 873911691 210 HPSYI 214
Cdd:PRK11300 244 NPDVI 248
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-207 |
2.85e-26 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 102.61 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVefDGRkvLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLqTKFSGTIT---------KAKKL--KIGYVP 73
Cdd:COG4138 1 LQLNDVAV--AGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILlngrplsdwSAAELarHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QklklNDSLPLNVERF----LKLTGKFSQQEILEAL-KLVGAEHLQK---SNMHQLSGGENQRVLIARSLLR-----RPD 140
Cdd:COG4138 76 Q----QQSPPFAMPVFqylaLHQPAGASSEAVEQLLaQLAEALGLEDklsRPLTQLSGGEWQRVRLAAVLLQvwptiNPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 141 --LLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:COG4138 152 gqLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEV 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-207 |
3.09e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.66 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 14 FDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-------------KAKKlKIGYVPQ------ 74
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhaRARR-GIGYLPQeasifr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 KLKLNDSLPLNVERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 155 GQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDV-ICLHHHICCSGAPADI 207
Cdd:PRK10895 172 SVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAyIVSQGHLIAHGTPTEI 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-169 |
5.61e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.64 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLKIGYV 72
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgedithlpmhKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQ------KLKLNDslplNVERFLKLTG--KFSQQEILEAL-KLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:COG1137 84 PQeasifrKLTVED----NILAVLELRKlsKKEREERLEELlEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180
....*....|....*....|....*....
gi 873911691 144 LDEPAQGVD---VqgqIDLYDLIDTIRHR 169
Cdd:COG1137 160 LDEPFAGVDpiaV---ADIQKIIRHLKER 185
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-195 |
7.08e-26 |
|
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: 102.19 E-value: 7.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 19 VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKA----KKLK------------------IGYVPQKL 76
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlYQLDrkqrrafrrdvqlvfqdsPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 77 KLNDSLPLNVERFLKLTGKFSQQEILEALKLVG--AEHLQKSNmHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSLDESEQKARIAELLDMVGlrSEDADKLP-RQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 873911691 155 GQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLH 195
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMD 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-211 |
7.43e-26 |
|
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: 105.54 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDG----RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL----QTKFSGTIT---------K 63
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILfdgqdllglS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 64 AKKL------KIGYVPQK--LKLNdslPL-NVERFL--------KLTGKFSQQEILEALKLVG---AEHLQKSNMHQLSG 123
Cdd:COG4172 83 ERELrrirgnRIAMIFQEpmTSLN---PLhTIGKQIaevlrlhrGLSGAAARARALELLERVGipdPERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 124 GENQRVLIARSLLRRPDLLVLDEP--AQGVDVQGQIdLyDLIDTIRHRFGCAVFMVSHDLHLV--MAktDDVICLHH-HI 198
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPttALDVTVQAQI-L-DLLKDLQRELGMALLLITHDLGVVrrFA--DRVAVMRQgEI 235
|
250
....*....|...
gi 873911691 199 CCSGAPADIKHHP 211
Cdd:COG4172 236 VEQGPTAELFAAP 248
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-194 |
9.52e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 9.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKL-----------K 68
Cdd:PRK13647 1 MDNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQklKLNDSL------------PLNverfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLL 136
Cdd:PRK13647 81 VGLVFQ--DPDDQVfsstvwddvafgPVN----MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVL 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-196 |
1.17e-25 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 100.30 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKL--KIGY 71
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltddkkNINELrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKL--------NDSL-PLNVerfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLL 142
Cdd:cd03262 81 VFQQFNLfphltvleNITLaPIKV---KGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 143 VLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-195 |
1.87e-25 |
|
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: 98.44 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRK--VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGY 71
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdpNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKLndslplnverflkLTGKfsqqeILEALklvgaehlqksnmhqLSGGENQRVLIARSLLRRPDLLVLDEPAQGV 151
Cdd:cd03246 81 LPQDDEL-------------FSGS-----IAENI---------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 873911691 152 DVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVmAKTDDVICLH 195
Cdd:cd03246 128 DVEGERALNQAIAALKAA-GATRIVIAHRPETL-ASADRILVLE 169
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-195 |
2.49e-25 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 104.48 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQK----LKLN 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqlefLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSlPLnvERFLKLTGKFSQQEILEALKLVGAEHLQKS-NMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQID 158
Cdd:PRK10636 392 ES-PL--QHLARLAPQELEQKLRDYLGGFGFQGDKVTeETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
170 180 190
....*....|....*....|....*....|....*...
gi 873911691 159 LYD-LIDtirhrFGCAVFMVSHDLHLVMAKTDDVICLH 195
Cdd:PRK10636 469 LTEaLID-----FEGALVVVSHDRHLLRSTTDDLYLVH 501
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-186 |
3.63e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.94 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRK----VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKlkiGY 71
Cdd:COG4525 4 LTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITldgvpvtgpGADR---GV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKLndsLPL-----NVERFLKLTG---KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:COG4525 81 VFQKDAL---LPWlnvldNVAFGLRLRGvpkAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 873911691 144 LDEPAQGVDV----QGQidlyDLIDTIRHRFGCAVFMVSHDLH--LVMA 186
Cdd:COG4525 158 MDEPFGALDAltreQMQ----ELLLDVWQRTGKGVFLITHSVEeaLFLA 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-212 |
4.56e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITkAKKLKIGYVPQKLKlndslP 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM-LDGVDLSHVPPYQR-----P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 LN-------------VER---FLKLTGKFSQQEIL----EALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:PRK11607 93 INmmfqsyalfphmtVEQniaFGLKQDKLPKAEIAsrvnEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 144 LDEPAQGVDVQ----GQIDLYDLIDtirhRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPS 212
Cdd:PRK11607 173 LDEPMGALDKKlrdrMQLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIYEHPT 242
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-207 |
4.70e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.39 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------TK----AKKLKIgy 71
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldvatTPsrelAKRLAI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 vpqkLKLNDSLPlnverfLKLT-------GKF--SQ--------QEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARS 134
Cdd:COG4604 80 ----LRQENHIN------SRLTvrelvafGRFpySKgrltaedrEIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 135 LLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICL-HHHICCSGAPADI 207
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEI 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-184 |
9.75e-25 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 102.58 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLE-----RGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKakKLKIGYVPQKLKlnDSLPLNVERFL- 90
Cdd:PRK13409 347 TKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQYIK--PDYDGTVEDLLr 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 91 KLTGKFS----QQEILEALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTI 166
Cdd:PRK13409 423 SITDDLGssyyKSEIIKPLQL---ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170
....*....|....*...
gi 873911691 167 RHRFGCAVFMVSHDLHLV 184
Cdd:PRK13409 500 AEEREATALVVDHDIYMI 517
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-218 |
1.06e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.09 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-----------TKAKKLKIG 70
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKLNDSLPLN----VERF-----LKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDL 141
Cdd:PRK10575 89 YLPQQLPAAEGMTVRelvaIGRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 142 LVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPSYIALFG 218
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGgEMIAQGTPAELMRGETLEQIYG 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-184 |
2.60e-24 |
|
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: 101.40 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRI-----TTLIGPNGAGKSTLVKVVLGLQTKFSGTITKakKLKIGYVPQKLKlNDSlPLNVERFL- 90
Cdd:COG1245 348 TKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--DLKISYKPQYIS-PDY-DGTVEEFLr 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 91 -----KLTGKFSQQEILEALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDT 165
Cdd:COG1245 424 santdDFGSSYYKTEIIKPLGL---EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170
....*....|....*....
gi 873911691 166 IRHRFGCAVFMVSHDLHLV 184
Cdd:COG1245 501 FAENRGKTAMVVDHDIYLI 519
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-216 |
3.36e-24 |
|
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: 96.77 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-QTKFSGTITKAKKLKIG-----YVPQKLKL------NDSLPLNVE 87
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGKQITEPgpdrmVVFQNYSLlpwltvRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 88 RFLKLTGKFSQQEILEA-LKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTI 166
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEhIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 167 RHRFGCAVFMVSHDLHLVMAKTDDVICLhhhiccSGAPA------------------DIKHHPSYIAL 216
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVML------TNGPAanigqilevpfprprdrlEVVEDPSYYDL 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-215 |
4.97e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGT-------ITKAK----KLKIGYVPQKLklNDSL--- 82
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlirgepITKENirevRKFVGLVFQNP--DDQIfsp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 ---------PLNverfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDV 153
Cdd:PRK13652 95 tveqdiafgPIN----LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873911691 154 QGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPSYIA 215
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIFLQPDLLA 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-192 |
5.00e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.06 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 7 LDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTitkakkLKIGYVP-------QKLKLN 79
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------LLAGTAPlaearedTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DS--LPL-----NVErfLKLTGKFsQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVD 152
Cdd:PRK11247 89 DArlLPWkkvidNVG--LGLKGQW-RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 873911691 153 VQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-180 |
5.95e-24 |
|
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: 100.39 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLNDSLPL--NVE------ 87
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVreNVEegvaei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 88 -----RFLKLTGKFSQ---------------QEILEALKL--------VGAEHLQ----KSNMHQLSGGENQRVLIARSL 135
Cdd:TIGR03719 97 kdaldRFNEISAKYAEpdadfdklaaeqaelQEIIDAADAwdldsqleIAMDALRcppwDADVTKLSGGERRRVALCRLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 873911691 136 LRRPDLLVLDEPAQGVDVQGqidlYDLIDTIRHRFGCAVFMVSHD 180
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-195 |
7.64e-24 |
|
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: 96.15 E-value: 7.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFD-GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYV 72
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKL-NDSLPLNVeRFLKLTGkfSQQEILEALKlVGAEHLQKSNMHQ------------LSGGENQRVLIARSLLRRP 139
Cdd:cd03253 81 PQDTVLfNDTIGYNI-RYGRPDA--TDEEVIEAAK-AAQIHDKIMRFPDgydtivgerglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 140 DLLVLDEPAQGVDVQGQIDLYD-LIDTIRHRfgcAVFMVSHDLHLVMaKTDDVICLH 195
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAaLRDVSKGR---TTIVIAHRLSTIV-NADKIIVLK 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-207 |
1.04e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.24 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--KIGYVP 73
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpismlSSRQLarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKL------KLNDSLPLNVERFLKLTGKFSQQE---ILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:PRK11231 83 QHHltpegiTVRELVAYGRSPWLSLWGRLSAEDnarVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 145 DEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDL--------HLVMAKTDDVIclhhhicCSGAPADI 207
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLnqasrycdHLVVLANGHVM-------AQGTPEEV 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-196 |
1.57e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.91 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----TKAKKLK------------------IGYVPQ 74
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgEPLAKLNraqrkafrrdiqmvfqdsISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 KLKLNDSLPLNVERFLKLTGKFSQQEILEALKLVG--AEHLQKSNmHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVD 152
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDldDSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 873911691 153 VQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-181 |
1.88e-23 |
|
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: 98.59 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDG-RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYV 72
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLNDSLPLNVERFLKltGKFSQQEILEALKLVG-AEHLQK------SNMHQ----LSGGENQRVLIARSLLRRPDL 141
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRLAR--PDATDEELWAALERVGlADWLRAlpdgldTVLGEggarLSGGERQRLALARALLADAPI 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 873911691 142 LVLDEPAQGVDVQGQIDLY-DLIDTIRHRfgcAVFMVSHDL 181
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLeDLLAALSGR---TVVLITHHL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-185 |
2.47e-23 |
|
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: 98.28 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRK--VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTItkakKLK-------------- 68
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV----RLDgadlsqwdreelgr 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 -IGYVPQKLKL-NDSLPLNVERFlkltGKFSQQEILEALKLVGA----EHLQK-------SNMHQLSGGENQRVLIARSL 135
Cdd:COG4618 407 hIGYLPQDVELfDGTIAENIARF----GDADPEKVVAAAKLAGVhemiLRLPDgydtrigEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 136 LRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSH--------DLHLVM 185
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHrpsllaavDKLLVL 539
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-227 |
3.59e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 14 FDGRKVLDnISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----------KAKKLK-----IGYVPQklkl 78
Cdd:PRK13634 18 FERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkKNKKLKplrkkVGIVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 79 ndsLPLN------VER---FLKLTGKFSQQEIL----EALKLVG--AEHLQKSNMhQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:PRK13634 93 ---FPEHqlfeetVEKdicFGPMNFGVSEEDAKqkarEMIELVGlpEELLARSPF-ELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 144 LDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPSYIALFGTATQ 222
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKgTVFLQGTPREIFADPDELEAIGLDLP 248
|
....*
gi 873911691 223 ETLAF 227
Cdd:PRK13634 249 ETVKF 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-207 |
4.86e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.76 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 15 DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-TKAKKLK------------IGYVPQKLklNDS 81
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlIKGEPIKydkksllevrktVGIVFQNP--DDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 82 L------------PLNverfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQ 149
Cdd:PRK13639 91 LfaptveedvafgPLN----LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873911691 150 GVDVQGQID----LYDLidtirHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK13639 167 GLDPMGASQimklLYDL-----NKEGITIIISTHDVDLVPVYADKVYVMSDgKIIKEGTPKEV 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-202 |
5.23e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 94.56 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-------KA-KKLKIGYVPQK 75
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrQAlQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKLNDSLPLNVER-----------FLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:PRK15056 87 EEVDWSFPVLVEDvvmmgryghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 145 DEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHHHICCSG 202
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-181 |
7.64e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.28 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVldNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQK--------- 75
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 --------------LKLNDSLPLNVERflkltgkfsQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDL 141
Cdd:COG3840 80 nnlfphltvaqnigLGLRPGLKLTAEQ---------RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 873911691 142 LVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDL 181
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDP 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-196 |
7.90e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 93.06 E-value: 7.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFD-GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYV 72
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQK-LKLNDSLPLNVeRFLKLTGKfsQQEILEALKLVGAEHLQKS-----------NMHQLSGGENQRVLIARSLLRRPD 140
Cdd:cd03254 83 LQDtFLFSGTIMENI-RLGRPNAT--DEEVIEAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 141 LLVLDEPAQGVDVQGQIDLYDLIDTIRHrfGCAVFMVSHDLHLVMaKTDDVICLHH 196
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIK-NADKILVLDD 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-179 |
1.09e-22 |
|
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: 91.06 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLNDslp 83
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 lnverflkltGKFSQQeilealklvgaehLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLI 163
Cdd:cd03223 78 ----------GTLREQ-------------LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170
....*....|....*.
gi 873911691 164 dtirHRFGCAVFMVSH 179
Cdd:cd03223 135 ----KELGITVISVGH 146
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-196 |
1.55e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLKIGYVP---------- 73
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsprDAIRAGIAYVPedrkgeglvl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 -QKLKLNDSLPlNVERFLKLtGKFSQQEILEAlklvgAEHLQK------SNMHQ----LSGGENQRVLIARSLLRRPDLL 142
Cdd:COG1129 344 dLSIRENITLA-SLDRLSRG-GLLDRRRERAL-----AEEYIKrlriktPSPEQpvgnLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 143 VLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRE 469
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-180 |
1.70e-22 |
|
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: 96.16 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKlklNDS 81
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS---RDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 82 LPLNverflkltgKFSQQEI---LEALKLVGAE--------------HLQKSNMHQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:TIGR03719 397 LDPN---------KTVWEEIsggLDIIKLGKREipsrayvgrfnfkgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190
....*....|....*....|....*....|....*.
