|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-249 |
6.75e-90 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 265.70 E-value: 6.75e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWrASAQRRLECRRRIG 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGL-HVRRswadrLRREVAdlvglrngTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAF 160
Cdd:COG1126 81 MVFQQFNLFpHLTVLENVTLAPiKVKK-----MSKAEA--------EERAMELLERVGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
....*....
gi 909710455 241 EDDRTQQFI 249
Cdd:COG1126 228 QHERTRAFL 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-236 |
2.15e-81 |
|
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: 243.63 E-value: 2.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEP-----PRDGSLEYGGTDVWrASAQRRLEC 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIY-DLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 RRRIGMVFQEASLFDASVRRNAEYGLHVRRSWadrLRREVADLVglrngtsdaMEALETVGLED--KLEQHAGSLSGGEA 155
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIK---LKEELDERV---------EEALRKAALWDevKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDR 235
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 909710455 236 I 236
Cdd:cd03260 227 I 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-249 |
2.03e-72 |
|
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: 221.39 E-value: 2.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQ 86
Cdd:COG1127 10 NLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDA-SVRRNAEYGLHVRRSWADRLRREVadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:COG1127 90 GGALFDSlTVFENVAFPLREHTDLSEAEIREL------------VLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAViLGDG-IIEVGETDRIFEDpEDD 243
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAV-LADGkIIAEGTPEELLAS-DDP 235
|
....*.
gi 909710455 244 RTQQFI 249
Cdd:COG1127 236 WVRQFL 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-251 |
3.81e-72 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 221.06 E-value: 3.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLL----RLLALFEPPR-DGSLEYGGTDVwRASAQRRLECRRRIGMVFQ 86
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMNDLIPGARvEGEILLDGEDI-YDPDVDVVELRRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDASVRRNAEYGLHVRRswaDRLRREVADLVglrngtsdaMEALETVGL----EDKLEQHAGSLSGGEAQRVAFAR 162
Cdd:COG1117 100 KPNPFPKSIYDNVAYGLRLHG---IKSKSELDEIV---------EESLRKAALwdevKDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPED 242
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246
|
....*....
gi 909710455 243 DRTQQFIDG 251
Cdd:COG1117 247 KRTEDYITG 255
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-248 |
1.77e-69 |
|
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: 213.52 E-value: 1.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQ 86
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDA-SVRRNAEYGLHVRRSWADRLRREVadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:cd03261 85 SGALFDSlTVFENVAFPLREHTRLSEEEIREI------------VLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPeDDR 244
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPL 231
|
....
gi 909710455 245 TQQF 248
Cdd:cd03261 232 VRQF 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-237 |
7.64e-64 |
|
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: 199.88 E-value: 7.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRRIG 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---ARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASL-FDASVRRNAEYGLHVRRSWADRLRREVADLVglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRYPHLGLFGRPSAEDREAV---------EEALERTGLEHLADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIF 237
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-241 |
1.47e-63 |
|
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: 198.33 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRI 81
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLR---ELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQ--EASLFDASVRRNAEYGL-HVRRSwadrlRREVADLVglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRV 158
Cdd:COG1122 78 GLVFQnpDDQLFAPTVEEDVAFGPeNLGLP-----REEIRERV---------EEALELVGLEHLADRPPHELSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDG-IIEVGETDRIF 237
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRV-IVLDDGrIVADGTPREVF 222
|
....
gi 909710455 238 EDPE 241
Cdd:COG1122 223 SDYE 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-226 |
2.95e-63 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 196.96 E-value: 2.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIG 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDASVRRNAEYGLHVRRSWADRLRrevadlvglrngtsdAMEALETVGL-EDKLEQHAGSLSGGEAQRVAFA 161
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDRER---------------ALELLERLGLpPDILDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVaVILGDG 226
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRV-LTLEAG 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-250 |
1.33e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 199.53 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 9 EHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQEA 88
Cdd:COG1135 12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 89 SLFDA-SVRRNAEYGL-HVRRSWADRLRReVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:COG1135 92 NLLSSrTVAENVALPLeIAGVPKAEIRKR-VAEL-------------LELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAViLGDG-IIEVGETDRIFEDPEDDR 244
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAV-LENGrIVEQGPVLDVFANPQSEL 236
|
....*.
gi 909710455 245 TQQFID 250
Cdd:COG1135 237 TRRFLP 242
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-241 |
4.77e-60 |
|
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: 189.33 E-value: 4.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 9 EHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQEA 88
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 89 SLFDA-SVRRNAEYGLHVRRSWADRLRREVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:cd03258 92 NLLSSrTVFENVALPLEIAGVPKAEIEERVLEL-------------LELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPE 241
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-250 |
7.93e-60 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 197.05 E-value: 7.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQ--EASLFDA 93
Cdd:COG1123 279 RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQdpYSSLNPR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 -SVRRNAEYGLHVRRSWADRLRREvadlvglrngtsDAMEALETVGL-EDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:COG1123 359 mTVGDIIAEPLRLHGLLSRAERRE------------RVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQFID 250
Cdd:COG1123 427 ILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLA 506
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-249 |
1.17e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 192.24 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRRIG 82
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-----KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGLHVRR-SWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAF 160
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGLRMRGvPKAEIRAR--------------VAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRntavienaVREA---------GDRGIGVAIATHDMNQARRIADQVAViLGDGIIE-V 230
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAK--------LREEmreelrrlqRELGITFIYVTHDQEEALALADRIAV-MNDGRIEqV 217
|
250
....*....|....*....
gi 909710455 231 GETDRIFEDPEDDRTQQFI 249
Cdd:COG3842 218 GTPEEIYERPATRFVADFI 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-239 |
3.90e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 187.19 E-value: 3.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAqrrlECRRRIG 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA----EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDA-SVRRNAEYglhvrrswadrlrreVADLVGLRNGTSD--AMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRF---------------FARLYGLPRKEARerIDELLELFGLTDAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAvILGDG-IIEVGETD---- 234
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVA-IIDKGrIVADGTPDelka 220
|
....*
gi 909710455 235 RIFED 239
Cdd:COG1131 221 RLLED 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-229 |
5.23e-59 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 186.40 E-value: 5.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDE----TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECR 78
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 79 RR-IGMVFQEASLFDA-SVRRNAEYGLHVRR-SWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEA 155
Cdd:COG1136 85 RRhIGFVFQFFNLLPElTALENVALPLLLAGvSRKERRER--------------ARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRiADQVaVILGDGIIE 229
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVTHDPELAAR-ADRV-IRLRDGRIV 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-255 |
6.91e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 187.19 E-value: 6.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGY-GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVF 85
Cdd:COG3638 7 NLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRIGMIF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 QEASLFD-ASVRRNAeygLHVR-------RSWADRLRREVADLvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQR 157
Cdd:COG3638 87 QQFNLVPrLSVLTNV---LAGRlgrtstwRSLLGLFPPEDRER---------ALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVaVILGDGIIevgetdrI 236
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRiAREDGITVVVNLHQVDLARRYADRI-IGLRDGRV-------V 226
|
250
....*....|....*....
gi 909710455 237 FEDPEDDRTQQFIDGelIY 255
Cdd:COG3638 227 FDGPPAELTDAVLRE--IY 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-228 |
9.78e-59 |
|
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: 185.77 E-value: 9.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDE----TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECR 78
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 79 RR-IGMVFQEASLF-DASVRRNAEYGLHVR-RSWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEA 155
Cdd:cd03255 81 RRhIGFVFQSFNLLpDLTALENVELPLLLAgVPKKERRER--------------AEELLERVGLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRiADQVaVILGDGII 228
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDPELAEY-ADRI-IELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-229 |
1.57e-57 |
|
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: 182.33 E-value: 1.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRRIGMVFQ 86
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFD-ASVRRNAEYGLHVRRSWADRLRREVadlvglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:cd03259 80 DYALFPhLTVAENIAFGLKLRGVPKAEIRARV-------------RELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREA-GDRGIGVAIATHDMNQARRIADQVAViLGDGIIE 229
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAV-MNEGRIV 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-245 |
1.86e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 183.37 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRAsaqrrlecRRRIGMVFQ 86
Cdd:COG1121 11 NLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--------RRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASL---FDASVRRNAEYGLHVRRSWADRLRREVADLVglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFARA 163
Cdd:COG1121 83 RAEVdwdFPITVRDVVLMGRYGRRGLFRRPSRADREAV---------DEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 164 LAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAViLGDGIIEVGETDRIFEDPEDD 243
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLL-LNRGLVAHGPPEEVLTPENLS 232
|
..
gi 909710455 244 RT 245
Cdd:COG1121 233 RA 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-255 |
1.22e-56 |
|
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: 181.15 E-value: 1.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 5 TVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRIGMV 84
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 85 FQEAslfdasvrrnaeYG-LHVRRSWADRLRrEVADLVGLRNGTSDAMEALETVGL-EDKLEQHAGSLSGGEAQRVAFAR 162
Cdd:COG1124 85 FQDP------------YAsLHPRHTVDRILA-EPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREA-GDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPE 241
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
250
....*....|....
gi 909710455 242 DDRTQQFIDGELIY 255
Cdd:COG1124 232 HPYTRELLAASLAF 245
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-221 |
7.94e-56 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 179.52 E-value: 7.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGY----GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASaqrrlecrRRIG 82
Cdd:COG1116 12 GVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--------PDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFD-ASVRRNAEYGLHVRR-SWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAF 160
Cdd:COG1116 84 VVFQEPALLPwLTVLDNVALGLELRGvPKAERRER--------------ARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAV 221
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-222 |
6.18e-55 |
|
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: 175.73 E-value: 6.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 4 QTVGVEHGYGD--ETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRI 81
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL---TKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQ--EASLFDASVRRNAEYGLhVRRSWADRLRREVADlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:cd03225 78 GLVFQnpDDQFFGPTVEEEVAFGL-ENLGLPEEEIEERVE------------EALELVGLEGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-222 |
9.79e-55 |
|
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: 175.03 E-value: 9.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 11 GYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRAsaqrrlecRRRIGMVFQEASL 90
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 ---FDASVRRNAEYGLHVRRSWADRLRREVADLVglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:cd03235 80 drdFPISVRDVVLMGLYGHKGLFRRLSKADKAKV---------DEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-228 |
1.23e-54 |
|
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: 175.03 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlECRRRIG 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIN-ELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGLHVRRSWAdrlRREVADLvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLAPIKVKGMS---KAEAEER---------ALELLEKVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDGII 228
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRV-IFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-249 |
4.55e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 177.96 E-value: 4.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRRIGMVFQ 86
Cdd:COG3839 8 NVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-----DRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDA-SVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:COG3839 83 SYALYPHmTVYENIAFPLKLRKVPKAEIDRRVR-------------EAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDP--RNTAVIE--NAVREagdRGIGVAIATHDMNQARRIADQVAViLGDGIIE-VGETDRIFEDP 240
Cdd:COG3839 150 REPKVFLLDEPLSNLDAklRVEMRAEikRLHRR---LGTTTIYVTHDQVEAMTLADRIAV-MNDGRIQqVGTPEELYDRP 225
|
....*....
gi 909710455 241 EDDRTQQFI 249
Cdd:COG3839 226 ANLFVAGFI 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-241 |
8.55e-53 |
|
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: 171.08 E-value: 8.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRRIG 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGLHVRRS---WADRLRREVADLVGlrngtsDAMEALETVGLEDKLEQHAGSLSGGEAQRV 158
Cdd:cd03219 79 RTFQIPRLFpELTVLENVMVAAQARTGsglLLARARREEREARE------RAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFE 238
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
...
gi 909710455 239 DPE 241
Cdd:cd03219 233 NPR 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-222 |
2.21e-52 |
|
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: 169.57 E-value: 2.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDE----TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASaqrrlecr 78
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 79 RRIGMVFQEASLFD-ASVRRNAEYGLHVRRsWADRLRREVadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQR 157
Cdd:cd03293 73 PDRGYVFQQDALLPwLTVLDNVALGLELQG-VPKAEARER------------AEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDP--RNT--AVIENAVREagdRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDAltREQlqEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-216 |
6.09e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 168.31 E-value: 6.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQEASL-F 91
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQDFRLlP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DASVRRNAEYGLHVrrswADRLRREVADLVglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:COG2884 93 DRTVYENVALPLRV----TGKSRKEIRRRV---------REVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMN-----QARRIA 216
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElvdrmPKRVLE 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-231 |
6.13e-52 |
|
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: 166.84 E-value: 6.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRRIGMVFQ 86
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 easlfdasvrrnaeyglhvrrswadrlrrevadlvglrngtsdameALETVGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:cd03214 81 ----------------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 167 DPDFLLLDEPTSDLDPRNT-AVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVG 231
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-249 |
2.06e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 170.71 E-value: 2.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVW-RASAQrrlecRR 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPR-----ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 80 RIGMVFQEASLF-DASVRRNAEYGLHVRRSWADRLRREVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGGEAQRV 158
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEL-------------LELVQLEGLADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVaVILGDG-IIEVGETDRI 236
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRV-VVMNQGrIEQVGTPDEV 221
|
250
....*....|...
gi 909710455 237 FEDPEDDRTQQFI 249
Cdd:COG1118 222 YDRPATPFVARFL 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-248 |
5.85e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 166.73 E-value: 5.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDV---WRASAQRRLEC 77
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 RRRIGMVFQEASLF-DASVRRN-AEYGLHVRRswadrLRREVAdlvglrngTSDAMEALETVGLEDKLEQHAGSLSGGEA 155
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENlIEAPCKVLG-----LSKEQA--------REKAMKLLARLRLTDKADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDr 235
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS- 226
|
250
....*....|...
gi 909710455 236 IFEDPEddrTQQF 248
Cdd:COG4161 227 HFTQPQ---TEAF 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-231 |
6.74e-51 |
|
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: 165.76 E-value: 6.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 5 TVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMV 84
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 85 FQEA-SLFDA--SVRRN-AEYGLHVRRSWADRLRREVadlvglrngtsdAMEALETVGL-EDKLEQHAGSLSGGEAQRVA 159
Cdd:cd03257 88 FQDPmSSLNPrmTIGEQiAEPLRIHGKLSKKEARKEA------------VLLLLVGVGLpEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGD-RGIGVAIATHDMNQARRIADQVAVILGDGIIEVG 231
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-222 |
3.52e-50 |
|
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: 162.36 E-value: 3.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLEcRRRIG 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL-RRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGlhvrrswadrlrrevadlvglrngtsdamealetvgledkleqhagsLSGGEAQRVAFA 161
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG-----------------------------------------------LSGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVL 174
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-250 |
1.50e-49 |
|
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: 162.74 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDV--WRASAQRRLecRRRIGM 83
Cdd:cd03256 5 NLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInkLKGKALRQL--RRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 84 VFQEASLFD-ASVRRNAEYGLHVRRSWadrlrreVADLVGL--RNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAF 160
Cdd:cd03256 83 IFQQFNLIErLSVLENVLSGRLGRRST-------WRSLFGLfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVaVILGDGIIevgetdrIFED 239
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADRI-VGLKDGRI-------VFDG 227
|
250
....*....|.
gi 909710455 240 PEDDRTQQFID 250
Cdd:cd03256 228 PPAELTDEVLD 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-251 |
1.58e-49 |
|
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: 163.58 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEhgygdetileNVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRR-R 80
Cdd:cd03294 34 TGQTVGVN----------DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLF-DASVRRNAEYGLHVR-RSWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRV 158
Cdd:cd03294 104 ISMVFQSFALLpHRTVLENVAFGLEVQgVPRAEREER--------------AAEALELVGLEGWEHKYPDELSGGMQQRV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDP-RNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAvILGDG-IIEVGETDRI 236
Cdd:cd03294 170 GLARALAVDPDILLMDEAFSALDPlIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIA-IMKDGrLVQVGTPEEI 248
|
250
....*....|....*
gi 909710455 237 FEDPEDDRTQQFIDG 251
Cdd:cd03294 249 LTNPANDYVREFFRG 263
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-249 |
8.38e-49 |
|
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: 160.97 E-value: 8.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRR 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-----ERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLF-DASVRRNAEYGLHVRRswadRLRREVADLVGLRngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:cd03296 76 VGFVFQHYALFrHMTVFDNVAFGLRVKP----RSERPPEAEIRAK-----VHELLKLVQLDWLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFE 238
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 909710455 239 DPEDDRTQQFI 249
Cdd:cd03296 227 HPASPFVYSFL 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-248 |
3.67e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 159.41 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDV---WRASAQRRLEC 77
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 RRRIGMVFQEASLF-DASVRRN-AEYGLHVRRswadrLRREVAdlvglrngTSDAMEALETVGLEDKLEQHAGSLSGGEA 155
Cdd:PRK11124 81 RRNVGMVFQQYNLWpHLTVQQNlIEAPCRVLG-----LSKDQA--------LARAEKLLERLRLKPYADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDG-IIEVGETD 234
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRV-VYMENGhIVEQGDAS 226
|
250
....*....|....
gi 909710455 235 RiFEDPEddrTQQF 248
Cdd:PRK11124 227 C-FTQPQ---TEAF 236
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-219 |
3.88e-48 |
|
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: 158.16 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRR-RIGMVFQEASL 90
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRReKLGYLFQNFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 FDA-SVRRNAEYGL-HVRRSWADRLRREVadlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:TIGR03608 88 IENeTVEENLDLGLkYKKLSKKEKREKKK--------------EALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRiADQV 219
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRV 203
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-238 |
7.07e-48 |
|
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: 158.48 E-value: 7.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLECRRRIG 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----RKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDA-SVRRNAEYGLHVRRSWADRLRREVADLVglrngtsdamealETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELI-------------ELLGLEEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDG-IIEVGETDRIFE 238
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRV-VILHKGkVVAQGSLDELRE 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-222 |
1.04e-47 |
|
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: 155.48 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRRIGMVFQ 86
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 easlfdasvrrnaeyglhvrrswadrlrrevadlvglrngtsdamealetvgledkleqhagsLSGGEAQRVAFARALAY 166
Cdd:cd00267 81 ---------------------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-250 |
1.38e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 160.74 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQEASLFDAsvrr 97
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNLLSS---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 98 naeyglhvrrswadrlrREVADLVGLR---NGTSDA------MEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:PRK11153 97 -----------------RTVFDNVALPlelAGTPKAeikarvTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQ 247
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
...
gi 909710455 248 FID 250
Cdd:PRK11153 240 FIQ 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-249 |
1.61e-47 |
|
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: 157.40 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRRIGMVFQ 86
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLF-DASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:cd03300 80 NYALFpHLTVFENIAFGLRLKKLPKAEIKERVA-------------EALDLVQLEGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDP--RNTAVIEnaVREAGDR-GIGVAIATHDMNQARRIADQVAViLGDGIIE-VGETDRIFEDPE 241
Cdd:cd03300 147 NEPKVLLLDEPLGALDLklRKDMQLE--LKRLQKElGITFVFVTHDQEEALTMSDRIAV-MNKGKIQqIGTPEEIYEEPA 223
|
....*...