gi 873911691 145 DEPAQGVDVQgqiDLYDLIDTIRHRFGCAVfMVSHD 180
Cdd:TIGR03719 468 DEPTNDLDVE---TLRALEEALLNFAGCAV-VISHD 499
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-184 |
1.83e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.03 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------------KAKKLKIGYVPQ--------K 75
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqditglsgrelRPLRRRMQMVFQdpyaslnpR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKLNDSL--PLNVERflKLTGKFSQQEILEALKLVG--AEHLQKsNMHQLSGGENQRVLIARSLLRRPDLLVLDEP--AQ 149
Cdd:COG4608 112 MTVGDIIaePLRIHG--LASKAERRERVAELLELVGlrPEHADR-YPHEFSGGQRQRIGIARALALNPKLIVCDEPvsAL 188
|
170 180 190
....*....|....*....|....*....|....*
gi 873911691 150 GVDVQGQIdLYDLIDtIRHRFGCAVFMVSHDLHLV 184
Cdd:COG4608 189 DVSIQAQV-LNLLED-LQDELGLTYLFISHDLSVV 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-211 |
3.10e-22 |
|
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: 95.14 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGR-----------KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQtKFSGTIT---------K 63
Cdd:COG4172 275 LLEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRfdgqdldglS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 64 AKKLKigyvPQKLKL-------NDSL-P-LNVER---------FLKLTGKFSQQEILEALKLVG--AEHLQKSNmHQLSG 123
Cdd:COG4172 354 RRALR----PLRRRMqvvfqdpFGSLsPrMTVGQiiaeglrvhGPGLSAAERRARVAEALEEVGldPAARHRYP-HEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 124 GENQRVLIARSLLRRPDLLVLDEP--AQGVDVQGQIdlYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICC 200
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPtsALDVSVQAQI--LDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDgKVVE 506
|
250
....*....|.
gi 873911691 201 SGAPADIKHHP 211
Cdd:COG4172 507 QGPTEQVFDAP 517
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-211 |
3.46e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 91.72 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLqTK-------FSGT-ITKAK-----KL 67
Cdd:COG4674 7 HGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGK-TRpdsgsvlFGGTdLTGLDeheiaRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 KIGYVPQK------------LKLndSLPLNVERFLKLTGKFSQQE---ILEALKLVGAEHLQKSNMHQLSGGENQRVLIA 132
Cdd:COG4674 86 GIGRKFQKptvfeeltvfenLEL--ALKGDRGVFASLFARLTAEErdrIEEVLETIGLTDKADRLAGLLSHGQKQWLEIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 133 RSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfgCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:COG4674 164 MLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK--HSVVVVEHDMEFVRQIARKVTVLHQgSVLAEGSLDEVQADP 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-196 |
3.91e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.23 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAkklkiGYVPQK---------------------- 75
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----GYVPFKrrkefarrigvvfgqrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKLNDSLPLN-------VERFLKLTGKFSqqEILEAlklvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPA 148
Cdd:COG4586 111 LPAIDSFRLLkaiyripDAEYKKRLDELV--ELLDL------GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 873911691 149 QGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-183 |
5.56e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 19 VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSG-TITKAKKL--------------KIGYVPQKLKL----- 78
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdVIFNGQPMsklssaakaelrnqKLGFIYQFHHLlpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 79 ---NDSLPLnverflkLTGKFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGV 151
Cdd:PRK11629 104 aleNVAMPL-------LIGKKKPAEInsraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|..
gi 873911691 152 DVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHL 183
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-194 |
6.25e-22 |
|
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: 92.87 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRK---VLDnISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------------TKAKKLKIGY 71
Cdd:TIGR02142 1 LSARFSKRLgdfSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKLndsLP-LNVERFL-----KLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLD 145
Cdd:TIGR02142 80 VFQEARL---FPhLSVRGNLrygmkRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 873911691 146 EPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-207 |
6.55e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.03 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------KAKKL-----KIGYV---PQKLKLND 80
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvditdKKVKLsdirkKVGLVfqyPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 81 SLPLNVERFLKLTGkFSQQEIL----EALKLVG--AEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:PRK13637 100 TIEKDIAFGPINLG-LSEEEIEnrvkRAMNIVGldYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 155 GQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHHHIC-CSGAPADI 207
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCeLQGTPREV 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-207 |
8.60e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.23 E-value: 8.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDG--RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKL----------- 67
Cdd:PRK13635 2 KEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 KIGYVPQK-----------------LKlNDSLPLN--VERflkltgkfsqqeILEALKLVGAEHLQKSNMHQLSGGENQR 128
Cdd:PRK13635 82 QVGMVFQNpdnqfvgatvqddvafgLE-NIGVPREemVER------------VDQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 129 VLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVmAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKgEILEEGTPEEI 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-147 |
9.19e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.03 E-value: 9.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLNDSLPL--NVE------ 87
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVreNVEegvaev 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 88 -----RFLKLTGKFSQ---------------QEILEALKL--------VGAEHLQ----KSNMHQLSGGENQRVLIARSL 135
Cdd:PRK11819 99 kaaldRFNEIYAAYAEpdadfdalaaeqgelQEIIDAADAwdldsqleIAMDALRcppwDAKVTKLSGGERRRVALCRLL 178
|
170
....*....|..
gi 873911691 136 LRRPDLLVLDEP 147
Cdd:PRK11819 179 LEKPDMLLLDEP 190
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-152 |
1.20e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----------KAKKLKIGYVPQ 74
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 --KLKLNDSLPLNV---ERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQ 149
Cdd:PRK13536 122 fdNLDLEFTVRENLlvfGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
...
gi 873911691 150 GVD 152
Cdd:PRK13536 202 GLD 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-194 |
1.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.95 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDG---RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-----------TKAKK 66
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 67 LKIGYVPQK-------LKLNDSLPLNVERfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRP 139
Cdd:PRK13650 81 HKIGMVFQNpdnqfvgATVEDDVAFGLEN-KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 140 DLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVmAKTDDVICL 194
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVM 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-207 |
1.38e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.82 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 8 DSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-----------TKAKKLKIGYVPQkl 76
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 77 klNDSLPLNVE-RFLKLTGKFSQQEIL------------EALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:PRK10253 89 --NATTPGDITvQELVARGRYPHQPLFtrwrkedeeavtKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 144 LDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREgKIVAQGAPKEI 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-147 |
1.42e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 90.05 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------KAKKL-----KIG 70
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITvdgedltdSKKDInklrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQklklndSLPL--------NVERFLKLTGKFSQQEI----LEALKLVG-AEHLQKSNmHQLSGGENQRVLIARSLLR 137
Cdd:COG1126 81 MVFQ------QFNLfphltvleNVTLAPIKVKKMSKAEAeeraMELLERVGlADKADAYP-AQLSGGQQQRVAIARALAM 153
|
170
....*....|
gi 873911691 138 RPDLLVLDEP 147
Cdd:COG1126 154 EPKVMLFDEP 163
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-189 |
1.56e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 89.51 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 6 QLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-------TKAK-----KLKIGYVP 73
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIrldgediTKLPpheraRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKlklNDSLP-LNVERFLkLTGkfsqqeiLEALKLVGAEHLQ---------KSNMHQ----LSGGENQRVLIARSLLRRP 139
Cdd:TIGR03410 82 QG---REIFPrLTVEENL-LTG-------LAALPRRSRKIPDeiyelfpvlKEMLGRrggdLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 873911691 140 DLLVLDEPAQGvdVQGQI--DLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTD 189
Cdd:TIGR03410 151 KLLLLDEPTEG--IQPSIikDIGRVIRRLRAEGGMAILLVEQYLDFARELAD 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-211 |
1.68e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----------------TKA 64
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipamsrsrlyTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 65 KKLKIGYVPQKLKLNDSLPLNVERFLKLTGKFSQQEI-------LEALKLVGAEHLQKSnmhQLSGGENQRVLIARSLLR 137
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLhstvmmkLEAVGLRGAAKLMPS---ELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 138 RPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDV-ICLHHHICCSGAPADIKHHP 211
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAyIVADKKIVAHGSAQALQANP 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-183 |
1.79e-21 |
|
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: 89.42 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRK----VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKA-KKL--------- 67
Cdd:COG4181 6 APIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgQDLfaldedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 -----KIGYVPQKLKL--------NDSLPLnverflKLTG-KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIAR 133
Cdd:COG4181 86 rlrarHVGFVFQSFQLlptltaleNVMLPL------ELAGrRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 134 SLLRRPDLLVLDEPAQGVDVQ-GQ--IDL-YDLidtiRHRFGCAVFMVSHDLHL 183
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAAtGEqiIDLlFEL----NRERGTTLVLVTHDPAL 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-207 |
1.87e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.84 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGR-----KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL------QT-----KFSGTITKAKKLK 68
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgQTivgdyAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 -----IGYV---PQKLKLNDSL-------PLNverfLKLTGKFSQQEILEALKLVG-AEHLQKSNMHQLSGGENQRVLIA 132
Cdd:PRK13645 87 rlrkeIGLVfqfPEYQLFQETIekdiafgPVN----LGENKQEAYKKVPELLKLVQlPEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 133 RSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEgKVISIGSPFEI 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-179 |
2.38e-21 |
|
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: 92.89 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVS-VEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKL---- 76
Cdd:TIGR00954 449 DNGIKFENIPlVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPymtl 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 77 -KLNDSL--PLNVERFlKLTGkFSQQEILEALKLVGAEHLQKSN---------MHQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:TIGR00954 529 gTLRDQIiyPDSSEDM-KRRG-LSDKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*..
gi 873911691 145 DE--PAQGVDVQGQIdlYDLIdtirHRFGCAVFMVSH 179
Cdd:TIGR00954 607 DEctSAVSVDVEGYM--YRLC----REFGITLFSVSH 637
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-210 |
2.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKA-------------KKL--KIGYVPQ--KLKLN 79
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetgnknlKKLrkKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSLPLNVERFLKLTGKFSQQEI----LEALKLVG-AEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGFSEDEAkekaLKWLKKVGlSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 155 GQIDLYDLIDTIRhRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI--------KHH 210
Cdd:PRK13641 180 GRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHgKLIKHASPKEIfsdkewlkKHY 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-152 |
5.00e-21 |
|
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: 88.03 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDG--RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----TKAKKL-------KIGY 71
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgTDIRQLdpadlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKL-NDSLPLNVERFLKLTgkfSQQEILEALKLVGAEHLQKSNMH-----------QLSGGENQRVLIARSLLRRP 139
Cdd:cd03245 83 VPQDVTLfYGTLRDNITLGAPLA---DDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDP 159
|
170
....*....|...
gi 873911691 140 DLLVLDEPAQGVD 152
Cdd:cd03245 160 PILLLDEPTSAMD 172
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-180 |
5.86e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.54 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 6 QLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLG-LQTKF--SGTIT---------KAKKLKIGYVP 73
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFsaSGEVLlngrrltalPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKLNDslPLNVERFL------KLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:COG4136 83 QDDLLFP--HLSVGENLafalppTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....
gi 873911691 148 AQGVDVQGQIDLYDLI-DTIRHRfGCAVFMVSHD 180
Cdd:COG4136 161 FSKLDAALRAQFREFVfEQIRQR-GIPALLVTHD 193
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-194 |
6.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKlKIGYVPQKL-KLN 79
Cdd:PRK13636 3 DYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSL-----------------------PLNverfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLL 136
Cdd:PRK13636 82 ESVgmvfqdpdnqlfsasvyqdvsfgAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-156 |
9.38e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.09 E-value: 9.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----------KAKKLKIGYVPQ 74
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 --KLKLNDSLPLNVERFLKLTGKFSQQ------EILEALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:PRK13537 88 fdNLDPDFTVRENLLVFGRYFGLSAAAaralvpPLLEFAKL---ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170
....*....|
gi 873911691 147 PAQGVDVQGQ 156
Cdd:PRK13537 165 PTTGLDPQAR 174
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-182 |
9.97e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.17 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-----QTKFSGTIT------KAKKL-- 67
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILldgediYDPDVdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 -----KIGYVPQklKLNdslPL------NVERFLKLTGKFSQQEILE----ALKLVG-----AEHLQKSNMHqLSGGENQ 127
Cdd:COG1117 88 velrrRVGMVFQ--KPN---PFpksiydNVAYGLRLHGIKSKSELDEiveeSLRKAAlwdevKDRLKKSALG-LSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 128 RVLIARSLLRRPDLLVLDEPAQGVDVQ--GQIDlyDLIDTIRHRFgcAVFMVSHDLH 182
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPIstAKIE--ELILELKKDY--TIVIVTHNMQ 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-192 |
1.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.60 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGR-----KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------------------ 61
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 62 ---------TKAKKLK--------IGYVPQ--KLKLNDSlplNVER---FLKLTGKFSQQEILEA----LKLVG--AEHL 113
Cdd:PRK13651 83 vleklviqkTRFKKIKkikeirrrVGVVFQfaEYQLFEQ---TIEKdiiFGPVSMGVSKEEAKKRaakyIELVGldESYL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 114 QKSNMhQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:PRK13651 160 QRSPF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTI 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-189 |
2.17e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVK-----------VVLGLQTKFSGTITKAKKLKIGYVP 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKclnrmneleseVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKL----NDSLPL----NVERFLKLTG---KFSQQEILE-ALKLVGAEHLQKSNMHQ----LSGGENQRVLIARSLLR 137
Cdd:PRK14258 88 RQVSMvhpkPNLFPMsvydNVAYGVKIVGwrpKLEIDDIVEsALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 873911691 138 RPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTD 189
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-207 |
2.32e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.49 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVS------VEFDGRKVLDnISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGT-------ITKAKKLK-IG 70
Cdd:PRK13649 3 INLQNVSytyqagTPFEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSvrvddtlITSTSKNKdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKLNDSLP---LNVERFLK----------LTGKFSQQEILEALKLVG-AEHLQKSNMHQLSGGENQRVLIARSLL 136
Cdd:PRK13649 82 QIRKKVGLVFQFPesqLFEETVLKdvafgpqnfgVSQEEAEALAREKLALVGiSESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDI 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-179 |
6.99e-20 |
|
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: 84.85 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 24 SLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITkAKKLKIGYVP----------------QKLKLNDSLPLNVE 87
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL-INGVDVTAAPpadrpvsmlfqennlfAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 88 RFLKLTGKfSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIR 167
Cdd:cd03298 97 PGLKLTAE-DRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170
....*....|..
gi 873911691 168 HRFGCAVFMVSH 179
Cdd:cd03298 176 AETKMTVLMVTH 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-207 |
9.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.33 E-value: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 14 FDGRKVLDnISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI--------TKAKKLKIGYVPQKLKLNDSLP-- 83
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsSTSKQKEIKPVRKKVGVVFQFPes 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 -LNVERFLK----------LTGKFSQQEILEALKLVG--AEHLQKSNMhQLSGGENQRVLIARSLLRRPDLLVLDEPAQG 150
Cdd:PRK13643 96 qLFEETVLKdvafgpqnfgIPKEKAEKIAAEKLEMVGlaDEFWEKSPF-ELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 151 VDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK13643 175 LDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKgHIISCGTPSDV 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-152 |
1.15e-19 |
|
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: 84.59 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF--DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKvvlgLQTKF----SGTIT---------KAKKL-- 67
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVN----LIPRFydvdSGRILidghdvrdyTLASLrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 KIGYVPQKLKL-NDSLPLNVerflkLTGKF--SQQEILEALKLVGA-EHLQK----------SNMHQLSGGENQRVLIAR 133
Cdd:cd03251 77 QIGLVSQDVFLfNDTVAENI-----AYGRPgaTREEVEEAARAANAhEFIMElpegydtvigERGVKLSGGQRQRIAIAR 151
|
170
....*....|....*....
gi 873911691 134 SLLRRPDLLVLDEPAQGVD 152
Cdd:cd03251 152 ALLKDPPILILDEATSALD 170
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-202 |
1.63e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.35 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGlqtkFSG-TITKAKKLkigyvpqkLKLNDSLPLNV-E 87
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKyEVTEGEIL--------FKGEDITDLPPeE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 88 RFLKltGKF-SQQEILEALKLVGAEHLQKSNMhQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTI 166
Cdd:cd03217 74 RARL--GIFlAFQYPPEIPGVKNADFLRYVNE-GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 873911691 167 RHRfGCAVFMVSHDLHLV-MAKTDDVICLHH-HICCSG 202
Cdd:cd03217 151 REE-GKSVLIITHYQRLLdYIKPDRVHVLYDgRIVKSG 187
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-192 |
1.88e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 85.79 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------------KAKKLKIGYV---------PQ 74
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdllkadpeaqKLLRQKIQIVfqnpygslnPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 KlKLNDSL--PLNVERflKLTGKFSQQEILEALKLVG--AEHLQKSNmHQLSGGENQRVLIARSLLRRPDLLVLDEPAQG 150
Cdd:PRK11308 109 K-KVGQILeePLLINT--SLSAAERREKALAMMAKVGlrPEHYDRYP-HMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 873911691 151 VDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-152 |
2.11e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 86.99 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 3 NLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQ--------TKF-----SG-TITKAKKlK 68
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysndlTLFgrrrgSGeTIWDIKK-H 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSLPLNVeRFLKLTGKF----------SQQEIL--EALKLVG-AEHLQKSNMHQLSGGENQRVLIARSL 135
Cdd:PRK10938 338 IGYVSSSLHLDYRVSTSV-RNVILSGFFdsigiyqavsDRQQKLaqQWLDILGiDKRTADAPFHSLSWGQQRLALIVRAL 416
|
170
....*....|....*..
gi 873911691 136 LRRPDLLVLDEPAQGVD 152
Cdd:PRK10938 417 VKHPTLLILDEPLQGLD 433
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-212 |
2.64e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------TKAKKLKIGYVPQK 75
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 76 LKLNDSLPL--NVERFLKLTGKFS---QQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQG 150
Cdd:PRK11000 84 YALYPHLSVaeNMSFGLKLAGAKKeeiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 151 VD----VQGQIDlydlIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPS 212
Cdd:PRK11000 164 LDaalrVQMRIE----ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAgRVAQVGKPLELYHYPA 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
2.71e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTItKAKKLKIG-YVPQKLKLNDSLPLNVERFLKLTGKF 96
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDIYIGdKKNNHELITNPYSKKIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 97 S---------------QQEIL---EALKLVGAEHLQKSNMH----------------QLSGGENQRVLIARSLLRRPDLL 142
Cdd:PRK13631 119 SmvfqfpeyqlfkdtiEKDIMfgpVALGVKKSEAKKLAKFYlnkmglddsylerspfGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 143 VLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPSYIAL 216
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKgKILKTGTPYEIFTDQHIINS 272
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-146 |
3.36e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.24 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRK----VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL---- 67
Cdd:PRK11153 2 IELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgqdltalSEKELrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 -KIGYVPQKLKL--------NDSLPLnverflKLTGKfSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARS 134
Cdd:PRK11153 82 rQIGMIFQHFNLlssrtvfdNVALPL------ELAGT-PKAEIkarvTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170
....*....|..
gi 873911691 135 LLRRPDLLVLDE 146
Cdd:PRK11153 155 LASNPKVLLCDE 166
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-197 |
3.54e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-----------TKAKKLKIG 70
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedistlkPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKL-NDSLPLNVERFLKLTGKFSQ-QEILEALKLVG-AEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:PRK10247 85 YCAQTPTLfGDTVYDNLIFPWQIRNQQPDpAIFLDDLERFAlPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 148 AQGVDVQGQIDLYDLIdtirHRF----GCAVFMVSHDLHLVmAKTDDVICLHHH 197
Cdd:PRK10247 165 TSALDESNKHNVNEII----HRYvreqNIAVLWVTHDKDEI-NHADKVITLQPH 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-180 |
3.73e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLK 68
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdgkditdwqtaKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSlpLNVERFLKLTGKFS-----QQEILEALKLVGAEHLQKSNMH-QLSGGENQRVLIARSLLRRPDLL 142
Cdd:PRK11614 82 VAIVPEGRRVFSR--MTVEENLAMGGFFAerdqfQERIKWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 873911691 143 VLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHD 180
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQN 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-180 |
3.83e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 86.33 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKlklNDS 81
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS---RDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 82 LPLN--------------------------VERFlkltgKFS---QQeilealKLVGaehlqksnmhQLSGGENQRVLIA 132
Cdd:PRK11819 399 LDPNktvweeisggldiikvgnreipsrayVGRF-----NFKggdQQ------KKVG----------VLSGGERNRLHLA 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 133 RSLLRRPDLLVLDEPAQGVDVqgqidlydliDTIR------HRF-GCAVfMVSHD 180
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDV----------ETLRaleealLEFpGCAV-VISHD 501
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-187 |
4.40e-19 |
|
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: 82.41 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 7 LDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK-------------LKIGYVP 73
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdepheniLYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 qKLKLNDSLPLNVeRFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDV 153
Cdd:TIGR01189 83 -GLKPELSALENL-HFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|....
gi 873911691 154 QGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAK 187
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQDLGLVEAR 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-152 |
4.47e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT--------------KAKKL--- 67
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdfsqkpseKAIRLlrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 KIGYVPQK------LKLNDSL---PLNVERFLKLTGKFSQQEILEALKLvgAEHLQKSNMHqLSGGENQRVLIARSLLRR 138
Cdd:COG4161 83 KVGMVFQQynlwphLTVMENLieaPCKVLGLSKEQAREKAMKLLARLRL--TDKADRFPLH-LSGGQQQRVAIARALMME 159
|
170
....*....|....
gi 873911691 139 PDLLVLDEPAQGVD 152
Cdd:COG4161 160 PQVLLFDEPTAALD 173
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-218 |
4.76e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.08 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEF-DGRK-VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-------QTKF--SGTITKAKKL--- 67
Cdd:PRK13640 3 DNIVEFKHVSFTYpDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpNSKItvDGITLTAKTVwdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 --KIGYVPQK-------LKLNDSLPLNVErflklTGKFSQQEIL----EALKLVGAEHLQKSNMHQLSGGENQRVLIARS 134
Cdd:PRK13640 83 reKVGIVFQNpdnqfvgATVGDDVAFGLE-----NRAVPRPEMIkivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 135 LLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDL-HLVMAktDDVICLHH-HICCSGAPADIKHHPS 212
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIdEANMA--DQVLVLDDgKLLAQGSPVEIFSKVE 235
|
....*.
gi 873911691 213 YIALFG 218
Cdd:PRK13640 236 MLKEIG 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-179 |
6.55e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 82.70 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTK---FSGTIT------KAKKLK--IGYVPQklkLNDSLP-L 84
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILfngqprKPDQFQkcVAYVRQ---DDILLPgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 NVERFLKLTGKFSQQEIL-----------EALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDv 153
Cdd:cd03234 97 TVRETLTYTAILRLPRKSsdairkkrvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD- 175
|
170 180
....*....|....*....|....*...
gi 873911691 154 qgQIDLYDLIDTIRH--RFGCAVFMVSH 179
Cdd:cd03234 176 --SFTALNLVSTLSQlaRRNRIVILTIH 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-203 |
7.44e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQT--------------------KFSGT 60
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshiellgrtvqregRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 61 ITKAKKlKIGYVPQKLKLNDSLPL--NV-----------ERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQ 127
Cdd:PRK09984 81 IRKSRA-NTGYIFQQFNLVNRLSVleNVligalgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 128 RVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGA 203
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQgHVFYDGS 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-207 |
7.54e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.12 E-value: 7.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRK--VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------------TKAKKlKIG 70
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitiskenlKEIRK-KIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQK-------LKLNDSLPLNVERfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:PRK13632 87 IIFQNpdnqfigATVEDDIAFGLEN-KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 144 LDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMaKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgKLIAQGKPKEI 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-194 |
1.10e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.88 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRK--VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------------TKAKKl 67
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfEKLRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 KIGYVPQKlklndslPLNveRFLKLTGKFS---------------QQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIA 132
Cdd:PRK13648 84 HIGIVFQN-------PDN--QFVGSIVKYDvafglenhavpydemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 133 RSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMaKTDDVICL 194
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVM 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
5-207 |
1.31e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.29 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVefDGRkvLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLqTKFSGTITKAKKLKIGYVPQKLKL------ 78
Cdd:PRK03695 1 MQLNDVAV--STR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARhrayls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 79 -NDSLPLNVERF----LKLTGKFSQQEILEALKLVgAEHLQ-----KSNMHQLSGGENQRVLIARSLLR-----RPD--L 141
Cdd:PRK03695 76 qQQTPPFAMPVFqyltLHQPDKTRTEAVASALNEV-AEALGlddklGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 142 LVLDEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICLHHHIC-CSGAPADI 207
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLlASGRRDEV 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-194 |
1.41e-18 |
|
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: 81.39 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF--DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKL--KIGY 71
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiGLHDLrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQK-LKLNDSLPLNVERFlkltGKFSQQEILEALKLVG-AEHLQKS----NMHQLSGGEN----QRVLI--ARSLLRRP 139
Cdd:cd03244 83 IPQDpVLFSGTIRSNLDPF----GEYSDEELWQALERVGlKEFVESLpgglDTVVEEGGENlsvgQRQLLclARALLRKS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 140 DLLVLDEPAQGVDVQGqidlyDLI--DTIRHRF-GCAVFMVSHDLHLVMaKTDDVICL 194
Cdd:cd03244 159 KILVLDEATASVDPET-----DALiqKTIREAFkDCTVLTIAHRLDTII-DSDRILVL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-199 |
1.70e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEF----DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-----------QTKFSG--------- 59
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvypsgDIRFHGesllhaseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 60 TITKAKKLKIGYVPQK--LKLNdslPL-NVERFLK--------LTGKFSQQEILEALKLVGAEHLQK---SNMHQLSGGE 125
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEpmVSLN---PLhTLEKQLYevlslhrgMRREAARGEILNCLDRVGIRQAAKrltDYPHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 126 NQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHHHIC 199
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-192 |
1.71e-18 |
|
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: 81.69 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRIT-----TLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKlKIGYVPQKLKLNdsLPLNVERFL-- 90
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKAD--YEGTVRDLLss 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 91 ----KLTGKFSQQEILEALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTI 166
Cdd:cd03237 85 itkdFYTHPYFKTEIAKPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180
....*....|....*....|....*.
gi 873911691 167 RHRFGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-192 |
1.81e-18 |
|
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: 81.33 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEF-----DGRK--VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-----------T 62
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 63 KA--------KKLKIGYVPQKLKlndSLP----LNV--ERFLKLTGKFSQ-----QEILEALKLvgAEHLqksnmHQL-- 121
Cdd:COG4778 81 QAspreilalRRRTIGYVSQFLR---VIPrvsaLDVvaEPLLERGVDREEararaRELLARLNL--PERL-----WDLpp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 122 ---SGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVV 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-195 |
1.99e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 22 NISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----------KAKKLKIG--YVPQK-----LKLNDSLPL 84
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeinalsTAQRLARGlvYLPEDrqssgLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 NVERFLKLTGKFSQQE-----ILE------ALKLVGAEHLQKSnmhqLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDV 153
Cdd:PRK15439 361 NVCALTHNRRGFWIKParenaVLEryrralNIKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 873911691 154 QGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLH 195
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMH 477
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-152 |
2.61e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------------TKAKKL----- 67
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsktPSDKAIrelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 KIGYVPQKLKLNDSL---------PLNVERFLKLTGKFSQQEILEALKLvgAEHLQKSNMHqLSGGENQRVLIARSLLRR 138
Cdd:PRK11124 83 NVGMVFQQYNLWPHLtvqqnlieaPCRVLGLSKDQALARAEKLLERLRL--KPYADRFPLH-LSGGQQQRVAIARALMME 159
|
170
....*....|....
gi 873911691 139 PDLLVLDEPAQGVD 152
Cdd:PRK11124 160 PQVLLFDEPTAALD 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-225 |
3.14e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK----------LK--IGYVPQKLKlNDSLPL--N 85
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdgLAngIVYISEDRK-RDGLVLgmS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 86 VERFLKLT--GKFS--------QQEILEALKLVGAEHLQKSNMHQ----LSGGENQRVLIARSLLRRPDLLVLDEPAQGV 151
Cdd:PRK10762 347 VKENMSLTalRYFSraggslkhADEQQAVSDFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 152 DVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICcsgAPADIKHhpsyialfgtATQETL 225
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEgRIS---GEFTREQ----------ATQEKL 487
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-152 |
3.89e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.91 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------TKAKKLKI----G 70
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkvndPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKLNDSL---------PLNVERFLKltgKFSQQEILEALKLVG-AEHlqksnMH----QLSGGENQRVLIARSLL 136
Cdd:PRK09493 81 MVFQQFYLFPHLtalenvmfgPLRVRGASK---EEAEKQARELLAKVGlAER-----AHhypsELSGGQQQRVAIARALA 152
|
170
....*....|....*.
gi 873911691 137 RRPDLLVLDEPAQGVD 152
Cdd:PRK09493 153 VKPKLMLFDEPTSALD 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-180 |
4.32e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.46 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 6 QLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQ---KLKLNDSL 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhraELDPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 PLNVERflkltGKfsqQEIlealkLVGAE------HLQ------KSNM---HQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:PRK11147 401 MDNLAE-----GK---QEV-----MVNGRprhvlgYLQdflfhpKRAMtpvKALSGGERNRLLLARLFLKPSNLLILDEP 467
|
170 180 190
....*....|....*....|....*....|...