gi 909710455 242 DDRTQQFI 249
Cdd:cd03300 224 NRFVADFI 231
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-227 |
7.31e-47 |
|
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: 155.10 E-value: 7.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGY-GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQ 86
Cdd:TIGR02673 7 VSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLF-DASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:TIGR02673 87 DFRLLpDRTVYENVALPLEVRGKKEREIQRRVG-------------AALRQVGLEHKADAFPEQLSGGEQQRVAIARAIV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDGI 227
Cdd:TIGR02673 154 NSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRV-IILDDGR 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-241 |
9.06e-47 |
|
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: 159.11 E-value: 9.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQtVGVEHGYGDETIleNVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdVWRASAQRR---LEc 77
Cdd:COG4148 1 MMLE-VDFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARGIflpPH- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 RRRIGMVFQEASLFD-ASVRRNAEYGLhvRRSWADRLRREVADLVglrngtsdamealETVGLEDKLEQHAGSLSGGEAQ 156
Cdd:COG4148 76 RRRIGYVFQEARLFPhLSVRGNLLYGR--KRAPRAERRISFDEVV-------------ELLGIGHLLDRRPATLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 157 RVAFARALAYDPDFLLLDEPTSDLD-PRNTAV---IENAVREAgdrGIGVAIATHDMNQARRIADQVaVILGDG-IIEVG 231
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDlARKAEIlpyLERLRDEL---DIPILYVSHSLDEVARLADHV-VLLEQGrVVASG 216
|
250
....*....|
gi 909710455 232 ETDRIFEDPE 241
Cdd:COG4148 217 PLAEVLSRPD 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-228 |
1.13e-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: 153.32 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRasaqRRLECRRRIG 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDA-SVRRNAEYglhvrrswadrlrrevadlvglrngtsdamealetvgledkleqhagslSGGEAQRVAFA 161
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-------------------------------------------------SGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAvILGDGII 228
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVA-ILNNGRI 173
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-228 |
1.72e-46 |
|
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: 155.15 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQEASLFD 92
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRIGMIFQHYNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 -ASVRRNAeygLHVR-------RSWADRLRREvadlvglrnGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARAL 164
Cdd:TIGR02315 93 rLTVLENV---LHGRlgykptwRSLLGRFSEE---------DKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 165 AYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVaVILGDGII 228
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRiNKEDGITVIINLHQVDLAKKYADRI-VGLKAGEI 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-231 |
1.84e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 162.64 E-value: 1.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwRASAQRRLecRRRIGMVF 85
Cdd:COG1132 344 NVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI-RDLTLESL--RRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 QEASLFDASVRRNAEYGlhvrRSWADRLR-REVADLVGlrngtsdAMEALEtvGLEDKLEQHAG----SLSGGEAQRVAF 160
Cdd:COG1132 421 QDTFLFSGTIRENIRYG----RPDATDEEvEEAAKAAQ-------AHEFIE--ALPDGYDTVVGergvNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIAtHDMNQARRiADQVAViLGDG-IIEVG 231
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIA-HRLSTIRN-ADRILV-LDDGrIVEQG 556
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-249 |
2.27e-46 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 154.87 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlECRRRIGMVFQE 87
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 ASLF-DASVRRNAEYG-LHVRRSwadrLRREVADLvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:PRK09493 86 FYLFpHLTALENVMFGpLRVRGA----SKEEAEKQ---------ARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDRT 245
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
|
....
gi 909710455 246 QQFI 249
Cdd:PRK09493 233 QEFL 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-253 |
3.23e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 154.55 E-value: 3.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALF-----EPPRDGSLEYGGTDVWRASAQRrLECRRRIGMVFQ 86
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDT-VDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDASVRRNAEYGLHVrrswadrlrrevadlvglrNGTSDAM---EALET--VG------LEDKLEQHAGSLSGGEA 155
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRL-------------------KGIKDKQvldEAVEKslKGasiwdeVKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDR 235
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQ 233
|
250
....*....|....*...
gi 909710455 236 IFEDPEDDRTQQFIDGEL 253
Cdd:PRK14239 234 MFMNPKHKETEDYISGKF 251
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-250 |
4.03e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.52 E-value: 4.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRA---SAQRRL--ECRRRIGMVFQ 86
Cdd:PRK11264 13 FHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslSQQKGLirQLRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLF-DASVRRNAEYGLHVRRSWAdrlrREVAdlvglrngTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:PRK11264 93 NFNLFpHRTVLENIIEGPVIVKGEP----KEEA--------TARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDRT 245
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....*
gi 909710455 246 QQFID 250
Cdd:PRK11264 241 RQFLE 245
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-241 |
5.73e-46 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 154.04 E-value: 5.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRRIG 82
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--ARLGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGLHVRR--SWADRLRREVADLVGLRNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:COG0411 83 RTFQNPRLFpELTVLENVLVAAHARLgrGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAViLGDG-IIEVGETDRIF 237
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVV-LDFGrVIAEGTPAEVR 241
|
....
gi 909710455 238 EDPE 241
Cdd:COG0411 242 ADPR 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-241 |
6.08e-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: 160.45 E-value: 6.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 6 VGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPR---DGSLEYGGTDVWRASAQRRlecRRRIG 82
Cdd:COG1123 10 LSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR---GRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQE--ASLFDASVRRNAEYGLHVRR-SWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:COG1123 87 MVFQDpmTQLNPVTVGDQIAEALENLGlSRAEARAR--------------VLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFE 238
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
...
gi 909710455 239 DPE 241
Cdd:COG1123 233 APQ 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-253 |
7.24e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 153.92 E-value: 7.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLR----LLALFEPPR-DGSLEYGGTDVWRASAqrrLECRRRIGMVFQ 86
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDV---IELRRRVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EAS-LFDASVRRNAEYGLHVRRswADRLRREVADLVglrngtsdaMEALETVGL----EDKLEQHAGSLSGGEAQRVAFA 161
Cdd:PRK14247 90 IPNpIPNLSIFENVALGLKLNR--LVKSKKELQERV---------RWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAgDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPE 241
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
250
....*....|..
gi 909710455 242 DDRTQQFIDGEL 253
Cdd:PRK14247 238 HELTEKYVTGRL 249
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-222 |
7.54e-46 |
|
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: 152.59 E-value: 7.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRRIG 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGLHVRRSwaDRLRREVADLVGL--RngtsdamealetvgLEDKLEQHAGSLSGGEAQRVA 159
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLGAYARRR--AKRKARLERVYELfpR--------------LKERRKQLAGTLSGGEQQMLA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-231 |
8.54e-46 |
|
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: 162.70 E-value: 8.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDET--ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRRIGMV 84
Cdd:COG2274 478 NVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---RRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 85 FQEASLFDASVRRNaeygLHVRRSWADRlrrevadlvglrngtSDAMEALETVGLEDKLEQH-----------AGSLSGG 153
Cdd:COG2274 555 LQDVFLFSGTIREN----ITLGDPDATD---------------EEIIEAARLAGLHDFIEALpmgydtvvgegGSNLSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 154 EAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAgDRGIGVAIATHDMNQARRiADQVaVILGDG-IIEVG 231
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRL-ADRI-IVLDKGrIVEDG 691
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-251 |
1.11e-44 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 151.09 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLR----LLALFEPPR-DGSLEYGGTDVWrASAQRRLEC 77
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrLNDLIPGFRvEGKVTFHGKNLY-APDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 RRRIGMVFQEASLFDASVRRNAEYGLHVrrswadrlrrevadlvglrNGTSDAMEALETVGL---------EDKLEQHAG 148
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAYGARI-------------------NGYKGDMDELVERSLrqaalwdevKDKLKQSGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 149 SLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgIGVAIATHDMNQARRIADQVA---VILGD 225
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAffnVELTE 229
|
250 260 270
....*....|....*....|....*....|..
gi 909710455 226 G------IIEVGETDRIFEDPEDDRTQQFIDG 251
Cdd:PRK14243 230 GggrygyLVEFDRTEKIFNSPQQQATRDYVSG 261
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-208 |
1.15e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 149.17 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLECRRR 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLFDA-SVRRNAEYglhvrrswadrlrreVADLVGLRNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLRF---------------WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHD 208
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-222 |
1.79e-44 |
|
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: 147.53 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASaqrRLECRRR 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLFDASVRRNAeyglhvrrswadrlrrevadlvglrngtsdamealetvgledkleqhagsLSGGEAQRVAF 160
Cdd:cd03228 78 IAYVPQDPFLFSGTIRENI--------------------------------------------------LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAgDRGIGVAIATHDMNQARRiADQVAVI 222
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVL 167
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-249 |
3.22e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 148.75 E-value: 3.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDETIleNVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWR-ASAQRRlecrrrIGMVFQ 86
Cdd:COG3840 7 LTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlPPAERP------VSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDA-SVRRNAEYGLHvrrswaDRLRREVADlvglrngTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:COG3840 79 ENNLFPHlTVAQNIGLGLR------PGLKLTAEQ-------RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDR 244
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDElCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPA 225
|
....*
gi 909710455 245 TQQFI 249
Cdd:COG3840 226 LAAYL 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-254 |
3.83e-44 |
|
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: 148.64 E-value: 3.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecrrRIGMVFQEASLF-DASVR 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR-----DISYVPQNYALFpHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLHVRRSWADRLRREVadlvglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEP 176
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKV-------------LEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 177 TSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQFIDGELI 254
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-241 |
1.44e-43 |
|
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: 148.37 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDET-----ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIG 82
Cdd:TIGR04521 6 VSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQ--EASLFDASVRRNAEYGLhvrrswadrlrrevadlvglRN-GTSD------AMEALETVGLEDK-LEQHAGSLSG 152
Cdd:TIGR04521 86 LVFQfpEHQLFEETVYKDIAFGP--------------------KNlGLSEeeaeerVKEALELVGLDEEyLERSPFELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 153 GEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVG 231
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
250
....*....|
gi 909710455 232 ETDRIFEDPE 241
Cdd:TIGR04521 226 TPREVFSDVD 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-222 |
3.68e-43 |
|
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: 146.28 E-value: 3.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRR 80
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLF-DASVRRNAEYGLHVRRSWADRLRR--EVADL--VglrngtsdamealetvgLEDKLEQHAGSLSGGEA 155
Cdd:COG0410 80 IGYVPEGRRIFpSLTVEENLLLGAYARRDRAEVRADleRVYELfpR-----------------LKERRRQRAGTLSGGEQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVL 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-231 |
5.81e-43 |
|
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: 153.00 E-value: 5.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGY--GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRR 79
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 80 RIGMVFQEASLFDASVRRNaeygLHVRRSWADRLR-REVADLVGLrngtSDAMEALETvGLEDKLEQHAGSLSGGEAQRV 158
Cdd:COG4987 410 RIAVVPQRPHLFDTTLREN----LRLARPDATDEElWAALERVGL----GDWLAALPD-GLDTWLGEGGRRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGdRGIGVAIATHDMNQARRiADQVaVILGDG-IIEVG 231
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLER-MDRI-LVLEDGrIVEQG 551
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
12-253 |
5.88e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 146.48 E-value: 5.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDV-WRASAQRRLEC---------RRRI 81
Cdd:COG4598 18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrLKPDRDGELVPadrrqlqriRTRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQEASLFD-ASVRRN-AEYGLHVRRswadRLRREVADlvglrngtsDAMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:COG4598 98 GMVFQSFNLWShMTVLENvIEAPVHVLG----RPKAEAIE---------RAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDGII-EVGETDRIFE 238
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHV-VFLHQGRIeEQGPPAEVFG 243
|
250
....*....|....*
gi 909710455 239 DPEDDRTQQFIDGEL 253
Cdd:COG4598 244 NPKSERLRQFLSSSL 258
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-251 |
6.08e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 149.87 E-value: 6.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 4 QTVGVEhgygdetileNVSLAVPPGEVVAIIGPSGVGKTTLLRLLA-LFEPPRdGSLEYGGTDVWRASAQRRLECRR-RI 81
Cdd:COG4175 39 QTVGVN----------DASFDVEEGEIFVIMGLSGSGKSTLVRCLNrLIEPTA-GEVLIDGEDITKLSKKELRELRRkKM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQEASLF-DASVRRNAEYGLHVRR-SWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:COG4175 108 SMVFQHFALLpHRTVLENVAFGLEIQGvPKAERRER--------------AREALELVGLAGWEDSYPDELSGGMQQRVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDP--RntavienavREAGD----------RGIgVAIaTHDMNQARRIADQVAvILGDG- 226
Cdd:COG4175 174 LARALATDPDILLMDEAFSALDPliR---------REMQDellelqaklkKTI-VFI-THDLDEALRLGDRIA-IMKDGr 241
|
250 260
....*....|....*....|....*
gi 909710455 227 IIEVGETDRIFEDPEDDRTQQFIDG 251
Cdd:COG4175 242 IVQIGTPEEILTNPANDYVADFVED 266
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-226 |
6.44e-43 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 146.45 E-value: 6.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRR 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPA---ELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASL-FDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsDAMEALETVGLEDKLEQhagSLSGGEAQRVA 159
Cdd:PRK13548 78 RAVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVA----------AALAQVDLAHLAGRDYP---QLSGGEQQRVQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 160 FARALA------YDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVaVILGDG 226
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLHDLNLAARYADRI-VLLHQG 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-231 |
7.48e-43 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 152.60 E-value: 7.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDE-TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRRIGMVF 85
Cdd:COG4988 341 DVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 QEASLFDASVRRNaeyglhvrrswadrlrrevadlvgLRNGTSDA-----MEALETVGLED-----------KLEQHAGS 149
Cdd:COG4988 418 QNPYLFAGTIREN------------------------LRLGRPDAsdeelEAALEAAGLDEfvaalpdgldtPLGEGGRG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 150 LSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGdRGIGVAIATHDMNQARRiADQVAVILGDGIIE 229
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVE 551
|
..
gi 909710455 230 VG 231
Cdd:COG4988 552 QG 553
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-240 |
1.10e-42 |
|
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: 147.51 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLR-LLALFEPPR--DGSLEYGGTDVWRASAQRRLECR-RRIGMVFQE--ASL- 90
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPGitSGEILFDGEDLLKLSEKELRKIRgREIQMIFQDpmTSLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 --------FDASVRrnaeygLHVRRSWADRLRRevadlvglrngtsdAMEALETVGL---EDKLEQHAGSLSGGEAQRVA 159
Cdd:COG0444 101 pvmtvgdqIAEPLR------IHGGLSKAEARER--------------AIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFE 238
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDlQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
..
gi 909710455 239 DP 240
Cdd:COG0444 241 NP 242
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-228 |
1.23e-42 |
|
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: 143.94 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGtdVWRASAQRRlecrRRIGMVF 85
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG--KPIKAKERR----KSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 QEAS--LFDASVRRNAEYGLhvrrswadrlrREVADlvglrnGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARA 163
Cdd:cd03226 78 QDVDyqLFTDSVREELLLGL-----------KELDA------GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 164 LAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDGII 228
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV-LLLANGAI 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-241 |
1.58e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 147.92 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRR 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR-----DRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLF-DASVRRNAEYGLHVRRswadrlRREVADLVGLRngtSDAMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:PRK10851 76 VGFVFQHYALFrHMTVFDNIAFGLTVLP------RRERPNAAAIK---AKVTQLLEMVQLAHLADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGD--RGIGVAIaTHDMNQARRIADQVaVILGDGIIE-VGETDRI 236
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFV-THDQEEAMEVADRV-VVMSQGNIEqAGTPDQV 224
|
....*
gi 909710455 237 FEDPE 241
Cdd:PRK10851 225 WREPA 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-253 |
4.44e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 144.21 E-value: 4.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLR----LLALFEPPR-DGSLEYGGTDVWRASAQRrLEC 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARvEGEVRLFGRNIYSPDVDP-IEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 RRRIGMVFQEASLF-DASVRRNAEYGLHVRRswadrlrrevadLVGLRNGTSDAME-ALETVGL----EDKLEQHAGSLS 151
Cdd:PRK14267 84 RREVGMVFQYPNPFpHLTIYDNVAIGVKLNG------------LVKSKKELDERVEwALKKAALwdevKDRLNDYPSNLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 152 GGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgIGVAIATHDMNQARRIADQVAVILGDGIIEVG 231
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
250 260
....*....|....*....|..
gi 909710455 232 ETDRIFEDPEDDRTQQFIDGEL 253
Cdd:PRK14267 231 PTRKVFENPEHELTEKYVTGAL 252
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-178 |
1.01e-41 |
|
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: 139.71 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRRIGMVFQEASLF-DASVR 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQLFpRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLHVRrswadRLRREVADlvglrngtSDAMEALETVGLEDKLEQHAG----SLSGGEAQRVAFARALAYDPDFLL 172
Cdd:pfam00005 78 ENLRLGLLLK-----GLSKREKD--------ARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 909710455 173 LDEPTS 178
Cdd:pfam00005 145 LDEPTA 150
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-222 |
1.11e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 142.95 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRRiG 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL--ARRR-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASL-FDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVALGRAPHGSSAAQDRQIVR-------------EALALVGLAHLAGRSYQTLSGGEQQRVQLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 162 RALA--YDPD-----FLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:COG4559 146 RVLAqlWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLL 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-229 |
5.28e-41 |
|
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: 140.12 E-value: 5.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 27 PGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdVWRASAQRRL--ECRRRIGMVFQEASLF-DASVRRNAEYGL 103
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKINlpPQQRKIGLVFQQYALFpHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 104 HVRRSWADRLRREvadlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPR 183
Cdd:cd03297 101 KRKRNREDRISVD---------------ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 909710455 184 NTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVIlGDGIIE 229
Cdd:cd03297 166 LRLQLLPELKQiKKNLNIPVIFVTHDLSEAEYLADRIVVM-EDGRLQ 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-237 |
7.03e-41 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 140.92 E-value: 7.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAqRRLEcrRR 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-RQLA--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQE-ASLFDASVRRNAEYGlhvrRS-----WAdRLRREVADLVglrngtSDAMEALETVGLEDKLeqhAGSLSGGE 154
Cdd:PRK11231 78 LALLPQHhLTPEGITVRELVAYG----RSpwlslWG-RLSAEDNARV------NQAMEQTRINHLADRR---LTDLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 155 AQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETD 234
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
...
gi 909710455 235 RIF 237
Cdd:PRK11231 224 EVM 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-251 |
2.45e-40 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 139.90 E-value: 2.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQ 86
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLF-DASVRRNAEYGLHVRRSWADRLRRevadlvglrngtSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:PRK11831 92 SGALFtDMNVFDNVAYPLREHTQLPAPLLH------------STVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPeDDR 244
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPR 238
|
....*..
gi 909710455 245 TQQFIDG 251
Cdd:PRK11831 239 VRQFLDG 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-229 |
3.36e-40 |
|
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: 137.77 E-value: 3.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRRIG 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVPKDEIDERVR-------------EVAELLQIEHLLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 162 RALAYDPDFLLLDEPTSDLDprntAVIENAVREAGDR-----GIGVAIATHDMNQARRIADQVAViLGDGIIE 229
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLD----AKLRVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADRIAV-MNDGQIQ 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-253 |
7.00e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 138.64 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLL----RLLALFEPP--RDGSLEYGGTDVWRASAqrrLECRRRIGMVFQE 87
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnRLIEIYDSKikVDGKVLYFGKDIFQIDA---IKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 ASLF-DASVRRNAEYGLhvrRSWADRLRREVADLVglrngtsdaMEALETVGL----EDKLEQHAGSLSGGEAQRVAFAR 162
Cdd:PRK14246 99 PNPFpHLSIYDNIAYPL---KSHGIKEKREIKKIV---------EECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPED 242
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
250
....*....|.
gi 909710455 243 DRTQQFIDGEL 253
Cdd:PRK14246 246 ELTEKYVIGRI 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-251 |
1.06e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 138.69 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPP-----RDGSLEYGGTDVWraSAQRRLEC 77
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIF--NYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 RRRIGMVFQEASLFDASVRRNAEYGLHVRRSWADRLRREVADLVGLRNGTSDAmealetvgLEDKLEQHAGSLSGGEAQR 157
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDA--------VKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIF 237
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
250
....*....|....
gi 909710455 238 EDPEDDRTQQFIDG 251
Cdd:PRK14271 251 SSPKHAETARYVAG 264
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-208 |
3.09e-39 |
|
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: 135.61 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQEASLF- 91
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFRLLp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DASVRRNAEYGLHVrrswADRLRREVADLVglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:cd03292 92 DRNVYENVAFALEV----TGVPPREIRKRV---------PAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHD 208
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-249 |
3.45e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 136.71 E-value: 3.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALF-----EPPRDGSLEYGGTDVWrasaQRRL---ECRRRIGM 83
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIY----ERRVnlnRLRRQVSM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 84 VFQEASLFDASVRRNAEYGLHVRrSWADRLrrEVADLVglrngtSDAMEALETVG-LEDKLEQHAGSLSGGEAQRVAFAR 162
Cdd:PRK14258 93 VHPKPNLFPMSVYDNVAYGVKIV-GWRPKL--EIDDIV------ESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRG-IGVAIATHDMNQARRIADQVAVILGD-----GIIEVGETDRI 236
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGNenrigQLVEFGLTKKI 243
|
250
....*....|...
gi 909710455 237 FEDPEDDRTQQFI 249
Cdd:PRK14258 244 FNSPHDSRTREYV 256
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-250 |
1.14e-38 |
|
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: 134.74 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLL-ALFEPPrDGSLEYGGTDVwraSAQRRLECRRRIGMVFQEASLF 91
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInRLIEPT-SGEIFIDGEDI---REQDPVELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 -DASVRRNAEYGLHVRRsWADRLRREVADlvglrngtsdamEALETVGLEDK--LEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:cd03295 88 pHMTVEENIALVPKLLK-WPKEKIRERAD------------ELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 169 DFLLLDEPTSDLDP-RNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQ 247
Cdd:cd03295 155 PLLLMDEPFGALDPiTRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
...
gi 909710455 248 FID 250
Cdd:cd03295 235 FVG 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-222 |
2.36e-38 |
|
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: 140.11 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGYGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRR 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLFDASVRRNAeygLHVRRSWADRLRREVADLVGLrngtSDAMEALETvGLEDKLEQHAGSLSGGEAQRVAF 160
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENI---RLARPDASDAEIREALERAGL----DEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGdRGIGVAIATHDMNQARRiADQVAVI 222
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-252 |
2.53e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.39 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRRIGMVFQ 86
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLF-DASVRRNAEYGLHVRRSWADRLRREVadlvglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:PRK09452 94 SYALFpHMTVFENVAFGLRMQKTPAAEITPRV-------------MEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVReAGDR--GIGVAIATHDMNQARRIADQVAViLGDGIIE-VGETDRIFEDPED 242
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELK-ALQRklGITFVFVTHDQEEALTMSDRIVV-MRDGRIEqDGTPREIYEEPKN 238
|
250
....*....|
gi 909710455 243 DRTQQFIdGE 252
Cdd:PRK09452 239 LFVARFI-GE 247
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-240 |
2.68e-38 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.01 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQE--ASLfdasv 95
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDpyASL----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 96 rrNAeyglhvrrswadrlRREVADLVG--LR-NGTSD-------AMEALETVGLEdklEQHAGS----LSGGEAQRVAFA 161
Cdd:COG4608 109 --NP--------------RMTVGDIIAepLRiHGLASkaerrerVAELLELVGLR---PEHADRypheFSGGQRQRIGIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgIGVA---IAtHDMNQARRIADQVAVI-LGdGIIEVGETDRIF 237
Cdd:COG4608 170 RALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDE-LGLTylfIS-HDLSVVRHISDRVAVMyLG-KIVEIAPRDELY 246
|
...
gi 909710455 238 EDP 240
Cdd:COG4608 247 ARP 249
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-240 |
5.86e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 136.00 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECrrrigMVFQEASLF 91
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC-----MVFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 -DASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDF 170
Cdd:PRK11432 91 pHMSLGENVGYGLKMLGVPKEERKQRVK-------------EALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-241 |
7.27e-38 |
|
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: 133.32 E-value: 7.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDET--ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLL-ALFEPPRdGSLEYGGTDVwrASAQRRLECRRRIGM 83
Cdd:TIGR04520 5 NVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnGLLLPTS-GKVTVDGLDT--LDEENLWEIRKKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 84 VFQ--EASLFDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:TIGR04520 82 VFQnpDNQFVGATVEDDVAFGLENLGVPREEMRKRVD-------------EALKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPR-NTAVIENAVREAGDRGIGVAIATHDMNQARRiADQVaVILGDG-IIEVGETDRIFED 239
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKgRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRV-IVMNKGkIVAEGTPREIFSQ 226
|
..
gi 909710455 240 PE 241
Cdd:TIGR04520 227 VE 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-241 |
9.59e-38 |
|
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: 132.28 E-value: 9.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRRIG 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKR--ARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGLHVRRSWADRLRREVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:cd03218 79 YLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEEL-------------LEEFHITHLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQvAVILGDG-IIEVGETDRIFEDP 240
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDR-AYIIYEGkVLAEGTPEEIAANE 224
|
.
gi 909710455 241 E 241
Cdd:cd03218 225 L 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-228 |
3.18e-37 |
|
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: 130.03 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEyggtdVWRASAQRRLECRRRIG 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-----FDGKSYQKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDA-SVRRNAEYGlhvrrswadrlrrevADLVGLRNgtSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLL---------------ARLLGIRK--KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDGII 228
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRI-GIINKGKL 204
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-222 |
5.41e-37 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 132.13 E-value: 5.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAqrrlECRRRIGMVFQEASLF 91
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPR----KVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DA-SVRRNAE-----YGLhvrrSWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:TIGR01188 79 EDlTGRENLEmmgrlYGL----PKDEAEER--------------AEELLELFELGEAADRPVGTYSGGMRRRLDIAASLI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:TIGR01188 141 HQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAII 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-219 |
1.14e-36 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 128.12 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 11 GYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdvwrasaqrrlecrRRIGMVFQEASL 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--------------ARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 ---FDASVRRNAEYGLHVRRSWADRLRREVADLVGlrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:NF040873 67 pdsLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVD---------DALERVGLADLAGRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQV 219
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-231 |
1.36e-36 |
|
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: 129.20 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasaqRRLEC---RRRIGMVFQEASL 90
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI------RDLNLrwlRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 FDASVRRNAEYGlhvRRSWADRLRREVADLVGLRNGTSDAMEALET-VGledkleQHAGSLSGGEAQRVAFARALAYDPD 169
Cdd:cd03249 89 FDGTIAENIRYG---KPDATDEEVEEAAKKANIHDFIMSLPDGYDTlVG------ERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 170 FLLLDEPTSDLDPRNTAVIENAVREA-GDRGIgVAIAtHDMNQARRiADQVAVILGDGIIEVG 231
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAmKGRTT-IVIA-HRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-234 |
4.21e-36 |
|
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: 127.49 E-value: 4.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAqrrlECRRRIGMVFQEASLF 91
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR----EVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DA-SVRRNAE-----YGLhvrrSWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:cd03265 86 DElTGWENLYiharlYGV----PGAERRER--------------IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETD 234
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-212 |
6.02e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 126.83 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPR---DGSLEYGGTDVWRASAQRRlecrrRIGMVFQEA 88
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR-----RIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 89 SLFD-ASVRRNAEYGLhvRRSWADRLRREVAdlvglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:COG4136 86 LLFPhLSVGENLAFAL--PPTIGRAQRRARV------------EQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQA 212
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEEDA 197
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-226 |
9.88e-36 |
|
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: 130.23 E-value: 9.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 9 EHGYGDETIleNVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdVWRASAQRRLEC--RRRIGMVFQ 86
Cdd:TIGR02142 6 SKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-TLFDSRKGIFLPpeKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLF-DASVRRNAEYGLhvRRSWADrlrrevadlvgLRNGTSDAMeaLETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:TIGR02142 83 EARLFpHLSVRGNLRYGM--KRARPS-----------ERRISFERV--IELLGIGHLLGRLPGRLSGGEKQRVAIGRALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 166 YDPDFLLLDEPTSDLD-PRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDG 226
Cdd:TIGR02142 148 SSPRLLLMDEPLAALDdPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRV-VVLEDG 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
12-253 |
1.06e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.78 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDV---------WRASAQRRLEC-RRRI 81
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqLKVADKNQLRLlRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQEASLFD-ASVRRNA-EYGLHVrrswadrlrrevadlVGLRNGTSD--AMEALETVGLEDKLEQ-HAGSLSGGEAQ 156
Cdd:PRK10619 95 TMVFQHFNLWShMTVLENVmEAPIQV---------------LGLSKQEARerAVKYLAKVGIDERAQGkYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 157 RVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDGII-EVGETDR 235
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHV-IFLHQGKIeEEGAPEQ 238
|
250
....*....|....*...
gi 909710455 236 IFEDPEDDRTQQFIDGEL 253
Cdd:PRK10619 239 LFGNPQSPRLQQFLKGSL 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-222 |
1.09e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.49 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLECRrrigMVFQ 86
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL----AEAREDTR----LMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFD-ASVRRNAeyGLHVRRSWADRlrrevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:PRK11247 89 DARLLPwKKVIDNV--GLGLKGQWRDA-----------------ALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 166 YDPDFLLLDEPTSDLDPRN----TAVIENAVREagdRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTriemQDLIESLWQQ---HGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-241 |
1.15e-35 |
|
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: 127.01 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRRI 81
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHER--ARLGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQEASLF-DASVRRNAEYGLHVRRSWADRLRREVADlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAF 160
Cdd:TIGR04406 79 GYLPQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLE------------ALLEEFQISHLRDNKAMSLSGGERRRVEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQvAVILGDG-IIEVGETDRIFED 239
Cdd:TIGR04406 147 ARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDR-AYIISDGkVLAEGTPAEIVAN 225
|
..
gi 909710455 240 PE 241
Cdd:TIGR04406 226 EK 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-226 |
1.26e-35 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 126.47 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDE--TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLECRRR 80
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLFDA-SVRRNAEYglhvrrsWAdRLRrevadlvGLRNGTSDA-MEA-LETVGLEDKLEQHAGSLSGGEAQR 157
Cdd:cd03263 77 LGYCPQFDALFDElTVREHLRF-------YA-RLK-------GLPKSEIKEeVELlLRVLGLTDKANKRARTLSGGMKRK 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGdRGIGVAIATHDMNQARRIADQVAvILGDG 226
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIA-IMSDG 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-229 |
2.36e-35 |
|
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: 126.01 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWR----ASAQRRlecRRRIGMVFQEASLF 91
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARARLR---ARHVGFVFQSFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DA-SVRRNaeyglhvrrswadrlrreVA---DLVGLRNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:COG4181 103 PTlTALEN------------------VMlplELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIadQVAVILGDGIIE 229
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFElNRERGTTLVLVTHDPALAARC--DRVLRLRAGRLV 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
3.76e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 126.73 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTL-LRLLALFEPpRDGSLEYGGTDVwRASAQRRLECRRR 80
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILKP-TSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQ--EASLFDASVRRNAEYG-LHVRRSwadrlRREVADLVglrngtsdaMEALETVGLEDKLEQHAGSLSGGEAQR 157
Cdd:PRK13639 80 VGIVFQnpDDQLFAPTVEEDVAFGpLNLGLS-----KEEVEKRV---------KEALKAVGMEGFENKPPHHLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIF 237
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
....
gi 909710455 238 EDPE 241
Cdd:PRK13639 226 SDIE 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-222 |
5.26e-35 |
|
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: 124.79 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLECRRRIGMVFQEASLFD-ASVR 96
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEARRRLGFVSDSTGLYDrLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYglhvrrswadrlrreVADLVGL-RNGTSDAMEAL-ETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLD 174
Cdd:cd03266 97 ENLEY---------------FAGLYGLkGDELTARLEELaDRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 909710455 175 EPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-208 |
6.14e-35 |
|
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: 130.94 E-value: 6.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGY-GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRR 80
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD---EVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLFDASVRRNAEYGlhvrrswadrlRREVADlvglrngtSDAMEALETVGLEDKLE-----------QHAGS 149
Cdd:TIGR02868 411 VSVCAQDAHLFDTTVRENLRLA-----------RPDATD--------EELWAALERVGLADWLRalpdgldtvlgEGGAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 150 LSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVReAGDRGIGVAIATHD 208
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL-AALSGRTVVLITHH 529
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-241 |
8.96e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 124.76 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRR 80
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKR--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLF-DASVRRNAEYGLHVRRSWADRLRREVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:COG1137 80 IGYLPQEASIFrKLTVEDNILAVLELRKLSKKEREERLEEL-------------LEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQvAVILGDG-IIEVGETDRIFE 238
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDR-AYIISEGkVLAEGTPEEILN 225
|
...
gi 909710455 239 DPE 241
Cdd:COG1137 226 NPL 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-231 |
1.84e-34 |
|
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: 123.88 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDE-TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwRASAQRRLecRRRIGMVFQ 86
Cdd:cd03253 6 VTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-REVTLDSL--RRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDASVRRNAEYGlhvRRSWADRLRREVADLvglrngtsdAMEALETVGLEDKLEQHAGS----LSGGEAQRVAFAR 162
Cdd:cd03253 83 DTVLFNDTIGYNIRYG---RPDATDEEVIEAAKA---------AQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIAtHDMnqaRRI--ADQVAVILGDGIIEVG 231
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRL---STIvnADKIIVLKDGRIVERG 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-222 |
2.04e-34 |
|
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: 121.55 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRIG 82
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI---SQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDASVRRNAeyglhvrrswadrlrrevadlvglrngtsdamealetvgledkleqhagsLSGGEAQRVAFAR 162
Cdd:cd03246 80 YLPQDDELFSGSIAENI--------------------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRiADQVAVI 222
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVL 168
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-231 |
2.14e-34 |
|
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: 123.49 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRI 81
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLA---SLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQEASLFDASVRRNAEYGLHvrrswaDRLRREVADLVGLRNGTSDAMEALEtvGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPE--GYDTVIGERGVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIAtHDMNQARRiADQVAVILGDGIIEVG 231
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA-HRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-252 |
2.96e-34 |
|
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: 129.03 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 5 TVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKT----TLLRLLAlfEPPR--DGSLEYGGTDVWRASAQRRLECR 78
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLP--DPAAhpSGSILFDGQDLLGLSERELRRIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 79 -RRIGMVFQE--ASLfdasvrrN---------AE-YGLHVRRSWADRLRRevadlvglrngtsdAMEALETVGLEDKlEQ 145
Cdd:COG4172 91 gNRIAMIFQEpmTSL-------NplhtigkqiAEvLRLHRGLSGAAARAR--------------ALELLERVGIPDP-ER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 146 HAGS----LSGGEAQRVAFARALAYDPDFLLLDEPTSDLDprntaV---------IENAVREagdRGIGVAIATHDMNQA 212
Cdd:COG4172 149 RLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALD-----VtvqaqildlLKDLQRE---LGMALLLITHDLGVV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 909710455 213 RRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQFIDGE 252
Cdd:COG4172 221 RRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLLAAE 260
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-222 |
3.00e-34 |
|
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: 122.39 E-value: 3.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGtdvwrasAQRRLECRRRIG 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------KPLDIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYglhvrrswadrlrreVADLVGL--RNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVY---------------LAQLKGLkkEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-249 |
3.16e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 126.49 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlecRRRIGMVFQEASLF-DASVR 96
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY-----QRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLHvrrswADRL-RREVADLVGlrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDE 175
Cdd:PRK11607 110 QNIAFGLK-----QDKLpKAEIASRVN---------EMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 176 PTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQFI 249
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-212 |
3.77e-34 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 121.76 E-value: 3.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwRASAQRRLECRRRIGMVFQEA--SL 90
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERRQRVGLVFQDPddQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 FDASVRRNAEYGLHVRRSWADRLRREVadlvglrngtSDAMEALETVGLEDKLEQHagsLSGGEAQRVAFARALAYDPDF 170
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRV----------REALTAVGASGLRERPTHC---LSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQA 212
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-249 |
4.94e-34 |
|
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: 128.26 E-value: 4.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTL----LRLLalfepPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQE--ASLf 91
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpfGSL- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 daSVRRN-----AEyGLHVRR---SWADRLRRevadlvglrngtsdAMEALETVGL-EDKLEQHAGSLSGGEAQRVAFAR 162
Cdd:COG4172 376 --SPRMTvgqiiAE-GLRVHGpglSAAERRAR--------------VAEALEEVGLdPAARHRYPHEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAViLGDG-IIEVGETDRIFEDP 240
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDlQREHGLAYLFISHDLAVVRALAHRVMV-MKDGkVVEQGPTEQVFDAP 517
|
....*....
gi 909710455 241 EDDRTQQFI 249
Cdd:COG4172 518 QHPYTRALL 526
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-228 |
6.29e-34 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 121.93 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETI--LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIGMV 84
Cdd:cd03245 7 NVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPA---DLRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 85 FQEASLFDASVRRNAEYGlhvRRSWADRLRREVADLVGLrngtsDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARAL 164
Cdd:cd03245 84 PQDVTLFYGTLRDNITLG---APLADDERILRAAELAGV-----TDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 165 AYDPDFLLLDEPTSDLDPRNTA-VIENAVREAGDRGIgvAIATHDMNqARRIADQVAVILGDGII 228
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEErLKERLRQLLGDKTL--IIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-231 |
8.02e-34 |
|
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: 121.53 E-value: 8.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGeVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRasaqRRLECRRRIG 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDA-SVRRNAEYglhvrrswadrlrreVADLVGLRNGTSDAM--EALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDY---------------IAWLKGIPSKEVKARvdEVLELVNLGDRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIgVAIATHDMNQARRIADQVAVILGDGIIEVG 231
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-238 |
1.21e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.82 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGG-----TDVWrasaqrrlECRRRIGMVFQ--EASL 90
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVW--------DVRRQVGMVFQnpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 FDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDF 170
Cdd:PRK13635 95 VGATVQDDVAFGLENIGVPREEMVERVD-------------QALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAVREAGD-RGIGVAIATHDMNQARRiADQVAVILGDGIIEVGETDRIFE 238
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-242 |
3.65e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 121.67 E-value: 3.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDETILE-----NVSLAVPPGEVVAIIGPSGVGKTTLLRLL-ALFEPPRdGSLEYGGTDVWRASAQRRLE-CRRR 80
Cdd:PRK13634 8 VEHRYQYKTPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLnGLLQPTS-GTVTIGERVITAGKKNKKLKpLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQ--EASLFDASVRRNAEYG---LHVRRSWADRLRREVADLVGLRngtsdamealetvglEDKLEQHAGSLSGGEA 155
Cdd:PRK13634 87 VGIVFQfpEHQLFEETVEKDICFGpmnFGVSEEDAKQKAREMIELVGLP---------------EELLARSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVI----ENAVREagdRGIGVAIATHDMNQARRIADQVAVILGDGIIEVG 231
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmemfYKLHKE---KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
250
....*....|.