gi 873911691 148 AQGVDVQGQIDLYDLIDTirhrFGCAVFMVSHD 180
Cdd:PRK11147 468 TNDLDVETLELLEELLDS----YQGTVLLVSHD 496
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-187 |
6.89e-18 |
|
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: 79.07 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 8 DSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---KAKKLKIGYVPQKLKLNDSLP- 83
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIARGLLYLGHAPg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 ----LNVERFLKLTGKF-SQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQID 158
Cdd:cd03231 84 ikttLSVLENLRFWHADhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|....*....
gi 873911691 159 LYDLIDTIRHRFGCAVFMVSHDLHLVMAK 187
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAG 192
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-215 |
1.74e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.49 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQT--------KFSGTIT-KAKKLKIGYVPQ 74
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTlNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 KLKLNDSLPLNVERFLKltgkFSQQEIL-----------------------EALKLVGAEHLQKSNMHQLSGGENQRVLI 131
Cdd:PRK13547 81 LARLRAVLPQAAQPAFA----FSAREIVllgrypharragalthrdgeiawQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 132 ARSL---------LRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCS 201
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADgAIVAH 236
|
250
....*....|....
gi 873911691 202 GAPADIKhHPSYIA 215
Cdd:PRK13547 237 GAPADVL-TPAHIA 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-194 |
2.32e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---KAKKLK--------- 68
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgKEVTFNgpkssqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSLPLNVERFL--KLTGKFSQ-------QEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRP 139
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLgrEFVNRFGRidwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 140 DLLVLDEPAQGV-DVQGQiDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:PRK10762 161 KVIIMDEPTDALtDTETE-SLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVF 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-213 |
2.48e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.77 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEF---DGR-KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKfSGTITKAKKL---KIGYVP 73
Cdd:PRK09473 9 ADALLDVKDLRVTFstpDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRIGGSATFngrEILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKlKLN------------DSL-PLN--------VERFLKLTGKFSQQE-------ILEALKLvgAEHLQKSNM--HQLSG 123
Cdd:PRK09473 88 EK-ELNklraeqismifqDPMtSLNpymrvgeqLMEVLMLHKGMSKAEafeesvrMLDAVKM--PEARKRMKMypHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 124 GENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSG 202
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAgRTMEYG 244
|
250
....*....|.
gi 873911691 203 APADIKHHPSY 213
Cdd:PRK09473 245 NARDVFYQPSH 255
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-196 |
2.51e-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: 78.68 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF--DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSG----------TITKAK-KLKIGY 71
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlaLADPAWlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQK-LKLNDSLPLNVErfLKLTGkFSQQEILEALKLVGA-----------EHLQKSNMHQLSGGENQRVLIARSLLRRP 139
Cdd:cd03252 81 VLQEnVLFNRSIRDNIA--LADPG-MSMERVIEAAKLAGAhdfiselpegyDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 140 DLLVLDEPAQGVDVQG----QIDLYDLIDtirhrfGCAVFMVSHDLHLVMaKTDDVICLHH 196
Cdd:cd03252 158 RILIFDEATSALDYESehaiMRNMHDICA------GRTVIIIAHRLSTVK-NADRIIVMEK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-217 |
2.60e-17 |
|
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: 78.84 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 22 NISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------------TKAKKLKIGYVPQKLKL--NDSLPL 84
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaamsrkelRELRRKKISMVFQSFALlpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 NVERFLKLTGKFSQQEI---LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYD 161
Cdd:cd03294 122 NVAFGLEVQGVPRAEREeraAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 162 LIDTIRHRFGCAVFMVSHDLhlvmaktDDVICLHHHICC--------SGAPADIKHHPS--YIALF 217
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDL-------DEALRLGDRIAImkdgrlvqVGTPEEILTNPAndYVREF 260
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-152 |
2.60e-17 |
|
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: 77.59 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQT--KFSGTIT--------KAKKLKIGYVPQklklNDSLpln 85
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLingrpldkRSFRKIIGYVPQ----DDIL--- 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 86 verflkltgkFSQQEILEALKLVgaehlqkSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVD 152
Cdd:cd03213 94 ----------HPTLTVRETLMFA-------AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-194 |
4.21e-17 |
|
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: 76.58 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDG--RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITkakklkigyvpqklkLNDSL 82
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------------LDGVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 PLNVERFL-KLTGKFSQQEILEALKLvgaehlqKSNM-HQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLY 160
Cdd:cd03247 66 VSDLEKALsSLISVLNQRPYLFDTTL-------RNNLgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190
....*....|....*....|....*....|....*
gi 873911691 161 DLIdtIRHRFGCAVFMVSHdlHLV-MAKTDDVICL 194
Cdd:cd03247 139 SLI--FEVLKDKTLIWITH--HLTgIEHMDKILFL 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-193 |
4.47e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.97 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL--------QTKFSGTITKAKKLK---- 68
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegEIIFEGEELQASNIRdter 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 --IGYVPQKLKL-------------NDSLPLNVERFLKLTGKfsQQEILEALKLVGAEHLQKSNmhqLSGGENQRVLIAR 133
Cdd:PRK13549 82 agIAIIHQELALvkelsvleniflgNEITPGGIMDYDAMYLR--AQKLLAQLKLDINPATPVGN---LGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 134 SLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAkTDDVIC 193
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKA-ISDTIC 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-194 |
4.54e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTK------FSG-TITKAK-------KLK 68
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPsagkiwFSGhDITRLKnrevpflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQK--LKLNDSLPLNVERFLKLTGKFSQ---QEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLV 143
Cdd:PRK10908 81 IGMIFQDhhLLMDRTVYDNVAIPLIIAGASGDdirRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 873911691 144 LDEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTL 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-154 |
4.56e-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: 80.23 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQT----------------------------- 55
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 56 -----------------KFSGTITKAKKLKIGYVPQK---LKLNDSLPLNVERFLKLTGKFSQQEILEALKLVGAEHLQK 115
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRtfaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 873911691 116 SNMH---QLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:TIGR03269 161 RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-164 |
4.82e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVV-----LGLQTKFSGTI-------------T 62
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIvynghniysprtdT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 63 KAKKLKIGYVPQKlklNDSLPL----NVERFLKLTGKFSQQEILEALK--LVGA-------EHLQKSNMhQLSGGENQRV 129
Cdd:PRK14239 82 VDLRKEIGMVFQQ---PNPFPMsiyeNVVYGLRLKGIKDKQVLDEAVEksLKGAsiwdevkDRLHDSAL-GLSGGQQQRV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 873911691 130 LIARSLLRRPDLLVLDEPAQGVD--VQGQID--LYDLID 164
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDpiSAGKIEetLLGLKD 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-195 |
5.47e-17 |
|
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: 79.87 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-QTKFSGTI------------TKAKKLKIGYVPQKLKLNDSLP 83
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVfingkpvdirnpAQAIRAGIAMVPEDRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 -LNVERFLKLTG--KFSQQEILEA---LKLVGAE----HLQKSN----MHQLSGGENQRVLIARSLLRRPDLLVLDEPAQ 149
Cdd:TIGR02633 353 iLGVGKNITLSVlkSFCFKMRIDAaaeLQIIGSAiqrlKVKTASpflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 873911691 150 GVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLH 195
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIG 477
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-183 |
6.33e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.13 E-value: 6.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 19 VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------------TKAKKLKIGYVPQKLKLNDSLP 83
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhqmdeearAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 L--NVERFLKLTGKFSQQEILEALKLVGAEHLQKSNMH---QLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQID 158
Cdd:PRK10584 105 AleNVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180
....*....|....*....|....*
gi 873911691 159 LYDLIDTIRHRFGCAVFMVSHDLHL 183
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQL 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-191 |
1.43e-16 |
|
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: 78.71 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL--------QTKFSGTITKAKKLK------I 69
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgEIYWSGSPLKASNIRdteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 70 GYVPQKLKLNDSLPLNVERFL--KLTGKFSQQE----ILEALKLVGAEHLQKSN----MHQLSGGENQRVLIARSLLRRP 139
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLgnEITLPGGRMAynamYLRAKNLLRELQLDADNvtrpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 873911691 140 DLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDV 191
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTI 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-196 |
1.86e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGR---KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKK 66
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgvplvqydhHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 67 LKIGYVPQKLKL-NDSLPLNVERFLKLTGKfsqQEILEALKLVGAeHLQKSNM------------HQLSGGENQRVLIAR 133
Cdd:TIGR00958 555 RQVALVGQEPVLfSGSVRENIAYGLTDTPD---EEIMAAAKAANA-HDFIMEFpngydtevgekgSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873911691 134 SLLRRPDLLVLDEPAQGVDVQGQIDLYDLidtiRHRFGCAVFMVSHDLHLVmAKTDDVICLHH 196
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQES----RSRASRTVLLIAHRLSTV-ERADQILVLKK 688
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-146 |
1.90e-16 |
|
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: 76.04 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGR---KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT----KAKKL-------KIG 70
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvDIRDLnlrwlrsQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKL-NDSLPLNVerflkLTGKFS--QQEILEALKLVGAEHLQKSNMH-----------QLSGGENQRVLIARSLL 136
Cdd:cd03249 81 LVSQEPVLfDGTIAENI-----RYGKPDatDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALL 155
|
170
....*....|
gi 873911691 137 RRPDLLVLDE 146
Cdd:cd03249 156 RNPKILLLDE 165
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-181 |
1.98e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.31 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 27 LERGRITTLIGPNGAGKSTLVKVVLGLQT-----------------KFSGTI-------TKAKKLKIGYVPQKLklnDSL 82
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyeeepswdevlkRFRGTElqnyfkkLYNGEIKVVHKPQYV---DLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 PL----NVERFLKLT---GKFSqqEILEALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQG 155
Cdd:PRK13409 173 PKvfkgKVRELLKKVderGKLD--EVVERLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180
....*....|....*....|....*.
gi 873911691 156 QIDLYDLIDTIRHrfGCAVFMVSHDL 181
Cdd:PRK13409 248 RLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-196 |
2.01e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRK-----------VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-----QTKFSG----TITK 63
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLinsqgEIWFDGqplhNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 64 AKKL----KIGYVPQKLklNDSL-P-LNVERFL---------KLTGKFSQQEILEALKLVGaehLQKSNMH----QLSGG 124
Cdd:PRK15134 355 RQLLpvrhRIQVVFQDP--NSSLnPrLNVLQIIeeglrvhqpTLSAAQREQQVIAVMEEVG---LDPETRHrypaEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 125 ENQRVLIARSLLRRPDLLVLDEPAQGVD--VQGQIdlYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDktVQAQI--LALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-146 |
2.06e-16 |
|
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: 78.32 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 11 SVEFD--------GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------------KAkkl 67
Cdd:COG5265 357 EVRFEnvsfgydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILidgqdirdvtqaslrAA--- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 kIGYVPQKLKL-NDSLPLNVeRFLKLTGkfSQQEILEALKL-----------------VGAEHLQksnmhqLSGGENQRV 129
Cdd:COG5265 434 -IGIVPQDTVLfNDTIAYNI-AYGRPDA--SEEEVEAAARAaqihdfieslpdgydtrVGERGLK------LSGGEKQRV 503
|
170
....*....|....*..
gi 873911691 130 LIARSLLRRPDLLVLDE 146
Cdd:COG5265 504 AIARTLLKNPPILIFDE 520
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-181 |
2.45e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.08 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRK-VLDNISLNLERGRITTLIGPNGAGKSTLVKVvlgLQTKF---SGTIT-----------KAKKLK 68
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL---LQRVFdpqSGRILidgtdirtvtrASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQK-LKLNDSLPLNVErflklTGK--FSQQEILEALKLVGA-EHLQKSNM----------HQLSGGENQRVLIARS 134
Cdd:PRK13657 411 IAVVFQDaGLFNRSIEDNIR-----VGRpdATDEEMRAAAERAQAhDFIERKPDgydtvvgergRQLSGGERQRLAIARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 873911691 135 LLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHrfGCAVFMVSHDL 181
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRL 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-181 |
2.66e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLK 68
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynkldhkLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSLP----LNVERFL--KLTG------KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLL 136
Cdd:PRK09700 82 IGIIYQELSVIDELTvlenLYIGRHLtkKVCGvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 873911691 137 RRPDLLVLDEPAQGVdVQGQID-LYDLIDTIRHRfGCAVFMVSHDL 181
Cdd:PRK09700 162 LDAKVIIMDEPTSSL-TNKEVDyLFLIMNQLRKE-GTAIVYISHKL 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-195 |
4.26e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-QTKFSGTIT------------KAKKLKIGYVPQKLKLNDSL 82
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFidgkpvkirnpqQAIAQGIAMVPEDRKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 PL----------NVERFLK---LTGKFSQQEILEALKL--VGAEHLQKSnMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:PRK13549 354 PVmgvgknitlaALDRFTGgsrIDDAAELKTILESIQRlkVKTASPELA-IARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 873911691 148 AQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLH 195
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMH 479
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-196 |
4.62e-16 |
|
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: 77.47 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFD-GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKL-----------KIGYV 72
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLNDSLPLNvERFLKLTGKFSQQEILEALKLV-----------GAEHLQKSNMHQLSGGENQRVLIARSLLRRPDL 141
Cdd:TIGR01193 554 PQEPYIFSGSILE-NLLLGAKENVSQDEIWAACEIAeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 142 LVLDEPAQGVDVQGQIDLYDLIDTIRHRfgcAVFMVSHDLHlVMAKTDDVICLHH 196
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDH 683
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-209 |
5.42e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------------TKAKKLKIGY 71
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarltpAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQKLKLNDSLPLNVERFLKLTGKFSQQEILEALKLVGAEHLqksNMHQLSG----GENQRVLIARSLLRRPDLLVLDEP 147
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQL---DLDSSAGslevADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873911691 148 AQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKH 209
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDgTIALSGKTADLST 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-207 |
5.73e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 14 FDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-KAKKL---KIGYV------------PQKLK 77
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwQGKPLdysKRGLLalrqqvatvfqdPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 78 LNDSLPLNVERFLKLTGkFSQQEIL----EALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDV 153
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLG-VPEAEITrrvdEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 154 QGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQgQILTHGAPGEV 223
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-184 |
7.84e-16 |
|
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: 74.87 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKlkiGYVPQKLKlndSLP 83
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMR---SGAELELY---QLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 LNVERFLKLTG-KFSQQEILEALKL--------------VGAEH-----------LQKSNM---------HQLSGGENQR 128
Cdd:TIGR02323 77 EAERRRLMRTEwGFVHQNPRDGLRMrvsaganigerlmaIGARHygnirataqdwLEEVEIdptriddlpRAFSGGMQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 129 VLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLV 184
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVA 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-194 |
8.31e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 8.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGR--KVLDNISLNLERGRITTLIGPNGAGKSTLvkvvLGLQTKF----SGTITKA-KKLK-------- 68
Cdd:PRK11160 338 SLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTRAwdpqQGEILLNgQPIAdyseaalr 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 --IGYVPQKLKL-NDSLPLNverfLKLTG-KFSQQEILEALKLVGAEHLQKSNM----------HQLSGGENQRVLIARS 134
Cdd:PRK11160 414 qaISVVSQRVHLfSATLRDN----LLLAApNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 135 LLRRPDLLVLDEPAQGVDVQG--QIdLYDLIDTIRHRfgcAVFMVSHDLHLvMAKTdDVICL 194
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETerQI-LELLAEHAQNK---TVLMITHRLTG-LEQF-DRICV 545
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-184 |
8.51e-16 |
|
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: 73.60 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYVPQKLKLND-SLPLN 85
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistiplEDLRSSLTIIPQDPTLFSgTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 86 VERFlkltGKFSQQEILEALKLvgaehlqKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYdliDT 165
Cdd:cd03369 102 LDPF----DEYSDEEIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ---KT 167
|
170 180
....*....|....*....|
gi 873911691 166 IRHRF-GCAVFMVSHDLHLV 184
Cdd:cd03369 168 IREEFtNSTILTIAHRLRTI 187
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-181 |
1.00e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.85 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 24 SLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQK---------------LKLNDSLPLNVER 88
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvsmlfqennlfshLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 89 FLKLTGkfSQQEILEAL-KLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIR 167
Cdd:PRK10771 99 GLKLNA--AQREKLHAIaRQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176
|
170
....*....|....