gi 909710455 232 ETDRIFEDPED 242
Cdd:PRK13634 229 TPREIFADPDE 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-238 |
3.98e-33 |
|
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: 120.02 E-value: 3.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGY-GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRIGMVFQ 86
Cdd:cd03254 8 VNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDASVRRNAEYGlhvRRSWADRLRREVADLVGLrngtSDAMEALETvGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:cd03254 85 DTFLFSGTIMENIRLG---RPNATDEEVIEAAKEAGA----HDFIMKLPN-GYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIAtHDMNQARRiADQVAVILGDGIIEVGETDRIFE 238
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-222 |
8.64e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.98 E-value: 8.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasaqrRLECRRRIGMVFQEASLF 91
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-------DPEDRRRIGYLPEERGLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 -DASVRRNAEYglhvrrswadrlrreVADLVGLrnGTSDAMEA----LETVGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:COG4152 84 pKMKVGEQLVY---------------LARLKGL--SKAEAKRRadewLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVII 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-228 |
8.71e-33 |
|
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: 118.75 E-value: 8.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 22 SLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecrrRIGMVFQEASLF-DASVRRNAE 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-----PVSMLFQENNLFaHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 101 YGLhvrrswADRLRrevadlvgLRNGTSDAME-ALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSD 179
Cdd:cd03298 93 LGL------SPGLK--------LTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 909710455 180 LDP--RN--TAVIENAVREagdRGIGVAIATHDMNQARRIADQVaVILGDGII 228
Cdd:cd03298 159 LDPalRAemLDLVLDLHAE---TKMTVLMVTHQPEDAKRLAQRV-VFLDNGRI 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-226 |
9.24e-33 |
|
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: 117.14 E-value: 9.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecRRRIG 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR--RAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQeaslfdasvrrnaeyglhvrrswadrlrrevadlvglrngtsdamealetvgledkleqhagsLSGGEAQRVAFAR 162
Cdd:cd03216 79 MVYQ---------------------------------------------------------------LSVGERQMVEIAR 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDG 226
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRV-TVLRDG 158
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-239 |
2.09e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 120.19 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEY-----------------GGTDVWRASAQRRL----E 76
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekvLEKLVIQKTRFKKIkkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 77 CRRRIGMVFQ--EASLFDASVRRNAEYG---LHVRRSWADRLRREVADLVGLRngtsdamealetvglEDKLEQHAGSLS 151
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsMGVSKEEAKKRAAKYIELVGLD---------------ESYLQRSPFELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 152 GGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVG 231
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
....*...
gi 909710455 232 ETDRIFED 239
Cdd:PRK13651 248 DTYDILSD 255
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-246 |
4.10e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.07 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQE--ASLfdaSV 95
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSL---NP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 96 RRNAEYGL------HVRRSWADRLRRevadlvglrngtsdAMEALETVGLEdklEQHAGS----LSGGEAQRVAFARALA 165
Cdd:PRK11308 108 RKKVGQILeeplliNTSLSAAERREK--------------ALAMMAKVGLR---PEHYDRyphmFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDR 244
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
|
..
gi 909710455 245 TQ 246
Cdd:PRK11308 251 TQ 252
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-236 |
4.58e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 117.38 E-value: 4.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 22 SLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecrrRIGMVFQEASLFD-ASVRRNAE 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR-----PVSMLFQENNLFShLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 101 YGLHVRRSWADRLRREVADLVglrngtsdamealETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDL 180
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIA-------------RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 181 DPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRI 236
Cdd:PRK10771 161 DPALRQEMLTLVSQvCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-235 |
4.86e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.43 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecRRRIG 82
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ--AAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAEYGLHVRR----SWAdRLRREvadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQR 157
Cdd:COG1129 83 IIHQELNLVpNLSVAENIFLGREPRRggliDWR-AMRRR-------------ARELLARLGLDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAViLGDGII----EVGET 233
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTV-LRDGRLvgtgPVAEL 227
|
..
gi 909710455 234 DR 235
Cdd:COG1129 228 TE 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-238 |
7.38e-32 |
|
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: 122.55 E-value: 7.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRRIGMVFQEASLFD 92
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRHIGYLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRN-AEYGLhvrrswADrlRREV---ADLVG-------LRNGtsdameaLETVgledkLEQHAGSLSGGEAQRVAFA 161
Cdd:COG4618 420 GTIAENiARFGD------AD--PEKVvaaAKLAGvhemilrLPDG-------YDTR-----IGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNqARRIADQVAViLGDGIIE-VGETDRIFE 238
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLV-LRDGRVQaFGPRDEVLA 555
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-255 |
8.07e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.78 E-value: 8.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRIGMVFQ--EASLFDAS 94
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQnpDNQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 VRRNAEYGLHVRRSWADRLRREVADLVglrngtsdamealETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLD 174
Cdd:PRK13632 101 VEDDIAFGLENKKVPPKKMKDIIDDLA-------------KKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 175 EPTSDLDPRNTAVIENAVREAGDRGIGVAIA-THDMNQArRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQfIDGEL 253
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNNKEILEKAK-IDSPF 245
|
..
gi 909710455 254 IY 255
Cdd:PRK13632 246 IY 247
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-181 |
9.49e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 117.27 E-value: 9.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 11 GYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRrlecrrriGMVFQEASL 90
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--------GVVFQKDAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 FD-ASVRRNAEYGLHVRR-SWADRLRRevadlvglrngtsdAMEALETVGLEDkLEQHA-GSLSGGEAQRVAFARALAYD 167
Cdd:COG4525 88 LPwLNVLDNVAFGLRLRGvPKAERRAR--------------AEELLALVGLAD-FARRRiWQLSGGMRQRVGIARALAAD 152
|
170
....*....|....
gi 909710455 168 PDFLLLDEPTSDLD 181
Cdd:COG4525 153 PRFLLMDEPFGALD 166
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-251 |
1.19e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 120.14 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDETILE---------NVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECR 78
Cdd:PRK10070 25 IEQGLSKEQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 79 RR-IGMVFQEASLF-DASVRRNAEYGLHVRRSWADRlRREvadlvglrngtsDAMEALETVGLEDKLEQHAGSLSGGEAQ 156
Cdd:PRK10070 105 RKkIAMVFQSFALMpHMTVLDNTAFGMELAGINAEE-RRE------------KALDALRQVGLENYAHSYPDELSGGMRQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 157 RVAFARALAYDPDFLLLDEPTSDLDPR-NTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDR 235
Cdd:PRK10070 172 RVGLARALAINPDILLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
250
....*....|....*.
gi 909710455 236 IFEDPEDDRTQQFIDG 251
Cdd:PRK10070 252 ILNNPANDYVRTFFRG 267
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-219 |
1.50e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.07 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECR-RRIGMVFQEASLF-DAS 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQFHHLLpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 VRRNAEYGL---HVRRSWAdrlrrevadlvglrngTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:PRK11629 104 ALENVAMPLligKKKPAEI----------------NSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQV 219
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-207 |
1.96e-31 |
|
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: 116.34 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSL------EYGGTDVWrasaqrrlECRRRIGMV- 84
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDVW--------ELRKRIGLVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 85 --FQEASLFDASVR------RNAEYGLHVRRSWADRLRrevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQ 156
Cdd:COG1119 85 paLQLRFPRDETVLdvvlsgFFDSIGLYREPTDEQRER---------------ARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 909710455 157 RVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATH 207
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTH 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-231 |
7.32e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 118.02 E-value: 7.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRR 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR---AASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASL-FDASVRRNAEYGLHVRRS----WADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEA 155
Cdd:PRK09536 79 VASVPQDTSLsFEFDVRQVVEMGRTPHRSrfdtWTETDRAAVE-------------RAMERTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVG 231
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-240 |
2.47e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.01 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 4 QTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGM 83
Cdd:PRK10419 14 AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 84 VFQEA-SLFDA--SVRRN-AEYGLHVRR-SWADRLRRevadlvglrngtsdAMEALETVGLEDK-LEQHAGSLSGGEAQR 157
Cdd:PRK10419 94 VFQDSiSAVNPrkTVREIiREPLRHLLSlDKAERLAR--------------ASEMLRAVDLDDSvLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDPR-NTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIE---VGET 233
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVlQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDK 239
|
....*..
gi 909710455 234 DRiFEDP 240
Cdd:PRK10419 240 LT-FSSP 245
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-246 |
4.21e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.10 E-value: 4.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTD-VWR-----ASAQRRLE 76
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRdlyalSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 77 CRRRIGMVFQEAslfdasvrrnaeyglhvrrswADRLRREVAD---------LVGLRN-GT--SDAMEALETVGLE-DKL 143
Cdd:PRK11701 87 LRTEWGFVHQHP---------------------RDGLRMQVSAggnigerlmAVGARHyGDirATAGDWLERVEIDaARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 144 EQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLD----PRNTAVIENAVREAgdrGIGVAIATHDMNQARRIADQV 219
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVREL---GLAVVIVTHDLAVARLLAHRL 222
|
250 260
....*....|....*....|....*..
gi 909710455 220 AVILGDGIIEVGETDRIFEDPEDDRTQ 246
Cdd:PRK11701 223 LVMKQGRVVESGLTDQVLDDPQHPYTQ 249
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-236 |
4.73e-30 |
|
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: 112.19 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIGMVFQEASLFDASVR 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA---WLRRQVGVVLQENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RN---AEYGLHVRRSwadrlrREVADLVGLRNGTSDAMEALET-VGledklEQHAGsLSGGEAQRVAFARALAYDPDFLL 172
Cdd:cd03252 94 DNialADPGMSMERV------IEAAKLAGAHDFISELPEGYDTiVG-----EQGAG-LSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 173 LDEPTSDLDPRNTAVIENAVREAGDrGIGVAIATHDMNQARRiADQVAVILGDGIIEVGETDRI 236
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-212 |
8.04e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 8.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 11 GYGDE-TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecrRRIGMVFQEAS 89
Cdd:COG1101 14 GTVNEkRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA---KYIGRVFQDPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 L---FDASV--------RRNAEYGLH--VRRSWADRLRREVADLvGLrngtsdamealetvGLEDKLEQHAGSLSGGEAQ 156
Cdd:COG1101 91 MgtaPSMTIeenlalayRRGKRRGLRrgLTKKRRELFRELLATL-GL--------------GLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 157 RVAFARALAYDPDFLLLDEPTSDLDPRNTAVI----ENAVREagdRGIGVAIATHDMNQA 212
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEE---NNLTTLMVTHNMEQA 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-222 |
8.79e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.36 E-value: 8.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLECRRRIG 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNAE-YGLHVRRSwADRLRREVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGGEAQRVAF 160
Cdd:PRK13537 84 VVPQFDNLDpDFTVRENLLvFGRYFGLS-AAAARALVPPL-------------LEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-229 |
9.59e-30 |
|
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: 112.21 E-value: 9.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRI 81
Cdd:TIGR02769 11 TYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQEA-SLFDAsvRRNAEYGL-----HVRR-SWADRLRR--EVADLVGLRngtSDAMealetvgleDKLEQHagsLSG 152
Cdd:TIGR02769 91 QLVFQDSpSAVNP--RMTVRQIIgeplrHLTSlDESEQKARiaELLDMVGLR---SEDA---------DKLPRQ---LSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 153 GEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIE 229
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-209 |
1.39e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 110.73 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQEASLF- 91
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVS-------------AALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDM 209
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-219 |
2.72e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecRRR 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY---RQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLFDASVRRNAEYGLHVRRSWADRlRREVADLVglRNGTSDAMealetvgledkLEQHAGSLSGGEAQRVAF 160
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDP-AIFLDDLE--RFALPDTI-----------LTKNIAELSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRN-TAVIENAVREAGDRGIGVAIATHDMNQARRiADQV 219
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNkHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-240 |
4.43e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.20 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasaqRRLEC---RRRIGMVFQEASL 90
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL------VQYDHhylHRQVALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 FDASVRRNAEYGLhvrRSWADRLRREVADLVGLRNGTSDAMEALETVGLEdkleqHAGSLSGGEAQRVAFARALAYDPDF 170
Cdd:TIGR00958 567 FSGSVRENIAYGL---TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE-----KGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAvREAGDRgiGVAIATHDMNQARRiADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQES-RSRASR--TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-221 |
5.45e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 109.82 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRRIGMVFQEASLFDA-SVR 96
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEI--ARLGIGRKFQKPTVFEElTVF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLHVRRSWAD----RLRREVADLVGlrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:COG4674 104 ENLELALKGDRGVFAslfaRLTAEERDRIE---------EVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 909710455 173 LDEPT---SDLDPRNTAVIENAVreAGDRGIgVAIaTHDMNQARRIADQVAV 221
Cdd:COG4674 175 LDEPVagmTDAETERTAELLKSL--AGKHSV-VVV-EHDMEFVRQIARKVTV 222
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
8-196 |
7.58e-29 |
|
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: 114.15 E-value: 7.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGY-GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwRASAQRRLecRRRIGMVFQ 86
Cdd:COG5265 363 VSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQASL--RAAIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDASVRRNAEYGlhvrRSWADRLR-REVADLVGLRNGTSDAMEALETV----GLEdkleqhagsLSGGEAQRVAFA 161
Cdd:COG5265 440 DTVLFNDTIAYNIAYG----RPDASEEEvEAAARAAQIHDFIESLPDGYDTRvgerGLK---------LSGGEKQRVAIA 506
|
170 180 190
....*....|....*....|....*....|....*
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAG 196
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVA 541
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-181 |
9.05e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.40 E-value: 9.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRrlecrrriG 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQ-EASLFDASVRRNAEYGLHVRRswADRLRREVAdlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQLAG--VEKMQRLEI-----------AHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIA 140
|
170 180
....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLD 181
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALD 160
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-236 |
1.43e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 108.63 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIGMVFQ 86
Cdd:COG4604 6 NVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSR---ELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLfdasvrrnaeyglhvrrswADRLRreVADLVGL--------RNGTSDAM---EALETVGLEDKLEQHAGSLSGGEA 155
Cdd:COG4604 83 ENHI-------------------NSRLT--VRELVAFgrfpyskgRLTAEDREiidEAIAYLDLEDLADRYLDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGD-RGIGVAIATHDMNQARRIADQVaVILGDG-IIEVGET 233
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDINFASCYADHI-VAMKDGrVVAQGTP 220
|
...
gi 909710455 234 DRI 236
Cdd:COG4604 221 EEI 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-228 |
2.57e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 108.54 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 11 GYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIGMVFQEASL 90
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK---EVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 -FDASVRRNAEYGLHVRRSWADRLRREVADLVGlrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPD 169
Cdd:PRK10253 93 pGDITVQELVARGRYPHQPLFTRWRKEDEEAVT---------KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 170 FLLLDEPTSDLDPRNTAVIENAVREAG-DRGIGVAIATHDMNQARRIADQVaVILGDGII 228
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHL-IALREGKI 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-222 |
2.84e-28 |
|
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: 107.17 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRIGMVFQEASLFDA 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRNAEYGLhvrRSWADRLRREVADlvglRNGTSDAMEALETvGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLL 173
Cdd:cd03248 103 SLQDNIAYGL---QSCSFECVKEAAQ----KAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 909710455 174 DEPTSDLDPRNTAVIENAVREaGDRGIGVAIATHDMNQARRiADQVAVI 222
Cdd:cd03248 175 DEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVL 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-244 |
2.93e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRRI 81
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAR--ARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQEASLFDA-SVRRNAEYGLHVRRSWADRLRREVADlvglrngtsDAMEALETVGLEDKLEQhagSLSGGEAQRVAF 160
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMAVLQIRDDLSAEQREDRAN---------ELMEEFHIEHLRDSMGQ---SLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
....
gi 909710455 241 EDDR 244
Cdd:PRK10895 229 HVKR 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-229 |
4.64e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYgGTDVwrasaqrrlecrrRIG 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFD--ASVRrnaeygLHVRRSWADRLRREVADLVG--LRNGtsdamealetvgleDKLEQHAGSLSGGEAQRV 158
Cdd:COG0488 382 YFDQHQEELDpdKTVL------DELRDGAPGGTEQEVRGYLGrfLFSG--------------DDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGdrgiGVAIATHDMNQARRIADQVAVILGDGIIE 229
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfPG----TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
14-237 |
4.82e-28 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 112.10 E-value: 4.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIGMVFQEASLFDA 93
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPA---ELRARMALVPQDPVLFAA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRNAEYGLhvrrswADRLRREVADlvglrngTSDAMEALETV-----GLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:TIGR02204 429 SVMENIRYGR------PDATDEEVEA-------AARAAHAHEFIsalpeGYDTYLGERGVTLSGGQRQRIAIARAILKDA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIAtHDMNQARRiADQVAVILGDGIIEVGETDRIF 237
Cdd:TIGR02204 496 PILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA-HRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-181 |
9.43e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.54 E-value: 9.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGsleyggtDVWRASaqrrlecRRRIGMVFQ 86
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVSIPK-------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFD-ASVRRNAEYGLHVRRSWADRLRR-------------EVADL------VGLRNGTSDAMEALETVGL-EDKLEQ 145
Cdd:COG0488 69 EPPLDDdLTVLDTVLDGDAELRALEAELEEleaklaepdedleRLAELqeefeaLGGWEAEARAEEILSGLGFpEEDLDR 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 909710455 146 HAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLD 181
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-241 |
9.57e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.14 E-value: 9.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETI-LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRIGMVFQ--EAS 89
Cdd:PRK13648 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKHIGIVFQnpDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 LFDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPD 169
Cdd:PRK13648 96 FVGSIVKYDVAFGLENHAVPYDEMHRRVS-------------EALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 170 FLLLDEPTSDLDPRNTAVIENAVREA-GDRGIGVAIATHDMNQARRiADQVaVILGDG-IIEVGETDRIFEDPE 241
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHV-IVMNKGtVYKEGTPTEIFDHAE 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-241 |
9.58e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.44 E-value: 9.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDET-----ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRl 75
Cdd:PRK13637 1 MSIKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 76 ECRRRIGMVFQ--EASLFDASVRRNAEYGLHVRRSWADRLRREVadlvglrngtsdaMEALETVGL--EDKLEQHAGSLS 151
Cdd:PRK13637 80 DIRKKVGLVFQypEYQLFEETIEKDIAFGPINLGLSEEEIENRV-------------KRAMNIVGLdyEDYKDKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 152 GGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEV 230
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
250
....*....|.
gi 909710455 231 GETDRIFEDPE 241
Cdd:PRK13637 227 GTPREVFKEVE 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-234 |
1.30e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.82 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTD---VWRASaqrrleCRRRIGMVFQEASLFDAS 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtVTRAS------LRRNIAVVFQDAGLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 VRRNAeyglhvrrswadRLRREVADLVGLRNGTSDAmEALETV-GLEDKLEQHAG----SLSGGEAQRVAFARALAYDPD 169
Cdd:PRK13657 425 IEDNI------------RVGRPDATDEEMRAAAERA-QAHDFIeRKPDGYDTVVGergrQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 170 FLLLDEPTSDLDprntAVIENAVREAGD---RGIGVAIATHDMNQARRiADQVAVILGDGIIEVGETD 234
Cdd:PRK13657 492 ILILDEATSALD----VETEAKVKAALDelmKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFD 554
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-239 |
2.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLE-CRRRIGMVFQ--EASLFDAS 94
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKqIRKKVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 VRRNAEYG---LHVRRSWADRLRREVADLVGLRngtsdamealetvglEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:PRK13649 103 VLKDVAFGpqnFGVSQEEAEALAREKLALVGIS---------------ESLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFED 239
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-241 |
2.25e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILE-----NVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRL 75
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEkkgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 76 -ECRRRIGMVFQ--EASLFDASVRRNAEYGlhvrrswadrlrrevadlvGLRNGTSD------AMEALETVGLEDKLEQH 146
Cdd:PRK13641 81 kKLRKKVSLVFQfpEAQLFENTVLKDVEFG-------------------PKNFGFSEdeakekALKWLKKVGLSEDLISK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 147 AG-SLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGD 225
Cdd:PRK13641 142 SPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
250
....*....|....*.