gi 873911691 168 HRFGCAVFMVSHDL 181
Cdd:PRK10771 177 QERQLTLLMVSHSL 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-181 |
1.12e-15 |
|
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: 75.98 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 27 LERGRITTLIGPNGAGKSTLVKVVLGLQT-----------------KFSGTI-------TKAKKLKIGYVPQ-------- 74
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkRFRGTElqdyfkkLANGEIKVAHKPQyvdlipkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 -KLKLNDSLPLNVERflkltGKFSqqEILEALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDV 153
Cdd:COG1245 176 fKGTVRELLEKVDER-----GKLD--ELAEKLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*...
gi 873911691 154 QGQIDLYDLIDTIRhRFGCAVFMVSHDL 181
Cdd:COG1245 246 YQRLNVARLIRELA-EEGKYVLVVEHDL 272
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-225 |
1.15e-15 |
|
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: 76.59 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----------TKAKKLKIGYVPQKLKLNDSLPL- 84
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdietnLDAVRQSLGMCPQHNILFHHLTVa 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 -NVERFLKLTGKF---SQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLY 160
Cdd:TIGR01257 1022 eHILFYAQLKGRSweeAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 161 DLIdtIRHRFGCAVFMVSHDLHLVMAKTDDV-ICLHHHICCSGAPADIKHhpsyiaLFGTATQETL 225
Cdd:TIGR01257 1102 DLL--LKYRSGRTIIMSTHHMDEADLLGDRIaIISQGRLYCSGTPLFLKN------CFGTGFYLTL 1159
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-211 |
1.23e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.16 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKV----LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL----------QTKFSG----TITKAK 65
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrvmaeKLEFNGqdlqRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 66 KLKIGYVPQKLKLNDSL-PLN--------VERFLKL----TGKFSQQEILEALKLVG----AEHLQKSNmHQLSGGENQR 128
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMtSLNpcytvgfqIMEAIKVhqggNKKTRRQRAIDLLNQVGipdpASRLDVYP-HQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 129 VLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAgQVVETGKAHDI 241
|
....
gi 873911691 208 KHHP 211
Cdd:PRK11022 242 FRAP 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-167 |
1.30e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.83 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKV--LDNISLNLERGRITTLIGPNGAGKSTLVKvvlgLQTKF----SGTIT------KAKKLK---- 68
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIAN----LLTRFydidEGEILldghdlRDYTLAslrn 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 -IGYVPQKLKL-NDSLPLNVErfLKLTGKFSQQEILEALKLVGA-EHLQK----------SNMHQLSGGENQRVLIARSL 135
Cdd:PRK11176 418 qVALVSQNVHLfNDTIANNIA--YARTEQYSREQIEEAARMAYAmDFINKmdngldtvigENGVLLSGGQRQRIAIARAL 495
|
170 180 190
....*....|....*....|....*....|..
gi 873911691 136 LRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIR 167
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQ 527
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-169 |
1.72e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.55 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLG---LQTK----FSGTITKAKKL-----KIGYV 72
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarkIQQGrvevLGGDMADARHRravcpRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLNDSLPL----NVERFLKLTGkFSQQE----ILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:NF033858 82 PQGLGKNLYPTLsvfeNLDFFGRLFG-QDAAErrrrIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180
....*....|....*....|....*....
gi 873911691 145 DEPAQGVD----VQgqidLYDLIDTIRHR 169
Cdd:NF033858 161 DEPTTGVDplsrRQ----FWELIDRIRAE 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-211 |
2.46e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDgRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQ----TKFSGTITKAKKlkiGYVPQKL 76
Cdd:PRK10418 1 MPQQIELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGK---PVAPCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 77 K--------------LNdslPLN------VERFLKLTGKFSQQEILEALKLVG---AEHLQKSNMHQLSGGENQRVLIAR 133
Cdd:PRK10418 77 RgrkiatimqnprsaFN---PLHtmhthaRETCLALGKPADDATLTAALEAVGlenAARVLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 134 SLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHgRIVEQGDVETLFNAP 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-180 |
2.81e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.93 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 3 NLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQklklnDSl 82
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ-----DH- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 plnVERF---LKLTGKFSQ--QE---------ILEALkLVGAEHLQKSnMHQLSGGENQRVLIARSLLRRPDLLVLDEPA 148
Cdd:PRK15064 392 ---AYDFendLTLFDWMSQwrQEgddeqavrgTLGRL-LFSQDDIKKS-VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
170 180 190
....*....|....*....|....*....|....*...
gi 873911691 149 QGVD------VQGQIDLYDlidtirhrfGCAVFmVSHD 180
Cdd:PRK15064 467 NHMDmesiesLNMALEKYE---------GTLIF-VSHD 494
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-147 |
2.94e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.14 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 22 NISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------------KAKKLKIGYVPQKLKLndsLP-LN 85
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlfdaekgiclPPEKRRIGYVFQDARL---FPhYK 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873911691 86 VERFLKL-TGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:PRK11144 93 VRGNLRYgMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-205 |
2.95e-15 |
|
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: 73.17 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 30 GRITTLIGPNGAGKSTLVKVVLGLQT-----------------KFSGT-----ITKAK--KLKIGYVPQKLklnDSLPL- 84
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKpnlgkfddppdwdeildEFRGSelqnyFTKLLegDVKVIVKPQYV---DLIPKa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 85 ---NVERFLKLTGKFSQQEIL-EALKLvgaEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLY 160
Cdd:cd03236 103 vkgKVGELLKKKDERGKLDELvDQLEL---RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 873911691 161 DLIDTIRhRFGCAVFMVSHDLhLVMAKTDDVIClhhhiCCSGAPA 205
Cdd:cd03236 180 RLIRELA-EDDNYVLVVEHDL-AVLDYLSDYIH-----CLYGEPG 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-196 |
3.42e-15 |
|
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: 71.73 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 11 SVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKklKIGYVPQK--LkLNDSLPLNVeR 88
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEpwI-QNGTIRENI-L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 89 FLKltgKFSQQEILEALKlvgAEHLQK--SNMHQ------------LSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:cd03250 88 FGK---PFDEERYEKVIK---ACALEPdlEILPDgdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 873911691 155 GQIDLYDliDTIRH--RFGCAVFMVSHDLHLVMaKTDDVICLHH 196
Cdd:cd03250 162 VGRHIFE--NCILGllLNNKTRILVTHQLQLLP-HADQIVVLDN 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-207 |
3.57e-15 |
|
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: 74.98 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 19 VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-----TKAK------KLKIGYVPQKLKL-NDSLPLNV 86
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIiidglNIAKiglhdlRFKITIIPQDPVLfSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 87 ERFlkltGKFSQQEILEALKLV-----------GAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQG 155
Cdd:TIGR00957 1381 DPF----SQYSDEEVWWALELAhlktfvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 156 QidlyDLID-TIRHRF-GCAVFMVSHDLHLVMAKTDDVICLHHHICCSGAPADI 207
Cdd:TIGR00957 1457 D----NLIQsTIRTQFeDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
10-153 |
3.69e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.41 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQ----TkfSGTIT-------------KAKKlKIGYV 72
Cdd:COG0396 6 LHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyevT--SGSILldgedilelspdeRARA-GIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQklklndsLP-----LNVERFLK----------LTGKFSQQEILEALKLVG--AEHLQKS-NMHqLSGGENQRVLIARS 134
Cdd:COG0396 83 FQ-------YPveipgVSVSNFLRtalnarrgeeLSAREFLKLLKEKMKELGldEDFLDRYvNEG-FSGGEKKRNEILQM 154
|
170
....*....|....*....
gi 873911691 135 LLRRPDLLVLDEPAQGVDV 153
Cdd:COG0396 155 LLLEPKLAILDETDSGLDI 173
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-152 |
4.35e-15 |
|
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: 74.37 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEF--DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKvvlgLQTKF----SGTIT---------KAKKLK 68
Cdd:TIGR02203 330 DVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVN----LIPRFyepdSGQILldghdladyTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 --IGYVPQKLKL-NDSLPLNVErfLKLTGKFSQQEILEALKlvgAEHLQK--------------SNMHQLSGGENQRVLI 131
Cdd:TIGR02203 406 rqVALVSQDVVLfNDTIANNIA--YGRTEQADRAEIERALA---AAYAQDfvdklplgldtpigENGVLLSGGQRQRLAI 480
|
170 180
....*....|....*....|.
gi 873911691 132 ARSLLRRPDLLVLDEPAQGVD 152
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALD 501
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-179 |
4.78e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.81 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRK------VLDNISLNLERGRITTLIGPNGAGKSTLVK-------------VVLGLQTKFSGTI 61
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnallipsegkvYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 62 TKAKKlKIGYVPQKLKlNDSLPLNVER---F----LKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARS 134
Cdd:PRK13633 81 WDIRN-KAGMVFQNPD-NQIVATIVEEdvaFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 873911691 135 LLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSH 179
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-189 |
5.33e-15 |
|
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: 74.07 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-----------TK--------AKKLkIG 70
Cdd:TIGR03269 290 ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKpgpdgrgrAKRY-IG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKLN------DSLPLNVErfLKLTGKFSQQEILEALKLVG-----AEHLQKSNMHQLSGGENQRVLIARSLLRRP 139
Cdd:TIGR03269 369 ILHQEYDLYphrtvlDNLTEAIG--LELPDELARMKAVITLKMVGfdeekAEEILDKYPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 873911691 140 DLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTD 189
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-152 |
5.75e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 3 NLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-------------------K 63
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslsqqkgliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 64 AKKLKIGYVPQKLKL---NDSLPLNVERFLKLTGKFSQQEILEALKL---VGAEHLQKSNMHQLSGGENQRVLIARSLLR 137
Cdd:PRK11264 82 QLRQHVGFVFQNFNLfphRTVLENIIEGPVIVKGEPKEEATARARELlakVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170
....*....|....*
gi 873911691 138 RPDLLVLDEPAQGVD 152
Cdd:PRK11264 162 RPEVILFDEPTSALD 176
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-181 |
6.62e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.27 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITkakklkigYVPQKLKLND 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH--------YRMRDGQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 81 --SLPLNVERFLKLT--GkFSQQEILEALKL--------------VGAEH-----------LQKSNM---------HQLS 122
Cdd:PRK11701 75 lyALSEAERRRLLRTewG-FVHQHPRDGLRMqvsaggnigerlmaVGARHygdiratagdwLERVEIdaariddlpTTFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 123 GGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDL 181
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDL 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-163 |
7.57e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK--------LKIGYVPQKLKLNDSLPL--N 85
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaEACHYLGHRNAMKPALTVaeN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 86 VE---RFLKlTGKFSQQEILEALKLVGAEHLQKSNmhqLSGGENQRVLIARSLL-RRPdLLVLDEPAQGVDVQGQIDLYD 161
Cdd:PRK13539 94 LEfwaAFLG-GEELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVsNRP-IWILDEPTAALDAAAVALFAE 168
|
..
gi 873911691 162 LI 163
Cdd:PRK13539 169 LI 170
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-183 |
7.70e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----TKAKK---------LKIG 70
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgEPIRRqrdeyhqdlLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPqklKLNDSL-PL-NVERFLKLTGKFSQQEILEALK---LVGAEHLQksnMHQLSGGENQRVLIARSLLRRPDLLVLD 145
Cdd:PRK13538 81 HQP---GIKTELtALeNLRFYQRLHGPGDDEALWEALAqvgLAGFEDVP---VRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 873911691 146 EPAQGVDVQGQIDLYDLIDtiRH--RFGCAVFMVSHDLHL 183
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLA--QHaeQGGMVILTTHQDLPV 192
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-192 |
1.36e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.73 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----------TKAKKL-----KIGYV---PQKLKLN 79
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditithkTKDKYIrpvrkRIGMVfqfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DslplNVERFLKLTGKFSQQEILEA--------LKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGV 151
Cdd:PRK13646 101 D----TVEREIIFGPKNFKMNLDEVknyahrllMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 873911691 152 DVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVI 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-194 |
1.53e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.97 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 22 NISLNLErGRITtLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKlnDSLPLNVERFLKLTGKFS---Q 98
Cdd:PLN03073 529 NFGIDLD-SRIA-MVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHV--DGLDLSSNPLLYMMRCFPgvpE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 99 QEI---LEALKLVGAEHLQKsnMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGqidLYDLIDTIRhRFGCAVF 175
Cdd:PLN03073 605 QKLrahLGSFGVTGNLALQP--MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLV-LFQGGVL 678
|
170
....*....|....*....