gi 909710455 226 GIIEVGETDRIFEDPE 241
Cdd:PRK13641 222 KLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
2.81e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwRASAQRRLECRRRI 81
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQEA--SLFDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVA 159
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVD-------------NALKRTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFE 238
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
...
gi 909710455 239 DPE 241
Cdd:PRK13636 232 EKE 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-222 |
4.48e-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: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRasaqRRLECRRRIGMVF-QEASL 90
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK----RRKKFLRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 -FDASVRRNAEYGLHVRRSWADRLRREVADLVglrngtsdamEALEtvgLEDKLEQHAGSLSGGEAQRVAFARALAYDPD 169
Cdd:cd03267 107 wWDLPVIDSFYLLAAIYDLPPARFKKRLDELS----------ELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 909710455 170 FLLLDEPTSDLDPRNTAVIENAVREAG-DRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-242 |
4.59e-27 |
|
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: 104.47 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecrrrigmVFQEASLFD-ASVR 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV--------VFQNYSLLPwLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAeyGLHVRRSWADRLRREVADLVGlrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEP 176
Cdd:TIGR01184 73 ENI--ALAVDRVLPDLSKSERRAIVE---------EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 177 TSDLDPRNTAVI-ENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDG----IIEVGETDriFEDPED 242
Cdd:TIGR01184 142 FGALDALTRGNLqEELMQIWEEHRVTVLMVTHDVDEALLLSDRV-VMLTNGpaanIGQILEVP--FPRPRD 209
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
18-249 |
4.60e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 104.92 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRleCRRrIGMVFQEAS-------- 89
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYR--CKH-IRMIFQDPNtslnprln 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 ---LFDASVRRNAEYglhvrrSWADRLRRevadlvglrngtsdAMEALETVGLedkLEQHAG----SLSGGEAQRVAFAR 162
Cdd:COG4167 106 igqILEEPLRLNTDL------TAEEREER--------------IFATLRLVGL---LPEHANfyphMLSSGQKQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAViLGDG-IIEVGETDRIFEDP 240
Cdd:COG4167 163 ALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLV-MHQGeVVEYGKTAEVFANP 241
|
....*....
gi 909710455 241 EDDRTQQFI 249
Cdd:COG4167 242 QHEVTKRLI 250
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-226 |
5.18e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 5.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRIGMVFQEA-- 88
Cdd:PRK13647 14 YKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKVGLVFQDPdd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 89 SLFDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:PRK13647 91 QVFSSTVWDDVAFGPVNMGLDKDEVERRVE-------------EALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDG 226
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQV-IVLKEG 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-236 |
1.33e-26 |
|
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: 107.90 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDEtILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASaqrRLECRRRIG 82
Cdd:TIGR01193 476 INDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDASVRRNAEYGlhVRRSWADRLRREVADLVGLRngtsDAMEALEtVGLEDKLEQHAGSLSGGEAQRVAFAR 162
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLG--AKENVSQDEIWAACEIAEIK----DDIENMP-LGYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIgVAIAtHDMNQARRiADQVAVILGDGIIEVGETDRI 236
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTI-IFVA-HRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-222 |
1.44e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.30 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLeCRRR 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARL-ARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASL-FDASVRRN-AEYGLHVRRSwadrlRREVADLVGlrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRV 158
Cdd:PRK13536 116 IGVVPQFDNLdLEFTVRENlLVFGRYFGMS-----TREIEAVIP---------SLLEFARLESKADARVSDLSGGMKRRL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-222 |
1.52e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 105.34 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 20 NVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdVWRASAQRrlEC----RRRIGMVFQEASLF-DAS 94
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDAEKG--IClppeKRRIGYVFQDARLFpHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 VRRNAEYGLhvrrswADRLRREVADLVGLrngtsdamealetVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLD 174
Cdd:PRK11144 93 VRGNLRYGM------AKSMVAQFDKIVAL-------------LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 909710455 175 EPTSDLD-PRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK11144 154 EPLASLDlPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-252 |
1.93e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.10 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 5 TVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKT----TLLRLLAlfEPP---RDGSLEYGGTDVWRASAQRRLEC 77
Cdd:PRK15134 12 SVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPvvyPSGDIRFHGESLLHASEQTLRGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 R-RRIGMVFQE--ASLfdaSVRRNAEYGLHVRRSWADRLRREVAdlvglrngTSDAMEALETVGLED---KLEQHAGSLS 151
Cdd:PRK15134 90 RgNKIAMIFQEpmVSL---NPLHTLEKQLYEVLSLHRGMRREAA--------RGEILNCLDRVGIRQaakRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 152 GGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEV 230
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
250 260
....*....|....*....|..
gi 909710455 231 GETDRIFEDPEDDRTQQFIDGE 252
Cdd:PRK15134 239 NRAATLFSAPTHPYTQKLLNSE 260
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-239 |
2.03e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.09 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLE-CRRRIGMVFQ--EASLFDAS 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 VRRNAEYGLHVRRswadrlrrevadlVGLRNGTSDAMEALETVGLE-DKLEQHAGSLSGGEAQRVAFARALAYDPDFLLL 173
Cdd:PRK13646 103 VEREIIFGPKNFK-------------MNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 174 DEPTSDLDPRNTAVIENAVREAG-DRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFED 239
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-239 |
3.63e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.27 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLE-CRRRIGMVFQ--EASLFDAS 94
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 VRRNAEYG---LHVRRSWADRLrrevadlvglrngtsdAMEALETVGLEDKL-EQHAGSLSGGEAQRVAFARALAYDPDF 170
Cdd:PRK13643 102 VLKDVAFGpqnFGIPKEKAEKI----------------AAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFED 239
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-219 |
5.51e-26 |
|
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: 101.36 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSL----EYGGTDVWRASAQRRLECRRR-IGMVFQeaslFd 92
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhDGGWVDLAQASPREILALRRRtIGYVSQ----F- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 asvrrnaeygLHV--RRSwadrlRREVADLVGLRNGTSD------AMEALETVGLEDKLEQHA-GSLSGGEAQRVAFARA 163
Cdd:COG4778 102 ----------LRVipRVS-----ALDVVAEPLLERGVDReeararARELLARLNLPERLWDLPpATFSGGEQQRVNIARG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 164 LAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIG-VAIaTHDMNQARRIADQV 219
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAiIGI-FHDEEVREAVADRV 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-207 |
5.52e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.72 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGtdvwraSAQRRLECRRRIGMVFQEASLFD 92
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVAEACHYLGHRNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 A-SVRRNAEYglhvrrsWADRLRrevadlvglrNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:PRK13539 87 AlTVAENLEF-------WAAFLG----------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATH 207
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-231 |
6.81e-26 |
|
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: 105.57 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETI--LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLEC-RRRIGM 83
Cdd:TIGR02203 335 NVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL----ADYTLASlRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 84 VFQEASLFDASVRRNAEYGlhvRRSWADR--LRREVADlvglrngtSDAMEALETV--GLEDKLEQHAGSLSGGEAQRVA 159
Cdd:TIGR02203 411 VSQDVVLFNDTIANNIAYG---RTEQADRaeIERALAA--------AYAQDFVDKLplGLDTPIGENGVLLSGGQRQRLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIAtHDMNQARRiADQVaVILGDG-IIEVG 231
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA-HRLSTIEK-ADRI-VVMDDGrIVERG 549
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-239 |
8.95e-26 |
|
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: 105.27 E-value: 8.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRR----IGMVFQeaslfda 93
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDGRGRakryIGILHQ------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 svrrnaEYGLHVRRSWADRLRR----EVADLVGLRNgtsdAMEALETVGLEDK-----LEQHAGSLSGGEAQRVAFARAL 164
Cdd:TIGR03269 373 ------EYDLYPHRTVLDNLTEaiglELPDELARMK----AVITLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 165 AYDPDFLLLDEPTSDLDP--RNTAV--IENAVREAGDRGIgvaIATHDMNQARRIADQVAVILGDGIIEVGETDRIFED 239
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPitKVDVThsILKAREEMEQTFI---IVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-250 |
1.03e-25 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 100.55 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRasaqRRLecrRRIG 82
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR----KDL---HKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLF-DASVRRNaeygLHVRrswadrlrrevADLVGLRngTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:TIGR03740 74 SLIESPPLYeNLTAREN----LKVH-----------TTLLGLP--DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVIlGDGIIevGETDRIfeDPE 241
Cdd:TIGR03740 137 IALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGII-SEGVL--GYQGKI--NKS 211
|
....*....
gi 909710455 242 DDRTQQFID 250
Cdd:TIGR03740 212 ENLEKLFVE 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-207 |
2.73e-25 |
|
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: 98.78 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 5 TVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLA--LFEPPRDGSLEYGGTDVwrasaqRRLECRRRIG 82
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DKRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDA-SVRRNAEYGLHVRrswadrlrrevadlvglrngtsdamealetvgledkleqhagSLSGGEAQRVAFA 161
Cdd:cd03213 86 YVPQDDILHPTlTVRETLMFAAKLR------------------------------------------GLSGGERKRVSIA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATH 207
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-249 |
2.74e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.42 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGT---DVWRAsaqrrlecRRRIGMVFQEA 88
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPA--------ERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 89 SLF-DASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:PRK11000 85 ALYpHLSVAENMSFGLKLAGAKKEEINQRVN-------------QVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 168 PDFLLLDEPTSDLDP--RNTAVIENAV--REAGDRGIGVaiaTHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDD 243
Cdd:PRK11000 152 PSVFLLDEPLSNLDAalRVQMRIEISRlhKRLGRTMIYV---THDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANR 228
|
....*.
gi 909710455 244 RTQQFI 249
Cdd:PRK11000 229 FVAGFI 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-241 |
3.04e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.64 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 15 ETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQ--EASLFD 92
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQnpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEYGLHVRRSWADRLRREVADlvglrngtsdameALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRD-------------VLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 173 LDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQArRIADQVaVILGDG-IIEVGETDRIFEDPE 241
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEA-NMADQV-LVLDDGkLLAQGSPVEIFSKVE 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-253 |
8.79e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 99.00 E-value: 8.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKT-TLLRLLALFEP---PRDGSLEYGGTDVwrASAQRRlecRRRIGMVFQE 87
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPV--APCALR---GRKIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 AslfdasvrRNAEYGLHVRRSWAdrlrREVADLVGLRNGTSDAMEALETVGLEDK---LEQHAGSLSGGEAQRVAFARAL 164
Cdd:PRK10418 88 P--------RSAFNPLHTMHTHA----RETCLALGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 165 AYDPDFLLLDEPTSDLD----PRNTAVIENAVREagdRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDvvaqARILDLLESIVQK---RALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
250
....*....|...
gi 909710455 241 EDDRTQQFIDGEL 253
Cdd:PRK10418 233 KHAVTRSLVSAHL 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-244 |
3.48e-24 |
|
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: 100.65 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFE--PPRDGSLEY------------------------GGT- 64
Cdd:TIGR03269 10 FDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverpskvgepcpvcGGTl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 65 -----DVWRASAQRRLECRRRIGMVFQEA-SLF-DASVRRNAEYGLHvrrswadRLRREVADLVGLrngtsdAMEALETV 137
Cdd:TIGR03269 90 epeevDFWNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNVLEALE-------EIGYEGKEAVGR------AVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 138 GLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREA-GDRGIGVAIATHDMNQARRIA 216
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 909710455 217 DQvAVILGDG-IIEVGETDRI-------FEDPEDDR 244
Cdd:TIGR03269 237 DK-AIWLENGeIKEEGTPDEVvavfmegVSEVEKEC 271
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-183 |
4.86e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.07 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRrlecRRRIGMVFQEASLFDA 93
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL----SSLISVLNQRPYLFDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRNaeyglhvrrswadrlrrevadlVGLRngtsdamealetvgledkleqhagsLSGGEAQRVAFARALAYDPDFLLL 173
Cdd:cd03247 90 TLRNN----------------------LGRR-------------------------FSGGERQRLALARILLQDAPIVLL 122
|
170
....*....|
gi 909710455 174 DEPTSDLDPR 183
Cdd:cd03247 123 DEPTVGLDPI 132
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-241 |
5.47e-24 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 96.07 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 23 LAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRAsaqrrlecRRRIGMVFQEASL---FDASVRRNA 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG--------WRHIGYVPQRHEFawdFPISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 100 EYGLHVRRSWadrLRRE-VADLVGLRngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTS 178
Cdd:TIGR03771 73 MSGRTGHIGW---LRRPcVADFAAVR-------DALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFT 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 179 DLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDGIIEVGETDRIfEDPE 241
Cdd:TIGR03771 143 GLDMPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL-QDPA 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-215 |
6.47e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.18 E-value: 6.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGY--GDETI--LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWR----ASAQRR 74
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 75 lecRRRIGMVFQEASLFD-ASVRRNAEY-GLHVRRSWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSG 152
Cdd:PRK10535 85 ---REHFGFIFQRYHLLShLTAAQNVEVpAVYAGLERKQRLLR--------------AQELLQRLGLEDRVEYQPSQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 153 GEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHD---MNQARRI 215
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDpqvAAQAERV 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-249 |
6.86e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTT----LLRLLAlfeppRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQE- 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 -ASLFDA-SVRRNAEYGLHVRRSWADRLRREvadlvglrngtSDAMEALETVGLEDKLEQ-HAGSLSGGEAQRVAFARAL 164
Cdd:PRK15134 372 nSSLNPRlNVLQIIEEGLRVHQPTLSAAQRE-----------QQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 165 AYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDD 243
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQE 520
|
....*.
gi 909710455 244 RTQQFI 249
Cdd:PRK15134 521 YTRQLL 526
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-181 |
1.20e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 97.61 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 21 VSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasaqRRLECRRR-IGMVFQEASLF-DASVRRN 98
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV------NELEPADRdIAMVFQNYALYpHMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 99 AEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTS 178
Cdd:PRK11650 97 MAYGLKIRGMPKAEIEERVA-------------EAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
...
gi 909710455 179 DLD 181
Cdd:PRK11650 164 NLD 166
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-195 |
1.58e-23 |
|
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: 94.48 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 6 VGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLlrLLALFE--PPRDGSLEYGGTDVwraSAQRRLECRRRIGM 83
Cdd:cd03244 8 VSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSL--LLALFRlvELSSGSILIDGVDI---SKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 84 VFQEASLFDASVRRNAE-YGLHvrrswadrlrrevadlvglrngtSDAM--EALETVGLEDKLEQHAGSL---------- 150
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDpFGEY-----------------------SDEElwQALERVGLKEFVESLPGGLdtvveeggen 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 909710455 151 -SGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREA 195
Cdd:cd03244 140 lSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREA 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-241 |
1.73e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLE----YGGTDVWRASA-----QRRL----ECRRRIG 82
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELitnpySKKIknfkELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQ--EASLFDASVRRNAEYG---LHVRRSWADRLrrevadlvglrngtsdAMEALETVGL-EDKLEQHAGSLSGGEAQ 156
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGpvaLGVKKSEAKKL----------------AKFYLNKMGLdDSYLERSPFGLSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 157 RVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRI 236
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
....*
gi 909710455 237 FEDPE 241
Cdd:PRK13631 264 FTDQH 268
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-230 |
2.00e-23 |
|
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: 92.13 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdvwrasaqrrlecrRRIGmvfq 86
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------VKIG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 easlfdasvrrnaeYglhvrrswadrlrrevadlvglrngtsdamealetvgledkLEQhagsLSGGEAQRVAFARALAY 166
Cdd:cd03221 67 --------------Y-----------------------------------------FEQ----LSGGEKMRLALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREagDRGiGVAIATHDmnqaRRIADQVAvilgDGIIEV 230
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEALKE--YPG-TVILVSHD----RYFLDQVA----TKIIEL 140
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-222 |
2.35e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecRRRIGMVFQEASLF 91
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAI--ALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DA-SVRRN----AEYGLHVRRSWAdRLRREVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:COG3845 93 PNlTVAENivlgLEPTKGGRLDRK-AARARIREL-------------SERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-222 |
2.79e-23 |
|
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: 92.88 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecRRRIGMV----FQEASLFDA 93
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI--RAGIAYVpedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRNAEYGLHvrrswadrlrrevadlvglrngtsdamealetvgledkleqhagsLSGGEAQRVAFARALAYDPDFLLL 173
Cdd:cd03215 94 SVAENIALSSL---------------------------------------------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 909710455 174 DEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVM 177
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
6.04e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.48 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGY-GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRI 81
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR---EVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 82 GMVFQ--EASLFDASVRRNAEYGlhvrrswadrlrrevADLVGLRNGTSD--AMEALETVGLEDKLEQHAGSLSGGEAQR 157
Cdd:PRK13652 81 GLVFQnpDDQIFSPTVEQDIAFG---------------PINLGLDEETVAhrVSSALHMLGLEELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRI 236
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....*
gi 909710455 237 FEDPE 241
Cdd:PRK13652 226 FLQPD 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1-219 |
6.70e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.75 E-value: 6.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGygdetiLENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRdGSLEYGGTDV--WRASAQRRLEC- 77
Cdd:COG4138 1 LQLNDVAVAGR------LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLsdWSAAELARHRAy 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 -----RRRIGM-VFQEASLFDASVRRNAEyglhvrrswadrLRREVADLVglrngtsdamEALetvGLEDKLEQHAGSLS 151
Cdd:COG4138 74 lsqqqSPPFAMpVFQYLALHQPAGASSEA------------VEQLLAQLA----------EAL---GLEDKLSRPLTQLS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 152 GGEAQRVAFARAL-----AYDPD--FLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQV 219
Cdd:COG4138 129 GGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRV 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-231 |
1.57e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.07 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRdGSLEYGGTDVwrasaqRRLEC---RRRIGMVFQEASLFD 92
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIEL------RELDPeswRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEYGLHvrrswadRLRREVADLVGLRNGTSDAMEALETvGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:PRK11174 437 GTLRDNVLLGNP-------DASDEQLQQALENAWVSEFLPLLPQ-GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 173 LDEPTSDLDPRNTAVIENAVREAGDRGIGVAIaTHDMNQARRIaDQVAVILGDGIIEVG 231
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMV-THQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-183 |
1.68e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 91.95 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfepprdGSLEYGGT---DVWRASAQR-RLECRRRIGMVFQEASLFD 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIS-------GRVEGGGTtsgQILFNGQPRkPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 A-SVRRNAEYGLHVR--RSWADRLRREVADLVGLRNgtsdamealetVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPD 169
Cdd:cd03234 95 GlTVRETLTYTAILRlpRKSSDAIRKKRVEDVLLRD-----------LALTRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170
....*....|....
gi 909710455 170 FLLLDEPTSDLDPR 183
Cdd:cd03234 164 VLILDEPTSGLDSF 177
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-235 |
3.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.10 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLalfepprDGSLEYGGTDVW----RASAQRRLECRRRIGMVFQ--E 87
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI-------DGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQnpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 ASLFDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:PRK13650 92 NQFVGATVEDDVAFGLENKGIPHEEMKERVN-------------EALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQArRIADQVAViLGDGIIEVGETDR 235
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLV-MKNGQVESTSTPR 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1-219 |
6.80e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 6.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEhgygdeTILENVSLAVPPGEVVAIIGPSGVGKTTLL-RLLALFepPRDGSLEYGGTDV--WRASAQRRLEC 77
Cdd:PRK03695 1 MQLNDVAVS------TRLGPLSAEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAGQPLeaWSAAELARHRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 ------RRRIGM-VFQEASLFDASVRRNAEYGLHVrrswadrlrREVADLvglrngtsdamealetVGLEDKLEQHAGSL 150
Cdd:PRK03695 73 ylsqqqTPPFAMpVFQYLTLHQPDKTRTEAVASAL---------NEVAEA----------------LGLDDKLGRSVNQL 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 151 SGGEAQRVAFARA-LAYDPD------FLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQV 219
Cdd:PRK03695 128 SGGEWQRVRLAAVvLQVWPDinpagqLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRV 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-183 |
7.13e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.12 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDET--ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDV--WRASAQRRLecr 78
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadYSEAALRQA--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 79 rrIGMVFQEASLFDASVRRNAeyglhvrrswadrlrrevadLVGLRNGTSDAM-EALETVGLEDKLEQHAG--------- 148
Cdd:PRK11160 416 --ISVVSQRVHLFSATLRDNL--------------------LLAAPNASDEALiEVLQQVGLEKLLEDDKGlnawlgegg 473
|
170 180 190
....*....|....*....|....*....|....*.