gi 873911691 176 MVSHDLHLVMAKTDDVICL 194
Cdd:PLN03073 679 MVSHDEHLISGSVDELWVV 697
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-179 |
1.88e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI------------------- 61
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIlidgqemrfasttaalaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 62 --------------TKAKKLKIGYVPQKLKLNDSLPLNverflkltgkfsqQEILEALKLVGAEHLQKSNMHQLSGGENQ 127
Cdd:PRK11288 81 vaiiyqelhlvpemTVAENLYLGQLPHKGGIVNRRLLN-------------YEAREQLEHLGVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 873911691 128 RVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSH 179
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSH 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-207 |
2.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGR---KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-KAKKL--------- 67
Cdd:PRK13642 1 MNKILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKiDGELLtaenvwnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 -KIGYV---PQKLKLNDSLPLNVERFLKLTGkFSQQEIL----EALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRP 139
Cdd:PRK13642 81 rKIGMVfqnPDNQFVGATVEDDVAFGMENQG-IPREEMIkrvdEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 140 DLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVmAKTDDVICLHH-HICCSGAPADI 207
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAgEIIKEAAPSEL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-192 |
4.33e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGR-------------KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK--LK 68
Cdd:PRK15079 8 LLEVADLKVHFDIKdgkqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdlLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLND----------SL------------PLNVERflkltGKFSQQEILEALKL----VG-AEHLQKSNMHQL 121
Cdd:PRK15079 88 MKDDEWRAVRSDiqmifqdplaSLnprmtigeiiaePLRTYH-----PKLSRQEVKDRVKAmmlkVGlLPNLINRYPHEF 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 122 SGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-207 |
5.31e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLKIGYVPQKLKLNDSLP- 83
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdisprsplDAVKKGMAYITESRRDNGFFPn 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 ------LNVERFLKLTG----------KFSQQEILEALKLVGAE-HLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:PRK09700 356 fsiaqnMAISRSLKDGGykgamglfheVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 147 PAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVIclhhhICCSGAPADI 207
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIA-----VFCEGRLTQI 490
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-196 |
6.10e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL------QTKFSGTI---------TKAKK 66
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVlyfgkdifqIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 67 LK--IGYVPQKLKLNDSLPL--NVERFLKLTGKFSQQEIL----EALKLVG----AEHLQKSNMHQLSGGENQRVLIARS 134
Cdd:PRK14246 88 LRkeVGMVFQQPNPFPHLSIydNIAYPLKSHGIKEKREIKkiveECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 135 LLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFgcAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYN 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-154 |
9.34e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 9.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQtkfSGTITKAK-KLKIGYVPQKLKLNDSLPLNVER 88
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCvDVPDNQFGREASLIDAIGRKGDF 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 89 FLKLtgkfsqqEILEALKLVGAeHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:COG2401 113 KDAV-------ELLNAVGLSDA-VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-217 |
1.04e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.55 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTK----------FSG------TITKAKKL-------------- 67
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtadrfrWNGidllklSPRERRKIigreiamifqepss 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 ------KIGYvpqklKLNDSLPLNverflKLTGKFSQ------QEILEALKLVGA---EHLQKSNMHQLSGGENQRVLIA 132
Cdd:COG4170 101 cldpsaKIGD-----QLIEAIPSW-----TFKGKWWQrfkwrkKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 133 RSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHhhicC-----SGAPADI 207
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLY----CgqtveSGPTEQI 246
|
250
....*....|...
gi 873911691 208 K---HHPSYIALF 217
Cdd:COG4170 247 LkspHHPYTKALL 259
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-184 |
1.27e-13 |
|
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: 68.27 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGR---KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK----LKIGYVP 73
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKLNDSLPLNVERFLK------LTGKfSQQEILEALklvgaehlQKSNMH-------------------QLSGGENQR 128
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQdniaygLQSC-SFECVKEAA--------QKAHAHsfiselasgydtevgekgsQLSGGQKQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 129 VLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLI-DTIRHRfgcAVFMVSHDLHLV 184
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALyDWPERR---TVLVIAHRLSTV 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-181 |
1.37e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFD-GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLK 68
Cdd:COG3845 255 EVVLEVENLSVRDDrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgeditglsprERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVP---QK--------------LKLNDSLPLNVERFL--KLTGKFSQqEILEALKLVGAEHLQKsnMHQLSGGENQRV 129
Cdd:COG3845 335 VAYIPedrLGrglvpdmsvaenliLGRYRRPPFSRGGFLdrKAIRAFAE-ELIEEFDVRTPGPDTP--ARSLSGGNQQKV 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 873911691 130 LIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDL 181
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDL 462
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-155 |
1.70e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.88 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTkfSGTITkakklkiGYVpqklkLNDSLPLNVErF 89
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVIT-------GEI-----LINGRPLDKN-F 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 90 LKLTGKFSQQEILEALKLVgAEHLQKS-NMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQG 155
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTV-REALRFSaLLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-217 |
2.66e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.91 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 24 SLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI---------------TKAKKLKIGYVPQKLKLNDSLPL--NV 86
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaelREVRRKKIAMVFQSFALMPHMTVldNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 87 ERFLKLTG---KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLI 163
Cdd:PRK10070 128 AFGMELAGinaEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 164 DTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPS--YIALF 217
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNgEVVQVGTPDEILNNPAndYVRTF 264
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-196 |
3.63e-13 |
|
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: 66.79 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK------LKIGYVP-----QKLKLNDSLpln 85
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllgLGGGFNPeltgrENIYLNGRL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 86 verfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDT 165
Cdd:cd03220 112 ----LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE 187
|
170 180 190
....*....|....*....|....*....|.
gi 873911691 166 IRHRfGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:cd03220 188 LLKQ-GKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-184 |
8.20e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---------KAKKLK-----IGYVPQ--------KLK 77
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlSPGKLQalrrdIQFIFQdpyasldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 78 LNDSL--PLNVERFLKltGKFSQQEILEALKLVG--AEHLQKSNmHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDV 153
Cdd:PRK10261 420 VGDSImePLRVHGLLP--GKAAAARVAWLLERVGllPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190
....*....|....*....|....*....|.
gi 873911691 154 QGQIDLYDLIDTIRHRFGCAVFMVSHDLHLV 184
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVV 527
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-169 |
1.70e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 13 EFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLG-LQTK-FSGTI-------TKAKKLKIGYVPQKLKLNDSLP 83
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNnFTGTIlannrkpTKQILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 ----LNVERFLKLTGKFSQQEILEALKLVGAE-HLQK--------SNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQG 150
Cdd:PLN03211 157 vretLVFCSLLRLPKSLTKQEKILVAESVISElGLTKcentiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170
....*....|....*....
gi 873911691 151 VDVQGQIDLYDLIDTIRHR 169
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQK 255
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-152 |
2.03e-12 |
|
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: 66.89 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKakKLKIGYVPQKLKL-NDSLPLNVERFLKLTGKFSQ 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--KGSVAYVPQQAWIqNDSLRENILFGKALNEKYYQ 731
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 99 QeILEALKLVG-AEHLQKSNMHQ-------LSGGENQRVLIARSLLRRPDLLVLDEPAQGVD 152
Cdd:TIGR00957 732 Q-VLEACALLPdLEILPSGDRTEigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-182 |
2.20e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.11 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-----DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-------TKAKKLK---- 68
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvTKLPEYKraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 IGYVPQKLKLNDSLPLNVE------------RFLK--LTGKFSQ--QEILEALKLvGAEHLQKSNMHQLSGGENQrvliA 132
Cdd:COG1101 82 IGRVFQDPMMGTAPSMTIEenlalayrrgkrRGLRrgLTKKRRElfRELLATLGL-GLENRLDTKVGLLSGGQRQ----A 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 133 RSLL----RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLH 182
Cdd:COG1101 157 LSLLmatlTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-179 |
2.27e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDsvsVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----------TKAKKLKIG 70
Cdd:PRK13540 1 MLDVIELD---FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqsikkdLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKLNDSLPLNVERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQG 150
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180
....*....|....*....|....*....
gi 873911691 151 VDVQGQIDLYDLIDTIRHRfGCAVFMVSH 179
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAK-GGAVLLTSH 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-192 |
3.55e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSvefdGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-KAKKLKI---------GY 71
Cdd:PRK11288 255 EVRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYlDGKPIDIrsprdairaGI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 V--PQKLKLNDSLP-------LNVE-RFLKLTGKF---SQQEILEALKLVGAEHLQKSNMHQ----LSGGENQRVLIARS 134
Cdd:PRK11288 331 MlcPEDRKAEGIIPvhsvadnINISaRRHHLRAGClinNRWEAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRW 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 135 LLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIV 467
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-210 |
4.01e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.95 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEF----------------------DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 59 GTITKAKK------LKIGYVPQklklndslplnverflkLTGK-----------FSQQEILEALKLVGA-----EHL-QK 115
Cdd:COG1134 81 GRVEVNGRvsalleLGAGFHPE-----------------LTGReniylngrllgLSRKEIDEKFDEIVEfaelgDFIdQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 116 snMHQLSGGENQRVLIARSLLRRPDLLVLDEpAQGV-DVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:COG1134 144 --VKTYSSGMRARLAFAVATAVDPDILLVDE-VLAVgDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|....*..
gi 873911691 195 HH-HICCSGAPADIKHH 210
Cdd:COG1134 220 EKgRLVMDGDPEEVIAA 236
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
5-153 |
4.14e-12 |
|
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: 64.20 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTK--FSGTIT-------------KAKK--- 66
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYevTSGTILfkgqdllelepdeRARAglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 67 ------LKIGYVPQKLKLNDSL----------PLNVERFLKLTgkfsqQEILEALKLVGaEHLQKSNMHQLSGGENQRVL 130
Cdd:TIGR01978 81 lafqypEEIPGVSNLEFLRSALnarrsargeePLDLLDFEKLL-----KEKLALLDMDE-EFLNRSVNEGFSGGEKKRNE 154
|
170 180
....*....|....*....|...
gi 873911691 131 IARSLLRRPDLLVLDEPAQGVDV 153
Cdd:TIGR01978 155 ILQMALLEPKLAILDEIDSGLDI 177
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-213 |
4.54e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 22 NISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLNDSLPLNVERF------------ 89
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVrgadmamifqep 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 90 -----------------LKLTGKFSQQE-------ILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLD 145
Cdd:PRK10261 114 mtslnpvftvgeqiaesIRLHQGASREEamveakrMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 146 EPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHPSY 213
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQgEAVETGSVEQIFHAPQH 262
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-192 |
4.99e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLN-------------------- 79
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgfalvteerrstgiyayldi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 --DSLPLNVERFLKLTG-------KFSQQEILEALKLVGAEHlqKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQG 150
Cdd:PRK10982 344 gfNSLISNIRNYKNKVGlldnsrmKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 873911691 151 VDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRIL 462
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-187 |
7.31e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.87 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 15 DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLqTKFSGTIT-----------KAKKLKIGYVPQklklNDSLP 83
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKingielreldpESWRKHLSWVGQ----NPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 L-----NVerflkLTGKF--SQQEILEALKLVGA-----------EHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLD 145
Cdd:PRK11174 436 HgtlrdNV-----LLGNPdaSDEQLQQALENAWVseflpllpqglDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 873911691 146 EPAQGVDVQG-QIDLYDLIDTIRHRfgcAVFMVSH---DLH-----LVMAK 187
Cdd:PRK11174 511 EPTASLDAHSeQLVMQALNAASRRQ---TTLMVTHqleDLAqwdqiWVMQD 558
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-211 |
1.34e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 22 NISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-KAKKLKIG---YVPQKLK-------------------L 78
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiDDHPLHFGdysYRSQRIRmifqdpstslnprqrisqiL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 79 NDSLPLNVErflkLTGKFSQQEILEALKLVG--AEHLQKSNmHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQ 156
Cdd:PRK15112 111 DFPLRLNTD----LEPEQREKQIIETLRQVGllPDHASYYP-HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 157 IDLYDLIDTIRHRFGCAVFMVSHdlHLVMAK--TDDVICLHH-HICCSGAPADIKHHP 211
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQ--HLGMMKhiSDQVLVMHQgEVVERGSTADVLASP 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-195 |
2.23e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGT---------------ITKAKKLKIGYVPQKLKLNDSL 82
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvatldadaLAQLRREHFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 PL--NVERFLKLTG------KFSQQEILEALKLVGAEHLQKSnmhQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ 154
Cdd:PRK10535 102 TAaqNVEVPAVYAGlerkqrLLRAQELLQRLGLEDRVEYQPS---QLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 873911691 155 GQIDLYDLIDTIRHRfGCAVFMVSHDLHlVMAKTDDVICLH 195
Cdd:PRK10535 179 SGEEVMAILHQLRDR-GHTVIIVTHDPQ-VAAQAERVIEIR 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-179 |
2.91e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.85 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 3 NLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVV-----LGLQTKFSGTI----TKAKKLKIGYVP 73
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVyldgQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKL---------------NDSLPLNVERFLKltgkfSQQEILEALKlvgaEHLQKSNM------------HQLSGGEN 126
Cdd:PRK14247 82 RRVQMvfqipnpipnlsifeNVALGLKLNRLVK-----SKKELQERVR----WALEKAQLwdevkdrldapaGKLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 873911691 127 QRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFgcAVFMVSH 179
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-179 |
3.54e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 15 DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-----QTKFSG------TITKAKKlKIGYVPQKL-KLNDSL 82
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLlstegEIQIDGvswnsvTLQTWRK-AFGVIPQKVfIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 83 PLNVERFlkltGKFSQQEILEALKLVGAehlqKSNMHQ---------------LSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:TIGR01271 1309 RKNLDPY----EQWSDEEIWKVAEEVGL----KSVIEQfpdkldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190
....*....|....*....|....*....|....
gi 873911691 148 AQGVD-VQGQIdlydLIDTIRHRFG-CAVFMVSH 179
Cdd:TIGR01271 1381 SAHLDpVTLQI----IRKTLKQSFSnCTVILSEH 1410
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-181 |
4.45e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLV-----------------KVVLGLQTKFSGTITKA 64
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlndlipgfrvegKVTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 65 K-KLKIGYVPQKLK-LNDSLPLNVERFLKLTG-KFSQQEILE-ALKLVGAEHLQKSNMHQ----LSGGENQRVLIARSLL 136
Cdd:PRK14243 88 EvRRRIGMVFQKPNpFPKSIYDNIAYGARINGyKGDMDELVErSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 873911691 137 RRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFgcAVFMVSHDL 181
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM 210
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-180 |
4.99e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLK--------------- 68
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqqdpprnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 69 --------IGYVPQKLK---------LNDSLPLNVERFLKLTGKFSQQ----------EILEALKLVGAEHLQksnmhQL 121
Cdd:PRK11147 83 vydfvaegIEEQAEYLKryhdishlvETDPSEKNLNELAKLQEQLDHHnlwqlenrinEVLAQLGLDPDAALS-----SL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 122 SGGENQRVLIARSLLRRPDLLVLDEPAQGVDvqgqIDLYDLIDTIRHRFGCAVFMVSHD 180
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHD 212
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-192 |
5.31e-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: 59.64 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVkvvlglqtkfsgtitkakkLKIGYVPQKLKLNDSLPLNVERFLKLTGKfsqq 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-------------------NEGLYASGKARLISFLPKFSRNKLIFIDQ---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 100 eiLEALKLVGAEHLQ-KSNMHQLSGGENQRVLIARSLLRRPD--LLVLDEPAQGVDvqgQIDLYDLIDTIRH--RFGCAV 174
Cdd:cd03238 68 --LQFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDINQLLEVIKGliDLGNTV 142
|
170
....*....|....*...
gi 873911691 175 FMVSHDLHlVMAKTDDVI 192
Cdd:cd03238 143 ILIEHNLD-VLSSADWII 159
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-154 |
7.43e-11 |
|
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: 60.04 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLK---------------IGYVPQK-LKLN 79
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKpWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSL--------PLNVERFLKLTGKFSQQEILEALKLVGAEHLQKSNMHqLSGGENQRVLIARSLLRRPDLLVLDEPAQGV 151
Cdd:cd03290 93 ATVeenitfgsPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
...