gi 909710455 149 -SLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPR 183
Cdd:PRK11160 474 rQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-226 |
1.26e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASaqRRLECRRRIGMVFQ 86
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD--HKLAAQLGIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDA-SVRRNAEYGLH-VRRSWAdrlrrevADLVGLRNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARAL 164
Cdd:PRK09700 88 ELSVIDElTVLENLYIGRHlTKKVCG-------VNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 165 AYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAViLGDG 226
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTV-MKDG 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-214 |
1.32e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 89.84 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECR-RRIGMVFQEASLFDAs 94
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 vrRNAeyglhvrrswadrlrREVADLVGLRNGTSD------AMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:PRK10584 103 --LNA---------------LENVELPALLRGESSrqsrngAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 169 DFLLLDEPTSDLDprntavienavREAGDR------------GIGVAIATHDMNQARR 214
Cdd:PRK10584 166 DVLFADEPTGNLD-----------RQTGDKiadllfslnrehGTTLILVTHDLQLAAR 212
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-207 |
1.62e-21 |
|
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: 88.95 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLECRRRIGMVFQEASLFD 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 A-SVRRNAEYglhvrrsWADRLRREvadlvglrngTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:TIGR01189 87 ElSALENLHF-------WAAIHGGA----------QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATH 207
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-249 |
1.71e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecRRRIGMV----FQEASLFDA 93
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI--RAGIAYVpedrKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRN---AEYGLHVRRSWADRlRREVADlvglrngTSDAMEALETvgledK---LEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:COG1129 346 SIRENitlASLDRLSRGGLLDR-RRERAL-------AEEYIKRLRI-----KtpsPEQPVGNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAViLGDGIIeVGETDRifedpeDDRTQQ 247
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILV-MREGRI-VGELDR------EEATEE 484
|
..
gi 909710455 248 FI 249
Cdd:COG1129 485 AI 486
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-241 |
1.96e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.05 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 20 NVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRrlecRRRIGMV--FQEASLF-DASVR 96
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ----IARMGVVrtFQHVRLFrEMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNaeygLHVrrswADRLRREVADLVGL------RNGTSDAMEA----LETVGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:PRK11300 99 EN----LLV----AQHQQLKTGLFSGLlktpafRRAESEALDRaatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPE 241
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-240 |
2.04e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.43 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDET-ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASaqRRLECRRRIGMVFQ 86
Cdd:PRK13644 7 VSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 --EASLFDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARAL 164
Cdd:PRK13644 85 npETQFVGRTVEEDLAFGPENLCLPPIEIRKRVD-------------RALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 165 AYDPDFLLLDEPTSDLDPRN-TAVIENaVREAGDRGIGVAIATHDMNQArRIADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSgIAVLER-IKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-226 |
2.14e-21 |
|
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: 88.68 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLaLFE-PPRDGSLEYGGtdvwrasaqrrlecrrRIGMVFQEASLFDASV 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPG----------------SIAYVSQEPWIQNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 96 RRNAEYGLHVRRSWADR------LRRevaDLVGLRNGtsDAMEaletVGlEDKLeqhagSLSGGEAQRVAFARALAYDPD 169
Cdd:cd03250 83 RENILFGKPFDEERYEKvikacaLEP---DLEILPDG--DLTE----IG-EKGI-----NLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 170 FLLLDEPTSDLDPrNTA--VIENAVREAGDRGIGVAIATHDMnQARRIADQVaVILGDG 226
Cdd:cd03250 148 IYLLDDPLSAVDA-HVGrhIFENCILGLLLNNKTRILVTHQL-QLLPHADQI-VVLDNG 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-241 |
2.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRL---LALFEPPRDGSLEYG-GTDVWRASAQRRLecRRRIGMVFQ--EASLF 91
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngLIISETGQTIVGDYAiPANLKKIKEVKRL--RKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DASVRRNAEYG-LHVRRSWADRLRR--EVADLVGLRngtsdamealetvglEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:PRK13645 105 QETIEKDIAFGpVNLGENKQEAYKKvpELLKLVQLP---------------EDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENA-VREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPE 241
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-228 |
3.87e-21 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 89.50 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLA--LFEPPRDGSLEYGGTDVWRASAQRRLECRR--RIGMVFQEAS-- 89
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdLTGGGAPRGARVTGDVTLNGEPLAAIDAPRlaRLRAVLPQAAqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 LFDASVRRNAEYGL--HVRRSWADRLR-REVADlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:PRK13547 95 AFAFSAREIVLLGRypHARRAGALTHRdGEIAW------------QALALAGATALVGRDVTTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 167 ---------DPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAvILGDGII 228
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRlARDWNLGVLAIVHDPNLAARHADRIA-MLADGAI 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-184 |
4.84e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.79 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfepprdgsleyggtDVWRAsAQRRLECRRRIGMVF--QEASLF 91
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---------------GLWPY-GSGRIARPAGARVLFlpQRPYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DASVRRNAEYGLHVRRSWADRLRrevadlvglrngtsdamEALETVGLE---DKLEQHAG---SLSGGEAQRVAFARALA 165
Cdd:COG4178 439 LGTLREALLYPATAEAFSDAELR-----------------EALEAVGLGhlaERLDEEADwdqVLSLGEQQRLAFARLLL 501
|
170
....*....|....*....
gi 909710455 166 YDPDFLLLDEPTSDLDPRN 184
Cdd:COG4178 502 HKPDWLFLDEATSALDEEN 520
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-239 |
5.10e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.65 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRAS---AQRRlecrr 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQL----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 80 RIGMVFQEASLF-DASVRRNAEYGLHVRRSWADRLRREVADLvglrngtsdamealetvGLEDKLEQHAGSLSGGEAQRV 158
Cdd:PRK15439 87 GIYLVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQLLAAL-----------------GCQLDLDSSAGSLEVADRQIV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFE 238
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
.
gi 909710455 239 D 239
Cdd:PRK15439 230 D 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-238 |
6.09e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGtdvwRASAQrrLEcrrrIGMVFQEaslfDASV 95
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----RVSAL--LE----LGAGFHP----ELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 96 RRNAE-----YGLhvRRSWADRLRREVADLvglrngtsdAmealetvGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDF 170
Cdd:COG1134 106 RENIYlngrlLGL--SRKEIDEKFDEIVEF---------A-------ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 171 LLLDEPTS--DLDPRNTAviENAVREAGDRGIGVAIATHDMNQARRIADQVAViLGDG-IIEVGETDRIFE 238
Cdd:COG1134 168 LLVDEVLAvgDAAFQKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIW-LEKGrLVMDGDPEEVIA 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-241 |
7.70e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 7.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwRASAQRRLECRRRIG 82
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQ--EASLFDASVRRNAEYGLHVRRSWADRLRREVADlvglrngtsdameALETVGLEDKLEQHAGSLSGGEAQRVAF 160
Cdd:PRK13638 81 TVFQdpEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDE-------------ALTLVDAQHFRHQPIQCLSHGQKKRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACT 227
|
.
gi 909710455 241 E 241
Cdd:PRK13638 228 E 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-222 |
8.37e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.53 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALF---EPPRDGSLEYGGTDVWRASAQRR--LECRRRIGMVFQEASLFD 92
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARdiRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 A-SVRRNAEYGL-------HVRRSWADRLRREvadlvglrngtsDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARAL 164
Cdd:PRK09984 100 RlSVLENVLIGAlgstpfwRTCFSWFTREQKQ------------RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 165 AYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVAL 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-240 |
1.33e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.92 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDV--WRASAQRR------LECRRRIGMVF 85
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLesWSSKAFARkvaylpQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 QEAslfdASVRRNAEYGLHVRRSWADRLRREvadlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALA 165
Cdd:PRK10575 103 REL----VAIGRYPWHGALGRFGAADREKVE---------------EAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 166 YDPDFLLLDEPTSDLD-PRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:PRK10575 164 QDSRCLLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-238 |
1.99e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.22 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLA--LFepPRDGSLEYGGTDVWRasaqRRLECRRRIGMVF-QEASLF--- 91
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTgiLV--PTSGEVRVLGYVPFK----RRKEFARRIGVVFgQRSQLWwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 ---DaSVRRNAE-YGLHvrrswADRLRREVADLVglrngtsdamealETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:COG4586 112 paiD-SFRLLKAiYRIP-----DAEYKKRLDELV-------------ELLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 168 PDFLLLDEPTSDLDprntAVIENAVREA-----GDRGIGVAIATHDMNQARRIADQVaVILGDG-IIEVGETDRIFE 238
Cdd:COG4586 173 PKILFLDEPTIGLD----VVSKEAIREFlkeynRERGTTILLTSHDMDDIEALCDRV-IVIDHGrIIYDGSLEELKE 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-230 |
2.12e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.43 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 11 GYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWrasaqrRLEcrrrIGMVFQEasl 90
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS------LLG----LGGGFNP--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 fDASVRRNAEYglhvrrswadrlrreVADLVGLRNGTSDAMEA--LETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:cd03220 98 -ELTGRENIYL---------------NGRLLGLSRKEIDEKIDeiIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQvAVILGDGIIEV 230
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDR-ALVLEKGKIRF 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-242 |
6.13e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLL-ALFEpprdgslEYGGT---DVWRASAQRRLECRRRIGMVFQ--E 87
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIdGLFE-------EFEGKvkiDGELLTAENVWNLRRKIGMVFQnpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 ASLFDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:PRK13642 92 NQFVGATVEDDVAFGMENQGIPREEMIKRVD-------------EALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRiADQVAVILGDGIIEVGETDRIFEDPED 242
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-231 |
6.22e-20 |
|
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: 84.50 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPR--DGSLEYGGTDVWRASAQRRleCRRRIGMVFQEAsl 90
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEER--ARLGIFLAFQYP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 fdasvrrnaeyglhvrrswadrlrrevADLVGLRNgtsdaMEALETVGLedkleqhagSLSGGEAQRVAFARALAYDPDF 170
Cdd:cd03217 87 ---------------------------PEIPGVKN-----ADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHdmnqARRIADQV----AVILGDG-IIEVG 231
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH----YQRLLDYIkpdrVHVLYDGrIVKSG 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-220 |
7.96e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 88.07 E-value: 7.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGsleyggtdvwrasaQRRLECRRRIGMVFQEASLfD 92
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPGIKVGYLPQEPQL-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 AS--VRRNAEYGLHVRRSWADRLRrEVADLVGLRNGTSDAM--------EALETVG---LEDKLEQHA------------ 147
Cdd:TIGR03719 81 PTktVRENVEEGVAEIKDALDRFN-EISAKYAEPDADFDKLaaeqaelqEIIDAADawdLDSQLEIAMdalrcppwdadv 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 148 GSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAgdRGIGVAIaTHDmnqaRRIADQVA 220
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAV-THD----RYFLDNVA 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-207 |
8.04e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.62 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfepprdgsleyggtdvwrasaqRRLECRRRIG 82
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-----------------------GALKGTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVfqeaslfdasvrrnaeyglhvrRSWADRLRREVA--DLVGLRNGTSDAMEALETVGLED------KLEQhagsLSGGE 154
Cdd:COG2401 88 CV----------------------DVPDNQFGREASliDAIGRKGDFKDAVELLNAVGLSDavlwlrRFKE----LSTGQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 909710455 155 AQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATH 207
Cdd:COG2401 142 KFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-249 |
8.18e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.37 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQE--ASLfdaSV 95
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASL---DP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 96 RRNAEYglhvrrSWADRLRrevadLVGLRNGTSDAMEA---LETVGLedkLEQHA----GSLSGGEAQRVAFARALAYDP 168
Cdd:PRK10261 417 RQTVGD------SIMEPLR-----VHGLLPGKAAAARVawlLERVGL---LPEHAwrypHEFSGGQRQRICIARALALNP 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQ 247
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQIINLLLDlQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRK 562
|
..
gi 909710455 248 FI 249
Cdd:PRK10261 563 LM 564
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-231 |
8.71e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 8.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwRASAQRRLecRRRIGMVFQEASLFDA 93
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL-RDYTLASL--RNQVALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRNAEYGLHVRRSwadrlRREVADLVGLrngtSDAMEALETV--GLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:PRK11176 432 TIANNIAYARTEQYS-----REQIEEAARM----AYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVaIAtHDMNQARRiADQVAVILGDGIIEVG 231
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDElQKNRTSLV-IA-HRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-244 |
9.90e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 87.68 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdvwrasaqrrlecrRRIGMVFQ 86
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET--------------VKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDASvrrnaeyglhvRRSWadrlrREVAD-----LVGLRNGTSDAMEALETVGLEDKlEQHAGSLSGGEAQRVAFA 161
Cdd:TIGR03719 393 SRDALDPN-----------KTVW-----EEISGgldiiKLGKREIPSRAYVGRFNFKGSDQ-QKKVGQLSGGERNRVHLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGdrGIGVAIaTHDMNQARRIADQVAVILGDGIIEVGETDriFEDPE 241
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVVI-SHDRWFLDRIATHILAFEGDSHVEWFEGN--FSEYE 530
|
...
gi 909710455 242 DDR 244
Cdd:TIGR03719 531 EDK 533
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-253 |
1.12e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.30 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 21 VSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQE--ASLfdaSVRRN 98
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASL---NPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 99 -----AEyglHVRRSWADRLRREVADLVglrngtsDAMeaLETVGL-EDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:PRK15079 117 igeiiAE---PLRTYHPKLSRQEVKDRV-------KAM--MLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 173 LDEPTSDLDPRNTAVIENAVREAgDRGIGVA---IAtHDMNQARRIADQVAVI-LGDGiIEVGETDRIFEDP-------- 240
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQL-QREMGLSlifIA-HDLAVVKHISDRVLVMyLGHA-VELGTYDEVYHNPlhpytkal 261
|
250 260
....*....|....*....|....
gi 909710455 241 -----------EDDRTQQFIDGEL 253
Cdd:PRK15079 262 msavpipdpdlERNKTIQLLEGEL 285
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-214 |
1.23e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwRASAQRRLECrRRIGMVFQ 86
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-ADARHRRAVC-PRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 ------EASLfdaSVRRNAE-----YGLhvrrSWADRLRReVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGGEA 155
Cdd:NF033858 84 glgknlYPTL---SVFENLDffgrlFGQ----DAAERRRR-IDEL-------------LRATGLAPFADRPAGKLSGGMK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDP--RNT--AVIENaVReAGDRGIGVAIATHDMNQARR 214
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDPlsRRQfwELIDR-IR-AERPGMSVLVATAYMEEAER 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-181 |
1.58e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.41 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPrdgSLEYGGTDVWRASAQRRLECRRRIGMVfQEASLFDAS- 94
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK---GVKGSGSVLLNGMPIDAKEMRAISAYV-QQDDLFIPTl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 -VRRNAEYGLHVR--RSWADRLRREVADLVGLRNGTSDAMEALetVGLEDKLEqhagSLSGGEAQRVAFARALAYDPDFL 171
Cdd:TIGR00955 115 tVREHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCANTR--IGVPGRVK----GLSGGERKRLAFASELLTDPPLL 188
|
170
....*....|
gi 909710455 172 LLDEPTSDLD 181
Cdd:TIGR00955 189 FCDEPTSGLD 198
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-241 |
3.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.37 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTD------VWrasaqrrlECRRRIGMVFQ--EAS 89
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenLW--------DIRNKAGMVFQnpDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 LFDASVRRNAEYGLHVRRSWADRLRREVAdlvglrngtsdamEALETVGLEDkLEQHAGS-LSGGEAQRVAFARALAYDP 168
Cdd:PRK13633 98 IVATIVEEDVAFGPENLGIPPEEIRERVD-------------ESLKKVGMYE-YRRHAPHlLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRiADQVAVILGDGIIEVGETDRIFEDPE 241
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-212 |
4.85e-19 |
|
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: 82.16 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGtdvwRASAQRRLECRRRIG 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDA-SVRRNAEYglhvrrsWADRlrrevadlvglrNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFA 161
Cdd:cd03231 77 YLGHAPGIKTTlSVLENLRF-------WHAD------------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 909710455 162 RALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATH-DMNQA 212
Cdd:cd03231 138 RLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLS 189
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-181 |
1.54e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEhgYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYggtdvwrasaQRRLecrrR 80
Cdd:PRK09544 5 VSLENVSVS--FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR----------NGKL----R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLfdasvrrNAEYGLHVRRswadrlrrevadLVGLRNGT--SDAMEALETVGLEDKLEQHAGSLSGGEAQRV 158
Cdd:PRK09544 69 IGYVPQKLYL-------DTTLPLTVNR------------FLRLRPGTkkEDILPALKRVQAGHLIDAPMQKLSGGETQRV 129
|
170 180
....*....|....*....|...