gi 873911691 152 DVQ 154
Cdd:cd03290 172 DIH 174
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-211 |
9.81e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 18 KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYVPQKLKLNDSLPLNV 86
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvngqtinlvrdKDGQLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 87 ERF-------------------LKLTGKFSQQEILEALKLVG-AEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDE 146
Cdd:PRK10619 99 QHFnlwshmtvlenvmeapiqvLGLSKQEARERAVKYLAKVGiDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 147 PAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICLHH-HICCSGAPADIKHHP 211
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQgKIEEEGAPEQLFGNP 243
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-192 |
1.10e-10 |
|
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: 59.12 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 27 LERGRITTLIGPNGAGKSTLVKVVLGlQTKFSGTITKAKKLKIGYVPQKLKLndslplnverflkltgkfsqqeilealk 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAG-QLIPNGDNDEWDGITPVYKPQYIDL---------------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 107 lvgaehlqksnmhqlSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMA 186
Cdd:cd03222 73 ---------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDY 137
|
....*.
gi 873911691 187 KTDDVI 192
Cdd:cd03222 138 LSDRIH 143
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-212 |
1.71e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.00 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLV------------KVVL-GLQTKFSGTITKAKKLkI 69
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLAlhlngllrpqkgKVLVsGIDTGDFSKLQGIRKL-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 70 GYVPQKLK-------LNDSLPLNVERfLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLL 142
Cdd:PRK13644 80 GIVFQNPEtqfvgrtVEEDLAFGPEN-LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 143 VLDEPAQGVDVQGQIDLYDLIDTIrHRFGCAVFMVSHDLHLVMAKTDDVICLHHHICCSGAPADIKHHPS 212
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-181 |
1.94e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.87 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 15 DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL-----QTKFSG----TITKAKKLK-IGYVPQKLKL-NDSLP 83
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLlntegDIQIDGvswnSVPLQKWRKaFGVIPQKVFIfSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 LNVERFlkltGKFSQQEILEALKLVGAehlqKSNMHQ---------------LSGGENQRVLIARSLLRRPDLLVLDEPA 148
Cdd:cd03289 95 KNLDPY----GKWSDEEIWKVAEEVGL----KSVIEQfpgqldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190
....*....|....*....|....*....|....*
gi 873911691 149 QGVD-VQGQIdlydLIDTIRHRF-GCAVFMVSHDL 181
Cdd:cd03289 167 AHLDpITYQV----IRKTLKQAFaDCTVILSEHRI 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-181 |
2.36e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.34 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 9 SVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKL-----------------KIGY 71
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifnyrdvlefrrRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 72 VPQK-----LKLNDSLPLNVeRFLKLTGKFSQQEILEA-LKLVGAEHLQKSNMH----QLSGGENQRVLIARSLLRRPDL 141
Cdd:PRK14271 106 LFQRpnpfpMSIMDNVLAGV-RAHKLVPRKEFRGVAQArLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 873911691 142 LVLDEPAQGVDVQGQIDLYDLIDTIRHRFgcAVFMVSHDL 181
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNL 222
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-179 |
3.16e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 19 VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-------TKAKKLK----IGYVPqKLKLNDSLPLNVE 87
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRfmayLGHLP-GLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 88 RFLKLTGKFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGqIDLYDLIDTIR 167
Cdd:PRK13543 105 FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG-ITLVNRMISAH 183
|
170
....*....|..
gi 873911691 168 HRFGCAVFMVSH 179
Cdd:PRK13543 184 LRGGGAALVTTH 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-218 |
3.48e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 13 EFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKklKIGYVPQK-LKLNDSLPLNV----- 86
Cdd:PTZ00243 669 ELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQaWIMNATVRGNIlffde 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 87 ERFLKLTG--KFSQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQ-GQIDLYDLI 163
Cdd:PTZ00243 747 EDAARLADavRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECF 826
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 873911691 164 dtIRHRFGCAVFMVSHDLHLVmAKTDDVICLHH-HICCSGAPADIKHHPSYIALFG 218
Cdd:PTZ00243 827 --LGALAGKTRVLATHQVHVV-PRADYVVALGDgRVEFSGSSADFMRTSLYATLAA 879
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-152 |
4.25e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRK-VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTK---FSGTIT------KAKKLKI--GYVPQKLKLNDSLP 83
Cdd:TIGR00955 36 PRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLlngmpiDAKEMRAisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 84 ----LNVERFLKLTGKFSQ-------QEILEALKLVGAEHL---QKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQ 149
Cdd:TIGR00955 116 vrehLMFQAHLRMPRRVTKkekrervDEVLQALGLRKCANTrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
...
gi 873911691 150 GVD 152
Cdd:TIGR00955 196 GLD 198
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-216 |
5.23e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.66 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 4 LIQLDSVSVEF---DGR-KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLqTKFSGTIT----------------K 63
Cdd:PRK15093 3 LLDIRNLTIEFktsDGWvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrmrfddidllrlspR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 64 AKKLKIGY-------VPQK---------LKLNDSLPLNV------ERFlkltgKFSQQEILEALKLVG-AEH--LQKSNM 118
Cdd:PRK15093 82 ERRKLVGHnvsmifqEPQScldpservgRQLMQNIPGWTykgrwwQRF-----GWRKRRAIELLHRVGiKDHkdAMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 119 HQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFGCAVFMVSHDLHLVMAKTDDVICLHHHI 198
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260
....*....|....*....|..
gi 873911691 199 CCSGAPAD----IKHHPSYIAL 216
Cdd:PRK15093 237 TVETAPSKelvtTPHHPYTQAL 258
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-181 |
5.41e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQ--TKFSGTITK------------AKKLKIGYVPQKLK---- 77
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKdgkevdvstvsdAIDAGLAYVTEDRKgygl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 78 -LNDSLPLNVErfLKLTGKFSQQEIL-EALKLVGAEHLQKSnMH-----------QLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:NF040905 352 nLIDDIKRNIT--LANLGKVSRRGVIdENEEIKVAEEYRKK-MNiktpsvfqkvgNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190
....*....|....*....|....*....|....*..
gi 873911691 145 DEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDL 181
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSEL 464
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-181 |
2.08e-09 |
|
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: 57.72 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 3 NLIQLDSVSVEFDGRK--VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKK----------LKIG 70
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisdvhQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 71 YVPQKLKLNDSLPLNVERFL--KLTGkFSQQEILE----ALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLyaRLRG-VPAEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190
....*....|....*....|....*....|....*..
gi 873911691 145 DEPAQGVDVQGQIDLYDLIDTIRhRFGCAVFMVSHDL 181
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSM 2130
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-147 |
2.10e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.16 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGR-KVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKL---------KIGYVPQ 74
Cdd:PRK11650 4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadrDIAMVFQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 75 KLKL--NDSLPLNVERFLKLTGkFSQQEI----LEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEP 147
Cdd:PRK11650 84 NYALypHMSVRENMAYGLKIRG-MPKAEIeervAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-179 |
2.11e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 1 MDNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKV------------VLGLQTKFSGTITKAK--- 65
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearVEGEVRLFGRNIYSPDvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 66 ---KLKIGYVPQ------KLKLNDSLPLNVERFLKLTGKFSQQEILE-ALKLVGAEHLQKSNMH----QLSGGENQRVLI 131
Cdd:PRK14267 81 ievRREVGMVFQypnpfpHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALWDEVKDRLNdypsNLSGGQRQRLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 873911691 132 ARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRFgcAVFMVSH 179
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-177 |
2.69e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 24 SLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSG-------TIT-----KAKKLkigyVPQKLKLNDSLPLNVERflK 91
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfsHITrlsfeQLQKL----VSDEWQRNNTDMLSPGE--D 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 92 LTGKFSQQEILEALK----------LVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYD 161
Cdd:PRK10938 97 DTGRTTAEIIQDEVKdparceqlaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170
....*....|....*.
gi 873911691 162 LIDTIRHRfGCAVFMV 177
Cdd:PRK10938 177 LLASLHQS-GITLVLV 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-199 |
4.50e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKklKIGYVPQ-------KLKLNDSLPLNVER 88
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQtswimpgTIKDNIIFGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 89 FlKLTGKFSQQEILEALKLVGaehlQKSNMH------QLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYD- 161
Cdd:TIGR01271 516 Y-RYTSVIKACQLEEDIALFP----EKDKTVlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEs 590
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 873911691 162 -----LIDTIRhrfgcaVFMVSHDLHLvmAKTDDVICLHHHIC 199
Cdd:TIGR01271 591 clcklMSNKTR------ILVTSKLEHL--KKADKILLLHEGVC 625
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-194 |
4.62e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI----------TKAKKLKIGYVPQKLKLN 79
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgkeidfkSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSLPLNVERFLKL-----TGKF-SQQEILEALKLVGAEhLQ-----KSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPA 148
Cdd:PRK10982 84 LVLQRSVMDNMWLgryptKGMFvDQDKMYRDTKAIFDE-LDididpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 873911691 149 QGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDVICL 194
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITIL 207
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-197 |
7.91e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 2 DNLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLG--LQTKFSGTItKAKKLKIGYVPQKLKLN 79
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDI-LFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSLPL-----------NVERFLKLT----GKFSQQEILEALKL--VGAEHLQKSNMHQ----------LSGGENQRVLIA 132
Cdd:CHL00131 84 LGIFLafqypieipgvSNADFLRLAynskRKFQGLPELDPLEFleIINEKLKLVGMDPsflsrnvnegFSGGEKKRNEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 133 RSLLRRPDLLVLDEPAQGVDvqgqidlydlIDTIRhrfgcavfMVSHDLHLVMAKTDDVICLHHH 197
Cdd:CHL00131 164 QMALLDSELAILDETDSGLD----------IDALK--------IIAEGINKLMTSENSIILITHY 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-179 |
1.60e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.34 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-------TKAKKLKIGYVPQKLKLNdsLPLNVERF 89
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncniNNIAKPYCTYIGHNLGLK--LEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 90 LKLTGKF--SQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIdTIR 167
Cdd:PRK13541 91 LKFWSEIynSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMK 169
|
170
....*....|..
gi 873911691 168 HRFGCAVFMVSH 179
Cdd:PRK13541 170 ANSGGIVLLSSH 181
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-181 |
2.07e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRK---VLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT------------KAKKLKI 69
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 70 GYVPQK-LKLNDSLPLNVERFL--------------------------------KLTGKFS-------QQEILEALK--- 106
Cdd:PTZ00265 463 GVVSQDpLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDLNdmsnttdSNELIEMRKnyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 107 ------------------LVGA-----EHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLI 163
Cdd:PTZ00265 543 tikdsevvdvskkvlihdFVSAlpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250
....*....|....*...
gi 873911691 164 DTIRHRFGCAVFMVSHDL 181
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRL 640
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-182 |
2.43e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 23 ISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTI-TKAKKLKIGYVPQKLKLNDSLPLNVERFLKLTGKFSQ--- 98
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKpan 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 99 ----QEILEALKL---VGAEHLQKSNMhQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLY-DLIDTIRHRf 170
Cdd:PRK10522 422 palvEKWLERLKMahkLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYqVLLPLLQEM- 499
|
170
....*....|..
gi 873911691 171 GCAVFMVSHDLH 182
Cdd:PRK10522 500 GKTIFAISHDDH 511
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-191 |
2.99e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 13 EFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGL--------QTKFSGTITKAKKLK------IGYVPQKLKL 78
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGEVCRFKDIRdsealgIVIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 79 ndsLPL-----NVerFL---KLTGKF-----SQQEILEALKLVGAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLD 145
Cdd:NF040905 90 ---IPYlsiaeNI--FLgneRAKRGVidwneTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 873911691 146 EPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMVSHDLHLVMAKTDDV 191
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSI 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-154 |
3.47e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTkfSGTITKAKKL------------KIGYVPQK-L 76
Cdd:TIGR00956 769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLvngrpldssfqrSIGYVQQQdL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 77 KLNDSL---PLNVERFLKLTGKFSQQE----ILEALKLVGAEHLQKSNMHQLSGGEN----QRVLIARSLLRRPDLLV-L 144
Cdd:TIGR00956 847 HLPTSTvreSLRFSAYLRQPKSVSKSEkmeyVEEVIKLLEMESYADAVVGVPGEGLNveqrKRLTIGVELVAKPKLLLfL 926
|
170
....*....|
gi 873911691 145 DEPAQGVDVQ 154
Cdd:TIGR00956 927 DEPTSGLDSQ 936
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-181 |
4.91e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.21 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTL---VKVVLGLQTKfsgTITKAKKLKIGYvpqklklndslplnverflkltgkF 96
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTIldaIGLALGGAQS---ATRRRSGVKAGC------------------------I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 97 SQQEILEALKLVgaehlqksnmHQLSGGENQRVLIA-----RSLLRRPdLLVLDEPAQGVDVQ-GQIdlydLIDTIRHRF 170
Cdd:cd03227 64 VAAVSAELIFTR----------LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRdGQA----LAEAILEHL 128
|
170
....*....|...
gi 873911691 171 --GCAVFMVSHDL 181
Cdd:cd03227 129 vkGAQVIVITHLP 141
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-180 |
1.04e-07 |
|
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: 50.06 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 29 RGRITTLIGPNGAGKSTLVKVVLGLqtkfsgtitkakklkigyvpqklklndsLPLNVERFLKLTGkfsqQEILEALKLV 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE----------------------------LGPPGGGVIYIDG----EDILEEVLDQ 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873911691 109 GAEHLQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDT-----IRHRFGCAVFMVSHD 180
Cdd:smart00382 49 LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSEKNLTVILTTND 125
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-152 |
2.58e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.26 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEF-DGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT-----------KAKKLKIGYV 72
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsslshSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQK-LKLNDSLPLNVerflKLTGKFSQQEILEALKLVGAEHLQKS---NMH--------QLSGGENQRVLIARSLLRRPD 140
Cdd:PRK10790 421 QQDpVVLADTFLANV----TLGRDISEEQVWQALETVQLAELARSlpdGLYtplgeqgnNLSVGQKQLLALARVLVQTPQ 496
|
170
....*....|..
gi 873911691 141 LLVLDEPAQGVD 152
Cdd:PRK10790 497 ILILDEATANID 508
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
21-146 |
2.71e-07 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain] Cd Length: 197 Bit Score: 49.77 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 21 DNISLNLERGrITTLIGPNGAGKSTLV---KVVLGLQTK------------FSGTiTKAKKLKIGYVPQKLKLNDSLPL- 84
Cdd:cd03278 14 DKTTIPFPPG-LTAIVGPNGSGKSNIIdaiRWVLGEQSAkslrgekmsdviFAGS-ETRKPANFAEVTLTFDNSDGRYSi 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873911691 85 ----NVERFLKLTGKFSQqeilealklvgaehlqksNMHQLSGGEnqRVLIARSLL-----RRPD-LLVLDE 146
Cdd:cd03278 92 isqgDVSEIIEAPGKKVQ------------------RLSLLSGGE--KALTALALLfaifrVRPSpFCVLDE 143
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-161 |
3.00e-07 |
|
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: 50.24 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 16 GRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKklKIGYVPQ-------KLKLNDSLPLNVE- 87
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQfswimpgTIKENIIFGVSYDe 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 88 -RFLKLTGKFSQQEILEALKLVGAEHLQKSNMhQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYD 161
Cdd:cd03291 127 yRYKSVVKACQLEEDITKFPEKDNTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-152 |
4.06e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.48 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVKVvlgLQTKFSgtITKAKklkIGYvpqklklnDSLPLNVERFLKLTGKF 96
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSL---IQRHFD--VSEGD---IRF--------HDIPLTKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 97 -------------------------SQQEILEALKLvgaehlqkSNMHQ-------------------LSGGENQRVLIA 132
Cdd:PRK10789 392 avvsqtpflfsdtvannialgrpdaTQQEIEHVARL--------ASVHDdilrlpqgydtevgergvmLSGGQKQRISIA 463
|
170 180
....*....|....*....|
gi 873911691 133 RSLLRRPDLLVLDEPAQGVD 152
Cdd:PRK10789 464 RALLLNAEILILDDALSAVD 483
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-176 |
5.95e-07 |
|
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: 48.80 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 13 EFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVV---LGLQTKFSGTIT----KAKKLK------IGYVPQklklN 79
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHyngiPYKEFAekypgeIIYVSE----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSLP--LNVERFLKLtgkfsqqeileALKLVGAEHLQKsnmhqLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQI 157
Cdd:cd03233 92 DVHFptLTVRETLDF-----------ALRCKGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170
....*....|....*....