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLD 181
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVD 152
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-235 |
1.71e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLEC--------RRRIGMVFqeas 89
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLVP---- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 lfDASVRRNAEYGLHVRRSWADR--LRREVAdlvglRNGTSDAMEALE--TVGLEDKleqhAGSLSGGEAQRVAFARALA 165
Cdd:COG3845 350 --DMSVAENLILGRYRRPPFSRGgfLDRKAI-----RAFAEELIEEFDvrTPGPDTP----ARSLSGGNQQKVILARELS 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILgDGIIeVGETDR 235
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMY-EGRI-VGEVPA 486
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-228 |
2.93e-18 |
|
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: 83.68 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 22 SLAVP-PGEVVAIIGPSGVGKTTLLRLLA------LFEPPRDGSLE-----YGGT---DVWRASAQRRLECRRRIGMVFQ 86
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSgelkpnLGDYDEEPSWDevlkrFRGTelqDYFKKLANGEIKVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDASVRrnaeyglhvrrswaDRLRRevADLVGlrngtsDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:COG1245 172 IPKVFKGTVR--------------ELLEK--VDERG------KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGD----GII 228
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEpgvyGVV 295
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-212 |
2.94e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.23 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETIL-ENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasaqrrlecrRRIGMVFQEASLF- 91
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI------------RRQRDEYHQDLLYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 --DASVRR--NAEYGLHvrrsWADRLRREVadlvglrnGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:PRK13538 80 ghQPGIKTelTALENLR----FYQRLHGPG--------DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDRGiGVAIAT--HDMNQA 212
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQHAEQG-GMVILTthQDLPVA 193
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-222 |
3.41e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecRRRIGMVFQEASLF 91
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--REAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 D-ASVRRNAEYG--LHVRRSWADRLRReVADLVGLrngtsdamealetvgLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:PRK11614 93 SrMTVEENLAMGgfFAERDQFQERIKW-VYELFPR---------------LHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 909710455 169 DFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVL 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-220 |
9.66e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.09 E-value: 9.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGyGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGsleyggtDVWRASAQRrlecrrr 80
Cdd:PRK11819 7 YTMNRVSKVVP-PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLfDAS--VRRNAEYGLHVRRSWADRLRrEVADLVGLRNGTSDAM--------EALETVG---LEDKLEQHA 147
Cdd:PRK11819 72 VGYLPQEPQL-DPEktVRENVEEGVAEVKAALDRFN-EIYAAYAEPDADFDALaaeqgelqEIIDAADawdLDSQLEIAM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 148 ------------GSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAgdRGIGVAIaTHDmnqaRRI 215
Cdd:PRK11819 150 dalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PGTVVAV-THD----RYF 222
|
....*
gi 909710455 216 ADQVA 220
Cdd:PRK11819 223 LDNVA 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-246 |
1.29e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.56 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETI----LENVSLAVPPGEVVAIIGPSGVGKT-TLLRLLALFEPP---RDGSLEYGGTDVWRASA-QRRLECRRRIG 82
Cdd:PRK11022 13 FGDESApfraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEkERRNLVGAEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQeaslfDASVRRNAEY--------GLHVRRSWADRLRREvadlvglrngtsDAMEALETVGLED---KLEQHAGSLS 151
Cdd:PRK11022 93 MIFQ-----DPMTSLNPCYtvgfqimeAIKVHQGGNKKTRRQ------------RAIDLLNQVGIPDpasRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 152 GGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEV 230
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250
....*....|....*.
gi 909710455 231 GETDRIFEDPEDDRTQ 246
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQ 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-195 |
1.94e-17 |
|
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: 79.51 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTL----LRLLALfepprDGSLEYGGTDVWRASAQrrlE 76
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNT-----EGDIQIDGVSWNSVPLQ---K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 77 CRRRIGMVFQEASLFDASVRRNAE-YGlhvrrSWADRLRREVADLVGLRNGTSDAMEALETVgledkLEQHAGSLSGGEA 155
Cdd:cd03289 75 WRKAFGVIPQKVFIFSGTFRKNLDpYG-----KWSDEEIWKVAEEVGLKSVIEQFPGQLDFV-----LVDGGCVLSHGHK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREA 195
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQA 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-222 |
3.38e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.36 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEP--PRDGSLEYGGTDVwRASAQRRLEcRRR 80
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEEL-QASNIRDTE-RAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLF-DASVRRN----AEYGLHVRRSWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEA 155
Cdd:PRK13549 84 IAIIHQELALVkELSVLENiflgNEITPGGIMDYDAMYLR--------------AQKLLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVI 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-222 |
5.81e-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: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEP--PRDGSLEYGGTDVwRASAQRRLEcRRR 80
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPL-KASNIRDTE-RAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLF-DASVRRNAEYGLHV-----RRSWADRLRREVADLVGLRngtSDAMEALETVGledkleqhagSLSGGE 154
Cdd:TIGR02633 80 IVIIHQELTLVpELSVAENIFLGNEItlpggRMAYNAMYLRAKNLLRELQ---LDADNVTRPVG----------DYGGGQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 155 AQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-224 |
1.63e-16 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 76.64 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 23 LAVP-PGEVVAIIGPSGVGKTTLLRLLALFEPPRDGslEYGGTDVWRAsaqrrlecrrrIGMVFQEASLFDASVR-RNAE 100
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWDE-----------ILDEFRGSELQNYFTKlLEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 101 YGLHVRRSWADRLRREVADLVGLRNGTSDAMEALETV----GLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEP 176
Cdd:cd03236 87 VKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELvdqlELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 909710455 177 TSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILG 224
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-195 |
1.78e-16 |
|
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: 78.80 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 1 MTLQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTL----LRLLAlfeppRDGSLEYGGTDVWRASAQRrle 76
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLS-----TEGEIQIDGVSWNSVTLQT--- 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 77 CRRRIGMVFQEASLFDASVRRNaeygLHVRRSWADRLRREVADLVGLRNGTSDAMEALETVgledkLEQHAGSLSGGEAQ 156
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTFRKN----LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFV-----LVDGGYVLSNGHKQ 1360
|
170 180 190
....*....|....*....|....*....|....*....
gi 909710455 157 RVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREA 195
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS 1399
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-222 |
2.17e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 20 NVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLEcrrrIGMVF-----QEASLF-DA 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA----RGLVYlpedrQSSGLYlDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRNAEYGLHVRRSWADRLRREVADLVGLRngtsdamEALeTVGLEDkLEQHAGSLSGGEAQRVAFARALAYDPDFLLL 173
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAVLERYR-------RAL-NIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 909710455 174 DEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-228 |
3.07e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 22 SLAVP-PGEVVAIIGPSGVGKTTLLRLLA------LFEPPRDGSLE-----YGGT---DVWRASAQRRLECRRRIGMVFQ 86
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKILSgelipnLGDYEEEPSWDevlkrFRGTelqNYFKKLYNGEIKVVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 EASLFDASVRrnaeyglhvrrswaDRLRRevADLVGLRNgtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:PRK13409 172 IPKVFKGKVR--------------ELLKK--VDERGKLD------EVVERLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGdRGIGVAIATHDMNQARRIADQVAVILGD----GII 228
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHIAYGEpgayGVV 294
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-222 |
3.74e-16 |
|
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: 77.75 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 29 EVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasaQRRLEC-RRRIGMVFQEASLFD-ASVRRNAEYGLHVR 106
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAvRQSLGMCPQHNILFHhLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 107 -RSWadrlrrEVADLvglrngtsdAMEA-LETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRN 184
Cdd:TIGR01257 1032 gRSW------EEAQL---------EMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190
....*....|....*....|....*....|....*...
gi 909710455 185 TAVIENAVREAgDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:TIGR01257 1097 RRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAII 1133
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-207 |
4.76e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdvwrasaqrrlecrrrigmvfq 86
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET---------------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 easlfdasvrrnaeyglhVRRSWADRLRrevadlvglrngtsDAMEALETV------GLE-------------------- 140
Cdd:PRK11819 387 ------------------VKLAYVDQSR--------------DALDPNKTVweeisgGLDiikvgnreipsrayvgrfnf 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 141 ---DKlEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AG------------DRgigvaI 204
Cdd:PRK11819 435 kggDQ-QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEfPGcavvishdrwflDR-----I 508
|
...
gi 909710455 205 ATH 207
Cdd:PRK11819 509 ATH 511
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-251 |
5.34e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGS-------LEYGGTDvWRAsaqrrlecrRRIGMVFQEAS- 89
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGElliddhpLHFGDYS-YRS---------QRIRMIFQDPSt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 ----------LFDASVRRNAEYglhvrrSWADRLRRevadlvglrngtsdAMEALETVGLedkLEQHAG----SLSGGEA 155
Cdd:PRK15112 99 slnprqrisqILDFPLRLNTDL------EPEQREKQ--------------IIETLRQVGL---LPDHASyyphMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDR-GIGVAIATHDMNQARRIADQVAVILGDGIIEVGETD 234
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTA 235
|
250
....*....|....*..
gi 909710455 235 RIFEDPEDDRTQQFIDG 251
Cdd:PRK15112 236 DVLASPLHELTKRLIAG 252
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-205 |
3.48e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.75 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIGMVFQEASLFD 92
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQGVAMVQQDPVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEYGLHVR--RSWADRLRREVADLVglrNGTSDamealetvGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDF 170
Cdd:PRK10790 429 DTFLANVTLGRDISeeQVWQALETVQLAELA---RSLPD--------GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190
....*....|....*....|....*....|....*
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIA 205
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-231 |
4.21e-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: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 5 TVGVEhgygDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFE--PPRDGSLEYGGTDVWRASAQRRleCRRRIG 82
Cdd:COG0396 7 HVSVE----GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDER--ARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQeaslfdasvrrnaeY-----GLHVR---RSWADRLRREVADLVGLRNgtsDAMEALETVGL-EDKLEQHA-GSLSG 152
Cdd:COG0396 81 LAFQ--------------YpveipGVSVSnflRTALNARRGEELSAREFLK---LLKEKMKELGLdEDFLDRYVnEGFSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 153 GEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHdmNQarRI-----ADQVAVILGDGI 227
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH--YQ--RIldyikPDFVHVLVDGRI 219
|
....
gi 909710455 228 IEVG 231
Cdd:COG0396 220 VKSG 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-181 |
4.71e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.16 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 7 GVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEyggtdvWRASAQrrlecrrrIGMVFQ 86
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------WSENAN--------IGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 --------EASLFDasvrrnaeyglhvrrsWADRLRREVADLVGLRnGTSDAMeaLETvglEDKLEQHAGSLSGGEAQRV 158
Cdd:PRK15064 390 dhaydfenDLTLFD----------------WMSQWRQEGDDEQAVR-GTLGRL--LFS---QDDIKKSVKVLSGGEKGRM 447
|
170 180
....*....|....*....|...
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLD 181
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-229 |
4.86e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.43 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLR-LLALFEpprdgsLEYGgtDVWRAsaqrrlecrRRIGMVFQEASLFDASV 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFE------ISEG--RVWAE---------RSIAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 96 RRNAeygLHVRRSWADRLrrevADLVglRNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDE 175
Cdd:PTZ00243 738 RGNI---LFFDEEDAARL----ADAV--RVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 909710455 176 PTSDLDPRntaVIENAVRE---AGDRGIGVAIATHDMNQARRiADQVaVILGDGIIE 229
Cdd:PTZ00243 809 PLSALDAH---VGERVVEEcflGALAGKTRVLATHQVHVVPR-ADYV-VALGDGRVE 860
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-226 |
5.24e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRrrIGMVFQEASLF-DASVR 96
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG--VAIIYQELHLVpEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYG-LHVRRSWADR--LRREvadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLL 173
Cdd:PRK11288 98 ENLYLGqLPHKGGIVNRrlLNYE-------------AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 909710455 174 DEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAViLGDG 226
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITV-FKDG 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-194 |
5.25e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 71.29 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRrleCRRRIGMVFQEASLFDASVR 96
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNaeygLHVRRSWADRlrrevadlvglrngtsDAMEALetvgledKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEP 176
Cdd:cd03369 100 SN----LDPFDEYSDE----------------EIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170
....*....|....*...
gi 909710455 177 TSDLDPRNTAVIENAVRE 194
Cdd:cd03369 153 TASIDYATDALIQKTIRE 170
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-237 |
7.41e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRlecrrrIGMVFQEASL---FD 92
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL------VAYVPQSEEVdwsFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEYGLHVRRSWADRLRREVADLVGlrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGWLRRAKKRDRQIVT---------AALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 173 LDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDgIIEVGETDRIF 237
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGT-VLASGPTETTF 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-196 |
8.10e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.88 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGsleyggtdvwrasaqrrlecrrRIGMVFQEASLF-- 91
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG----------------------RIGMPEGEDLLFlp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 ------DASVRRnaeyglHVRRSWADRLrrevadlvglrngtsdamealetvgledkleqhagslSGGEAQRVAFARALA 165
Cdd:cd03223 71 qrpylpLGTLRE------QLIYPWDDVL-------------------------------------SGGEQQRLAFARLLL 107
|
170 180 190
....*....|....*....|....*....|.
gi 909710455 166 YDPDFLLLDEPTSDLDPRNTAVIENAVREAG 196
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELG 138
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-247 |
1.12e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSL----EYGGTDV----WRAsaqrrlecrrRIGMVF 85
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindSHNLKDInlkwWRS----------KIGVVS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 QEASLFDASVRRNAEYGLHVRR--------------------SWADRLRREVADLVGLRNGTSDAMEALE---------- 135
Cdd:PTZ00265 467 QDPLLFSNSIKNNIKYSLYSLKdlealsnyynedgndsqenkNKRNSCRAKCAGDLNDMSNTTDSNELIEmrknyqtikd 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 136 ---------------TVGLEDKLEQHAGS----LSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVR--E 194
Cdd:PTZ00265 547 sevvdvskkvlihdfVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlK 626
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 909710455 195 AGDRGIGVAIAtHDMNQArRIADQVAVILGDGIIEVGETDRIFEDPEDDRTQQ 247
Cdd:PTZ00265 627 GNENRITIIIA-HRLSTI-RYANTIFVLSNRERGSTVDVDIIGEDPTKDNKEN 677
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-224 |
3.27e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 70.13 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 28 GEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrASAQRRLECRrrigmvfqeaslFDASVRrnaeyglhvrr 107
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV--SYKPQYIKAD------------YEGTVR----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 108 swaDRLRREVADLVGLRNGTSDAMEALetvGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAV 187
Cdd:cd03237 80 ---DLLSSITKDFYTHPYFKTEIAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 909710455 188 IENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILG 224
Cdd:cd03237 154 ASKVIRRfAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-240 |
3.52e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRL-ECRRRIGMVFQEASLFD 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQLdSWRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEYGLhvrrswADRLRREVADLVGLRNGTSDAMEALEtvGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:PRK10789 403 DTVANNIALGR------PDATQQEIEHVARLASVHDDILRLPQ--GYDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 173 LDEPTSDLDPRNTAVIENAVREAGdRGIGVAIATHDMNqARRIADQVAVILGDGIIEVGETDRIFEDP 240
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-226 |
4.18e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVW----RASAQRRlecr 78
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEAG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 79 rrIGMVFQEASLFDA-SVRRNAEYGLHVRRSWA----DRLRREVADLvglrngtsdameaLETVGLEDKLEQHAGSLSGG 153
Cdd:PRK10762 81 --IGIIHQELNLIPQlTIAENIFLGREFVNRFGridwKKMYAEADKL-------------LARLNLRFSSDKLVGELSIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 909710455 154 EAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAViLGDG 226
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTV-FRDG 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-207 |
6.64e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVW--RASAQRRLeCrrr 80
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdLCTYQKQL-C--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 igMVFQEASLF-DASVRRNAEYGLHVrrswadrlrrevadlvglrngTSDAMEALETV---GLEDKLEQHAGSLSGGEAQ 156
Cdd:PRK13540 78 --FVGHRSGINpYLTLRENCLYDIHF---------------------SPGAVGITELCrlfSLEHLIDYPCGLLSSGQKR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 909710455 157 RVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATH 207
Cdd:PRK13540 135 QVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-226 |
6.65e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLEcrRRIGMVFQEASLF-DASVR 96
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE--NGISMVHQELNLVlQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLHVRRSWadrlrreVADLVGLRNGTSDAMEALET-VGLEDKLeqhaGSLSGGEAQRVAFARALAYDPDFLLLDE 175
Cdd:PRK10982 92 DNMWLGRYPTKGM-------FVDQDKMYRDTKAIFDELDIdIDPRAKV----ATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 909710455 176 PTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDG 226
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEI-TILRDG 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-214 |
1.03e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrasAQRRLECRRRIGMVFQEASLF 91
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIATRRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 -DASVRRNAEygLHVR--RSWADRLRREVAdlvglrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:NF033858 352 gELTVRQNLE--LHARlfHLPAAEIAARVA-------------EMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 909710455 169 DFLLLDEPTSDLDP--RN---TAVIENAvREagdRGIGVAIATHDMNQARR 214
Cdd:NF033858 417 ELLILDEPTSGVDPvaRDmfwRLLIELS-RE---DGVTIFISTHFMNEAER 463
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
13-231 |
1.29e-13 |
|
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: 68.06 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPR--DGSLEYGGTDVWRASAQRRleCRRRIGMVFQ---- 86
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQDLLELEPDER--ARAGLFLAFQypee 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 ----EASLFDASVRrNAeyglhVRRSWADrlrrEVADLVGLRNGTSDAMEALETVGLEDKLEQHAGsLSGGEAQRVAFAR 162
Cdd:TIGR01978 89 ipgvSNLEFLRSAL-NA-----RRSARGE----EPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEG-FSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 163 ALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIA-DQVAVILGDGIIEVG 231
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSG 227
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-181 |
1.48e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 11 GYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGgTDVWRAsaqrRLE---CRRRIGMVFQE 87
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVA----RLQqdpPRNVEGTVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 ASlfdASVRRNAEY-------GLHVRRSWADRLRREVADLVGL---RNG---TSDAMEALETVGLEDklEQHAGSLSGGE 154
Cdd:PRK11147 87 VA---EGIEEQAEYlkryhdiSHLVETDPSEKNLNELAKLQEQldhHNLwqlENRINEVLAQLGLDP--DAALSSLSGGW 161
|
170 180
....*....|....*....|....*..
gi 909710455 155 AQRVAFARALAYDPDFLLLDEPTSDLD 181
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-246 |
1.75e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKT-TLLRLLALfepprdgsLEYGGTDVwrasAQRRLECRRRIGMVFQEASLFDASVR 96
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRL--------LEQAGGLV----QCDKMLLRRRSRQVIELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 --RNAEYGLHVRRSWAD-----RLRREVADLVGLRNGTS------DAMEALETVGLEDK---LEQHAGSLSGGEAQRVAF 160
Cdd:PRK10261 100 hvRGADMAMIFQEPMTSlnpvfTVGEQIAESIRLHQGASreeamvEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 161 ARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE-AGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFED 239
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVlQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
....*..
gi 909710455 240 PEDDRTQ 246
Cdd:PRK10261 260 PQHPYTR 266
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-252 |
2.14e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.67 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 78 RRRIGMVFQEASLFDASVRRNAEYGlhvrrswadrlrREVADLVGLRNGTSDAM--EALETvgLEDKLEQHAG----SLS 151
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENIKFG------------KEDATREDVKRACKFAAidEFIES--LPNKYDTNVGpygkSLS 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 152 GGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRgigvaiathdmnqarriADQVAVILGDGIIEVG 231
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK-----------------ADKTIITIAHRIASIK 1423
|
170 180
....*....|....*....|...
gi 909710455 232 ETDRI--FEDPedDRTQQFIDGE 252
Cdd:PTZ00265 1424 RSDKIvvFNNP--DRTGSFVQAH 1444
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-183 |
2.59e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 69.06 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGYGDET-----ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLE 76
Cdd:COG4615 327 TLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 77 CRRRIGMVFQEASLFDasvrrnaeyglhvrrswadrlrrevaDLVGLRNGTSD--AMEALETVGLEDKLEQHAG-----S 149
Cdd:COG4615 404 YRQLFSAVFSDFHLFD--------------------------RLLGLDGEADParARELLERLELDHKVSVEDGrfsttD 457
|
170 180 190
....*....|....*....|....*....|....
gi 909710455 150 LSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPR 183
Cdd:COG4615 458 LSQGQRKRLALLVALLEDRPILVFDEWAADQDPE 491
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-195 |
2.82e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwrASAQRRlECRRRIGMVFQEASLFDASVR 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--GAYGLR-ELRRQFSMIPQDPVLFDGTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLHVRRS--WAdrlrreVADLVGLRNGTsdameALETVGLEDKLEQHAGSLSGGEAQRVAFARA-LAYDPDFLLL 173
Cdd:PTZ00243 1402 QNVDPFLEASSAevWA------ALELVGLRERV-----ASESEGIDSRVLEGGSNYSVGQRQLMCMARAlLKKGSGFILM 1470
|
170 180
....*....|....*....|..
gi 909710455 174 DEPTSDLDPRNTAVIENAVREA 195
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSA 1492
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-250 |
3.15e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.01 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPR-----DgSLEYGGTDVWRASA-QRRLECRRRIGMVFQEA-S 89
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtaD-RFRWNGIDLLKLSPrERRKIIGREIAMIFQEPsS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 LFDASVR---------RNAEYGLHVRRSWADRLRREVADL--VGLRNGtsdamealetvglEDKLEQHAGSLSGGEAQRV 158
Cdd:COG4170 101 CLDPSAKigdqlieaiPSWTFKGKWWQRFKWRKKRAIELLhrVGIKDH-------------KDIMNSYPHELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVI------ENAVreagdRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGE 232
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIfrllarLNQL-----QGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
250
....*....|....*...