gi 873911691 158 DLYDLIDTIRHRFGCAVFM 176
Cdd:cd03233 156 EILKCIRTMADVLKTTTFV 174
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-182 |
7.20e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQ--------------- 74
Cdd:PRK15064 7 ITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQdqfafeeftvldtvi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 75 -------KLKLND----SLPLNVE----RFLKLTGKFSQQ----------EILeaLKLVGAEHLQKSNMHQLSGGENQRV 129
Cdd:PRK15064 87 mghtelwEVKQERdriyALPEMSEedgmKVADLEVKFAEMdgytaearagELL--LGVGIPEEQHYGLMSEVAPGWKLRV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 873911691 130 LIARSLLRRPDLLVLDEPAQGVDvqgqidlydlIDTIR------HRFGCAVFMVSHDLH 182
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLD----------INTIRwledvlNERNSTMIIISHDRH 213
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
102-192 |
1.30e-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: 49.24 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 102 LEALKLVGAEHLQ-KSNMHQLSGGENQRVLIARSLLRR---PDLLVLDEPAQGVDVQGQIDLYDLIDTIRHRfGCAVFMV 177
Cdd:TIGR00630 810 LQTLCDVGLGYIRlGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTVVVI 888
|
90
....*....|....*
gi 873911691 178 SHDLHLVmaKTDDVI 192
Cdd:TIGR00630 889 EHNLDVI--KTADYI 901
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-195 |
1.43e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 5 IQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKV---------------------VLG-----LQTKFS 58
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYmamhaidgipkncqilhveqeVVGddttaLQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 59 GTITKAKKLK--IGYVPQKLKL-------NDSLPLNVERFLKLTGKfSQQEILEALKLVGA-----------------EH 112
Cdd:PLN03073 258 TDIERTQLLEeeAQLVAQQRELefetetgKGKGANKDGVDKDAVSQ-RLEEIYKRLELIDAytaearaasilaglsftPE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 113 LQKSNMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLydliDTIRHRFGCAVFMVSHDLHLVMAKTDDVI 192
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL----ETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
...
gi 873911691 193 CLH 195
Cdd:PLN03073 413 HLH 415
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
121-169 |
1.72e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.72e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 121 LSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQ-------IDLYDLID----TIRHR 169
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEkliektiVDIKDKADktiiTIAHR 1418
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-192 |
4.26e-06 |
|
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: 46.48 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLV----------KVVLGLQT---KFSGTITKAKKLKI-GYVP-----QKL---- 76
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAyarQFLGQMDKPDVDSIeGLSPaiaidQKTtsrn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 77 ---------KLNDSLPLnverflkLTGKFSQQEILEALKLVGAEHLQKS-NMHQLSGGENQRVLIARSLLRRPD--LLVL 144
Cdd:cd03270 91 prstvgtvtEIYDYLRL-------LFARVGIRERLGFLVDVGLGYLTLSrSAPTLSGGEAQRIRLATQIGSGLTgvLYVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 873911691 145 DEPAQGVDvqgQIDLYDLIDTIRH--RFGCAVFMVSHDLHLVMAkTDDVI 192
Cdd:cd03270 164 DEPSIGLH---PRDNDRLIETLKRlrDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-152 |
4.40e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 30 GRITTLIGPNGAGKSTLVKVVLGLQT--------KFSGTITKAKKL-KI-GYVPQ------KLKLNDSLPLNVerFLKLT 93
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggyiegdiRISGFPKKQETFaRIsGYCEQndihspQVTVRESLIYSA--FLRLP 983
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 94 GKFSQQEIL----EALKLVGAEHLQKS-----NMHQLSGGENQRVLIARSLLRRPDLLVLDEPAQGVD 152
Cdd:PLN03140 984 KEVSKEEKMmfvdEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
123-185 |
2.19e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 2.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 123 GGEN----QRVLI--ARSLLRRPDLLVLDEPAQGVDVQGQIdlydLID-TIRHRF-GCAVFMVSHDLHLVM 185
Cdd:PLN03130 1371 AGENfsvgQRQLLslARALLRRSKILVLDEATAAVDVRTDA----LIQkTIREEFkSCTMLIIAHRLNTII 1437
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
100-223 |
2.56e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 100 EILEALKLVGAEHLQKSN-MHQLSGGENQRVLIARSLL---RRPDLLVLDEPAQGV---DVQGQID-LYDLIDTirhrfG 171
Cdd:PRK00635 788 EKIHALCSLGLDYLPLGRpLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYvLQSLTHQ-----G 862
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 172 CAVFMVSHDLHLVmaKTDDVIC--------LHHHICCSGAPADI--KHHPSYIAL--FGTATQE 223
Cdd:PRK00635 863 HTVVIIEHNMHVV--KVADYVLelgpeggnLGGYLLASCSPEELihLHTPTAKALrpYLSSPQE 924
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
123-185 |
2.67e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 2.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873911691 123 GGEN----QRVLI--ARSLLRRPDLLVLDEPAQGVDVqgQIDlyDLID-TIRHRF-GCAVFMVSHDLHLVM 185
Cdd:PLN03232 1368 GGENfsvgQRQLLslARALLRRSKILVLDEATASVDV--RTD--SLIQrTIREEFkSCTMLVIAHRLNTII 1434
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-184 |
2.69e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKAKKLKIGYVPQKLKLNDSLPLNVErFLKLTGKFSQQ 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIE-FKMLCMGFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 100 EILEAL-KLVGAEHLQK---SNMHQLSGGENQRVLIARSLLRRPDLLVLDEpaqGVDVQGQIDLYDLIDTIrHRF---GC 172
Cdd:PRK13546 119 EIKAMTpKIIEFSELGEfiyQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCLDKI-YEFkeqNK 194
|
170
....*....|..
gi 873911691 173 AVFMVSHDLHLV 184
Cdd:PRK13546 195 TIFFVSHNLGQV 206
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-179 |
3.36e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 3 NLIQLDSVSVEFDGRKVLDNISLNLERGRITTLIGPNGAG--KSTLVKVVLGLQT-----KFSGTITKAKKLK--IG-YV 72
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrpwRF*TWCANRRALRrtIG*HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 73 PQKLKLNDSLP-----LNVERFLKLTGKFSQ---QEILEALKLVGAEHLQKSnmhQLSGGENQRVLIARSLLRRPDLLVL 144
Cdd:NF000106 92 PVR*GRRESFSgrenlYMIGR*LDLSRKDARaraDELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 873911691 145 DEPAQGVDVQGQIDLYDLIDTIRhRFGCAVFMVSH 179
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQ 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-214 |
4.52e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 19 VLDNISLNLERGRITTLIGPNGAGKSTLVKV------VLGLQTKFSGTITKAKKLK-----IGYVPQKLKLND-SLPLNV 86
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTfmrmveVCGGEIRVNGREIGAYGLRelrrqFSMIPQDPVLFDgTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 87 ERFLKLtgkfSQQEILEALKLVG-----AEHLQKSNMHQLSGGEN----QRVL--IARSLLRRPDLLVL-DEPAQGVD-- 152
Cdd:PTZ00243 1405 DPFLEA----SSAEVWAALELVGlrervASESEGIDSRVLEGGSNysvgQRQLmcMARALLKKGSGFILmDEATANIDpa 1480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 153 VQGQIDlydliDTIRHRFGC-AVFMVSHDLHLVmAKTDDVICLHHHICCS-GAPADIKHHPSYI 214
Cdd:PTZ00243 1481 LDRQIQ-----ATVMSAFSAyTVITIAHRLHTV-AQYDKIIVMDHGAVAEmGSPRELVMNRQSI 1538
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
100-192 |
4.53e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.76 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 100 EILEALKLVGAEHLQ-KSNMHQLSGGENQRVLIARSLLRR---PDLLVLDEPAQGV---DVQGQID-LYDLIDTirhrfG 171
Cdd:cd03271 148 RKLQTLCDVGLGYIKlGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKLLEvLQRLVDK-----G 222
|
90 100
....*....|....*....|.
gi 873911691 172 CAVFMVSHDLHLVmaKTDDVI 192
Cdd:cd03271 223 NTVVVIEHNLDVI--KCADWI 241
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
10-153 |
4.56e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 10 VSVEfdGRKVLDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQ--TKFSGTIT-KAKKL------------------- 67
Cdd:PRK09580 9 VSVE--DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEfKGKDLlelspedragegifmafqy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 68 --KIGYVPQKLKLNDSlpLNVERflkltgKFSQQEIL----------EALKLVG--AEHLQKSNMHQLSGGENQRVLIAR 133
Cdd:PRK09580 87 pvEIPGVSNQFFLQTA--LNAVR------SYRGQEPLdrfdfqdlmeEKIALLKmpEDLLTRSVNVGFSGGEKKRNDILQ 158
|
170 180
....*....|....*....|
gi 873911691 134 SLLRRPDLLVLDEPAQGVDV 153
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDI 178
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-196 |
5.67e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTIT---KAKKLKIGYvpqklKLNDSLP--LNVErfLK-LT 93
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDikgSAALIAISS-----GLNGQLTgiENIE--LKgLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 94 GKFSQQEILEAL-KLVGAEHLQKSnMHQ----LSGGENQRVLIARSLLRRPDLLVLDEPAQGVDVQGQIDLYDLIDTIRH 168
Cdd:PRK13545 113 MGLTKEKIKEIIpEIIEFADIGKF-IYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKE 191
|
170 180
....*....|....*....|....*...
gi 873911691 169 RfGCAVFMVSHDLHLVMAKTDDVICLHH 196
Cdd:PRK13545 192 Q-GKTIFFISHSLSQVKSFCTKALWLHY 218
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
11-64 |
1.04e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 1.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 873911691 11 SVEFDGRKVLDNISLNLerGRITTLIGPNGAGKSTLVKVVLGLQTKFSGTITKA 64
Cdd:COG4637 4 RIRIKNFKSLRDLELPL--GPLTVLIGANGSGKSNLLDALRFLSDAARGGLQDA 55
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
24-152 |
3.88e-04 |
|
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: 40.66 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 24 SLNLergrittLIGPNGAGKSTLV-KVVLGLQTKfSGTITKAKKL--------KIGYVPQKLKLN------DSLPL---- 84
Cdd:cd03277 24 SLNM-------IIGPNGSGKSSIVcAICLGLGGK-PKLLGRAKKVgefvkrgcDEGTIEIELYGNpgniqvDNLCQflpq 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873911691 85 -NVERFLKLtgkfSQQEILeaLKLVGAEHLQKSNMHQLSGGEnqRV------LIARSLLRRPDLLVLDEPAQGVD 152
Cdd:cd03277 96 dRVGEFAKL----SPIELL--VKFREGEQLQELDPHHQSGGE--RSvstmlyLLSLQELTRCPFRVVDEINQGMD 162
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
5-69 |
5.04e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 5.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873911691 5 IQLDSVSVEfdGRKVLDNISLNLERG-RITTLIGPNGAGKSTLVK-VVLGLQTKFSGTIT-KAKKLKI 69
Cdd:COG3950 1 MRIKSLTIE--NFRGFEDLEIDFDNPpRLTVLVGENGSGKTTLLEaIALALSGLLSRLDDvKFRKLLI 66
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
11-57 |
1.11e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.57 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 873911691 11 SVEFDGRKVLDNISLNLerGRITTLIGPNGAGKSTLVKVVLGL-QTKF 57
Cdd:COG4938 3 SISIKNFGPFKEAELEL--KPLTLLIGPNGSGKSTLIQALLLLlQSNF 48
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-195 |
1.99e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.83 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 20 LDNISLNLERGrITTLIGPNGAGKSTLVK---VVLGLQTK--------FSGTITKAKKLKIGYV---------PQKLKLN 79
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEalrLLLGPSSSrkfdeedfYLGDDPDLPEIEIELTfgsllsrllRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 80 DSLPLnVERFLKLTGKFSQ--QEILEALKLVGAEHLQKSNM----------------------------HQLSGGENQRV 129
Cdd:COG3593 93 DKEEL-EEALEELNEELKEalKALNELLSEYLKELLDGLDLelelsldeledllkslslriedgkelplDRLGSGFQRLI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 873911691 130 LIA--RSLLR-----RPDLLVLDEPAQGVDVQGQIDLYDLIDTIRhRFGCAVFMVSHDLHLV-MAKTDDVICLH 195
Cdd:COG3593 172 LLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELS-EKPNQVIITTHSPHLLsEVPLENIRRLR 244
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
74-180 |
2.16e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873911691 74 QKLKLNDSLPLNVERFLKltgkfsqqEILEALKL---VGAEHLQKS-NMHQLSGGENQRVLIARSLLRRPD--LLVLDEP 147
Cdd:TIGR00630 446 NQLTLTPEEKKIAEEVLK--------EIRERLGFlidVGLDYLSLSrAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEP 517
|
90 100 110
....*....|....*....|....*....|....*
gi 873911691 148 AQGVDvqgQIDLYDLIDTIRH--RFGCAVFMVSHD 180
Cdd:TIGR00630 518 SIGLH---QRDNRRLINTLKRlrDLGNTLIVVEHD 549
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-150 |
4.50e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 4.50e-03
10 20 30
....*....|....*....|....*....|...
gi 873911691 121 LSGGENQRVLIARSLLRRPD---LLVLDEPAQG 150
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTG 863
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
14-47 |
6.77e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 6.77e-03
10 20 30
....*....|....*....|....*....|....
gi 873911691 14 FDGRkvldniSLNLERGRITTLIGPNGAGKSTLV 47
Cdd:pfam13555 12 FDGH------TIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-147 |
7.38e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 7.38e-03
10 20 30
....*....|....*....|....*....|
gi 873911691 121 LSGGENQRVLIARSLLRRPD---LLVLDEP 147
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEP 856
|
|
| COG1373 |
COG1373 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
17-48 |
9.87e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 36.85 E-value: 9.87e-03
10 20 30
....*....|....*....|....*....|..
gi 873911691 17 RKVLDNISLNLERGRITTLIGPNGAGKSTLVK 48
Cdd:COG1373 7 RKILDKLLKLLDNRKAVVITGPRQVGKTTLLK 38
|
|
| |