gi 909710455 233 TDRIFEDPEDDRTQQFID 250
Cdd:COG4170 243 TEQILKSPHHPYTKALLR 260
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-199 |
3.61e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfEPPRDGSLEYGGtdvwRASAQRRLEC--RRRIGMVFQ---- 86
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGD----RLVNGRPLDSsfQRSIGYVQQqdlh 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 87 -------EASLFDASVRRNAeyglHVRRSWADRLRREVADLVGLRNgTSDAMEALETVGLedKLEQHagslsggeaQRVA 159
Cdd:TIGR00956 848 lptstvrESLRFSAYLRQPK----SVSKSEKMEYVEEVIKLLEMES-YADAVVGVPGEGL--NVEQR---------KRLT 911
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 909710455 160 FARALAYDPDFLL-LDEPTSDLDPRNTAVIENAVREAGDRG 199
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHG 952
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-209 |
4.28e-13 |
|
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: 68.27 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPG-----EVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEyggTDVwrasaqrrlecrrRIGMVFQEASlfd 92
Cdd:COG1245 351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDL-------------KISYKPQYIS--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 asvrrnAEYGLHVRrswaDRLRREVADLVGlrnGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:COG1245 412 ------PDYDGTVE----EFLRSANTDDFG---SSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 909710455 173 LDEPTSDLD--PRNTA--VIENAVREagdRGIGVAIATHDM 209
Cdd:COG1245 479 LDEPSAHLDveQRLAVakAIRRFAEN---RGKTAMVVDHDI 516
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-222 |
5.13e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.89 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEP--PRDGSLEYGGtDVWRASAQRRLEcRRRIGMVFQEASLF-DAS 94
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDG-EVCRFKDIRDSE-ALGIVIIHQELALIpYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 95 VRRN-------AEYGLhvrRSWADRLRRevadlvglrngtsdAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYD 167
Cdd:NF040905 95 IAENiflgnerAKRGV---IDWNETNRR--------------ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVL 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-181 |
1.36e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPG-----EVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEyggTDVwrasaqrrlecrrRIGMVFQEASL-F 91
Cdd:PRK13409 350 LGDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PEL-------------KISYKPQYIKPdY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 92 DASVRrnaeyglhvrrswaDRLRREVADLvglrngtSDAM---EALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDP 168
Cdd:PRK13409 414 DGTVE--------------DLLRSITDDL-------GSSYyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170
....*....|...
gi 909710455 169 DFLLLDEPTSDLD 181
Cdd:PRK13409 473 DLYLLDEPSAHLD 485
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-184 |
1.76e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.58 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRL------------LALFEPPRdGSleygGTDVWrasaqrrlECRR 79
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLFGRRR-GS----GETIW--------DIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 80 RIGMVFQEASL---FDASVRRNAEYGLHvrrswadrlrrevaDLVGLRNGTSD-----AMEALETVGLEDKLEQHA-GSL 150
Cdd:PRK10938 337 HIGYVSSSLHLdyrVSTSVRNVILSGFF--------------DSIGIYQAVSDrqqklAQQWLDILGIDKRTADAPfHSL 402
|
170 180 190
....*....|....*....|....*....|....
gi 909710455 151 SGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRN 184
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-181 |
4.63e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGY------GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGsleygGTDVWRASaqrrle 76
Cdd:PLN03130 612 LPAISIKNGYfswdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-----ASVVIRGT------ 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 77 crrrIGMVFQEASLFDASVRRNAEYGLHVRrswADRLRREVaDLVGLRNGtsdameaLETVGLEDKLE--QHAGSLSGGE 154
Cdd:PLN03130 681 ----VAYVPQVSWIFNATVRDNILFGSPFD---PERYERAI-DVTALQHD-------LDLLPGGDLTEigERGVNISGGQ 745
|
170 180
....*....|....*....|....*..
gi 909710455 155 AQRVAFARALAYDPDFLLLDEPTSDLD 181
Cdd:PLN03130 746 KQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-249 |
5.79e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfepprdgsleyGGT-DVWRASAQR---------RLECRRR------- 80
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAIC------------GVTkDNWRVTADRmrfddidllRLSPRERrklvghn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQE-ASLFDASVRRNAEY-----GLHVRRSWADRL----RRevadlvglrngtsdAMEALETVGLEDK---LEQHA 147
Cdd:PRK15093 91 VSMIFQEpQSCLDPSERVGRQLmqnipGWTYKGRWWQRFgwrkRR--------------AIELLHRVGIKDHkdaMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 148 GSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAV-REAGDRGIGVAIATHDMNQARRIADQVAVILGDG 226
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260
....*....|....*....|...
gi 909710455 227 IIEVGETDRIFEDPEDDRTQQFI 249
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYTQALI 259
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-210 |
9.66e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIGMVFQEASLFDASVR 96
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLT---DLRRVLSIIPQSPVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAE-YGLHVRRS-WADRLRREVADLVGlRNgtsdamealeTVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLD 174
Cdd:PLN03232 1328 FNIDpFSEHNDADlWEALERAHIKDVID-RN----------PFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190
....*....|....*....|....*....|....*.
gi 909710455 175 EPTSDLDPRNTAVIENAVREAGdRGIGVAIATHDMN 210
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEF-KSCTMLVIAHRLN 1431
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-207 |
1.40e-11 |
|
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: 61.49 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEppRDGSLEyggTDVWRASAQRRLECRRRIGMVFQEASLFD 92
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVIT---GEILINGRPLDKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 -ASVRRNAEYGlhvrrswadrlrrevADLVGLrngtsdamealetvGLEDKleqhagslsggeaQRVAFARALAYDPDFL 171
Cdd:cd03232 93 nLTVREALRFS---------------ALLRGL--------------SVEQR-------------KRLTIGVELAAKPSIL 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATH 207
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-196 |
1.56e-11 |
|
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: 64.00 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEV--------------VAIIGPSGVGKTTLLRLLALFEPPrdgsleYGGTdvwrasaqRRLECRRRIG 82
Cdd:TIGR00954 453 KFENIPLVTPNGDVlieslsfevpsgnnLLICGPNGCGKSSLFRILGELWPV------YGGR--------LTKPAKGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 MVFQEASLFDASVRRNAEYGLhvrrSWADRLRREVADlvglrngtSDAMEALETVGLEDKLEQHAG---------SLSGG 153
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIYPD----SSEDMKRRGLSD--------KDLEQILDNVQLTHILEREGGwsavqdwmdVLSGG 586
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 909710455 154 EAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAG 196
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFG 629
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
14-206 |
1.59e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQeaslfDA 93
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKA-----DL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRNAEY--GLHVRRswADRLRREVADLVGLrngtsdamealetVGLEDKLEQHagsLSGGEAQRVAFARALAYDPDFL 171
Cdd:PRK13543 98 STLENLHFlcGLHGRR--AKQMPGSALAIVGL-------------AGYEDTLVRQ---LSAGQKKRLALARLWLSPAPLW 159
|
170 180 190
....*....|....*....|....*....|....*
gi 909710455 172 LLDEPTSDLDPRNTAVIeNAVREAGDRGIGVAIAT 206
Cdd:PRK13543 160 LLDEPYANLDLEGITLV-NRMISAHLRGGGAALVT 193
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-181 |
2.01e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfepPRDGSLEYGGTdVWRASAQRRLECRRRIGMVFQEASLF-D 92
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA----GRIQGNNFTGT-ILANNRKPTKQILKRTGFVTQDDILYpH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEYG--LHVRRSWADRLRREVADLVglrngtsdameaLETVGLEDKLEQHAGS-----LSGGEAQRVAFARALA 165
Cdd:PLN03211 155 LTVRETLVFCslLRLPKSLTKQEKILVAESV------------ISELGLTKCENTIIGNsfirgISGGERKRVSIAHEML 222
|
170
....*....|....*.
gi 909710455 166 YDPDFLLLDEPTSDLD 181
Cdd:PLN03211 223 INPSLLILDEPTSGLD 238
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
9-207 |
1.70e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 9 EHGYGDE--TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfepprdgSLEYGG---TDVWRASAQRRLECRRRIG- 82
Cdd:PLN03140 885 EQGVTEDrlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--------GRKTGGyieGDIRISGFPKKQETFARISg 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 83 -----------MVFQEASLFDASVRRNAEYGLHVRRSWADrlrrEVADLVGLRNgTSDAMEALETVGledkleqhagSLS 151
Cdd:PLN03140 957 yceqndihspqVTVRESLIYSAFLRLPKEVSKEEKMMFVD----EVMELVELDN-LKDAIVGLPGVT----------GLS 1021
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 152 GGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATH 207
Cdd:PLN03140 1022 TEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-229 |
1.84e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLR-LLALFEPPRDGSLEYGGTdvwrasaqrrlecrrrIGMVFQEASLFDASVR 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS----------------VAYVPQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYG--LHVRRSWadrlrrEVADLVGLRNGtsdameaLETVGLEDKLE--QHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:PLN03232 697 ENILFGsdFESERYW------RAIDVTALQHD-------LDLLPGRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 173 LDEPTSDLDPRNTAVIENAVREAGDRGIGVAIAT---HDMNQARRIadqvaVILGDGIIE 229
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLMDRI-----ILVSEGMIK 818
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-182 |
1.99e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 2 TLQTVGVEHGYGDETI-LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRR 80
Cdd:PRK10522 322 TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 81 IGMVFQEASLFDasvrrnaeyglhvrrswadrlrrevaDLVGLRNGTSDAMEA---LETVGLEDKLEQHAG-----SLSG 152
Cdd:PRK10522 399 FSAVFTDFHLFD--------------------------QLLGPEGKPANPALVekwLERLKMAHKLELEDGrisnlKLSK 452
|
170 180 190
....*....|....*....|....*....|
gi 909710455 153 GEAQRVAFARALAYDPDFLLLDEPTSDLDP 182
Cdd:PRK10522 453 GQKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-223 |
2.64e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.41 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfeppRDGSLEYGGTDVWRASAQRRL-ECRRRIGMVFQEASLFDASVR 96
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT-----GDTTVTSGDATVAGKSILTNIsDVHQNMGYCPQFDAIDDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYgLHVRrswadrlrrevadlvgLRNGTSDAME-----ALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFL 171
Cdd:TIGR01257 2030 REHLY-LYAR----------------LRGVPAEEIEkvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 909710455 172 LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVIL 223
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMV 2144
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-181 |
3.16e-10 |
|
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: 60.31 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGtdvwrasaqrrlecrrRIGMVFQEASLFDASVR 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLhvrrSWADRLRREVADLVGLRNGTSDAMEALETVGLEDKLeqhagSLSGGEAQRVAFARALAYDPDFLLLDEP 176
Cdd:TIGR01271 505 DNIIFGL----SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGI-----TLSGGQRARISLARAVYKDADLYLLDSP 575
|
....*
gi 909710455 177 TSDLD 181
Cdd:TIGR01271 576 FTHLD 580
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-231 |
7.29e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdvwrasaqrrlecrrrIGMVFQEASLFD 92
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------------VAYVPQQAWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEYGLHVRRSWADRLRREVADLVGLrngtsdamEALETvGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:TIGR00957 713 DSLRENILFGKALNEKYYQQVLEACALLPDL--------EILPS-GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 173 LDEPTSDLDPR-NTAVIENAVREAGD-RGIGVAIATHDMNQARRIaDQVAVILGDGIIEVG 231
Cdd:TIGR00957 784 FDDPLSAVDAHvGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-181 |
8.54e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLECRRRigmvfQE 87
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRA-----DE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 ASLfdasvrrnaeygLHVRRSWADRLRREVADLVGlrngtsdamealeTVGLE-DKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:PRK10636 393 SPL------------QHLARLAPQELEQKLRDYLG-------------GFGFQgDKVTEETRRFSGGEKARLVLALIVWQ 447
|
170
....*....|....*
gi 909710455 167 DPDFLLLDEPTSDLD 181
Cdd:PRK10636 448 RPNLLLLDEPTNHLD 462
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-181 |
1.01e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLL--ALfePPRDGSLEYGGTDVWRASAQRRL--------ECRRRIGMVFqe 87
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLygAL--PRTSGYVTLDGHEVVTRSPQDGLangivyisEDRKRDGLVL-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 aslfDASVRRN---------AEYGLHVRRswaDRLRREVADLVGLRNGTSDAMEaletvgledkleQHAGSLSGGEAQRV 158
Cdd:PRK10762 344 ----GMSVKENmsltalryfSRAGGSLKH---ADEQQAVSDFIRLFNIKTPSME------------QAIGLLSGGNQQKV 404
|
170 180
....*....|....*....|...
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLD 181
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-181 |
1.49e-09 |
|
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: 57.17 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGtdvwrasaqrrlecrrRIGMVFQEASLFDASVR 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------------RISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLhvrrSWADRLRREVADLVGLRNGTSDAMEALETVGLEDKLeqhagSLSGGEAQRVAFARALAYDPDFLLLDEP 176
Cdd:cd03291 116 ENIIFGV----SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGI-----TLSGGQRARISLARAVYKDADLYLLDSP 186
|
....*
gi 909710455 177 TSDLD 181
Cdd:cd03291 187 FGYLD 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-235 |
1.55e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 19 ENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecrrRIGMVF------QEASLFD 92
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAI----RAGIMLcpedrkAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRN---------AEYGLHVRRSW----ADRLRREvadlvgLRNGTSDAmealetvgledklEQHAGSLSGGEAQRVA 159
Cdd:PRK11288 346 HSVADNinisarrhhLRAGCLINNRWeaenADRFIRS------LNIKTPSR-------------EQLIMNLSGGNQQKAI 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 160 FARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVaVILGDGIIeVGETDR 235
Cdd:PRK11288 407 LGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRI-VVMREGRI-AGELAR 480
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-221 |
1.70e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECRRRiGMVF-----QEA 88
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSPLDAVKK-GMAYitesrRDN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 89 SLF-DASVRRNaeygLHVRRSWADRLRREVADLVGLRNGTSDAMEALETVGLE-DKLEQHAGSLSGGEAQRVAFARALAY 166
Cdd:PRK09700 351 GFFpNFSIAQN----MAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 167 DPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAV 221
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-236 |
1.84e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 3 LQTVGVEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPrdgsleyGGTDVWRAS---AQRRlECRR 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPD-------AGRRPWRF*twcANRR-ALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 80 RIGMvfqeaslfdasvRRNAEYGLhvRRSWADRlrrEVADLVGL------RNGTSDAMEALETVGLEDKLEQHAGSLSGG 153
Cdd:NF000106 86 TIG*------------HRPVR*GR--RESFSGR---ENLYMIGR*ldlsrKDARARADELLERFSLTEAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 154 EAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGET 233
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
...
gi 909710455 234 DRI 236
Cdd:NF000106 229 DEL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-194 |
3.50e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRllALF---EPPRdGSLEYGGTDVWRASAqrrLECRRRIGMVFQEASLFDA 93
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLN--ALFrivELER-GRILIDGCDISKFGL---MDLRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 94 SVRRNAE-YGLHVRRSWADRLRREVADLVGLRNgtsdamealeTVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:PLN03130 1328 TVRFNLDpFNEHNDADLWESLERAHLKDVIRRN----------SLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180
....*....|....*....|..
gi 909710455 173 LDEPTSDLDPRNTAVIENAVRE 194
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIRE 1419
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-219 |
5.15e-09 |
|
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: 54.96 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLlrllalfepprdgsleygGTDVWRASAQRR-LE-----CRRRIGMVFQEA--- 88
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL------------------AFDTIYAEGQRRyVEslsayARQFLGQMDKPDvds 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 89 --------SLFDASVRRNAeyglhvrRSWADRLRrEVADLVGL---RNGTSDAMEALETVGLED-KLEQHAGSLSGGEAQ 156
Cdd:cd03270 73 ieglspaiAIDQKTTSRNP-------RSTVGTVT-EIYDYLRLlfaRVGIRERLGFLVDVGLGYlTLSRSAPTLSGGEAQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 157 RVAFARALAYDPDFLL--LDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDmNQARRIADQV 219
Cdd:cd03270 145 RIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-217 |
5.32e-09 |
|
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: 54.25 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRllalfepprdgsleyggtDVWRASAQRRLEcrrrigmvfqeaslfdaSVRR 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------EGLYASGKARLI-----------------SFLP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 98 NAEYGLHVRrswadrlrrevadlvglrngtSDAMEALETVGLED-KLEQHAGSLSGGEAQRVAFARALAYDPD--FLLLD 174
Cdd:cd03238 56 KFSRNKLIF---------------------IDQLQFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILD 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 909710455 175 EPTSDLDPRNTAVIENAVREAGDRGIGVAIATHD---MNQARRIAD 217
Cdd:cd03238 115 EPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNldvLSSADWIID 160
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-228 |
6.59e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 54.91 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTL----LRLLALFepprDGSLEYGGTDVWRASAQrrlECRRRIGMVFQEASLFD 92
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLH---TLRSRLSIILQDPILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEyglHVRRSWADRLRR--EVADLVGLRNGTSDAMEALETVGLEDkleqhagsLSGGEAQRVAFARALAYDPDF 170
Cdd:cd03288 109 GSIRFNLD---PECKCTDDRLWEalEIAQLKNMVKSLPGGLDAVVTEGGEN--------FSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAVREA-GDRGIgVAIAtHDMNQARRiADQVaVILGDGII 228
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAfADRTV-VTIA-HRVSTILD-ADLV-LVLSRGIL 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-225 |
1.35e-08 |
|
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: 55.34 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 17 ILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQrrlECRRRIGMVFQEASLFDASVR 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH---DLRFKITIIPQDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNaeygLHVRRSWADR---LRREVADLVGLRNGTSDamealetvGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLL 173
Cdd:TIGR00957 1378 MN----LDPFSQYSDEevwWALELAHLKTFVSALPD--------KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 909710455 174 DEPTSDLDPRNTAVIENAVREAGDRGIGVAIAtHDMNQarrIADQVAVILGD 225
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQFEDCTVLTIA-HRLNT---IMDYTRVIVLD 1493
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-181 |
1.93e-08 |
|
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: 53.10 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLrLLALFEPPR-DGSLEYGGTDVWRASAQ-RRLECRRRIGMVFQEASLFDASV 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL-LAILGEMQTlEGKVHWSNKNESEPSFEaTRSRNRYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 96 RRNAEYGlhvrrSWADRLR-REVADLVGLRNGTSdameaLETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLD 174
Cdd:cd03290 96 EENITFG-----SPFNKQRyKAVTDACSLQPDID-----LLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
....*..
gi 909710455 175 EPTSDLD 181
Cdd:cd03290 166 DPFSALD 172
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-240 |
1.98e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.96 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKT-TLLRLLALFEPPR--DGSLEYGGTDVWRASaQRRLECRR--RIGMVFQe 87
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLP-EKELNKLRaeQISMIFQ- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 aslfDASVRRNAEYglhvrrswadRLRREVADLVGLRNGTSDAMEALETVGLED---------KLEQHAGSLSGGEAQRV 158
Cdd:PRK09473 105 ----DPMTSLNPYM----------RVGEQLMEVLMLHKGMSKAEAFEESVRMLDavkmpearkRMKMYPHEFSGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 159 AFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAgDRGIGVAI--ATHDMNQARRIADQVAVILGDGIIEVGETDRI 236
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNEL-KREFNTAIimITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
....
gi 909710455 237 FEDP 240
Cdd:PRK09473 250 FYQP 253
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-231 |
3.00e-08 |
|
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: 51.61 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 27 PGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASAQRRLecrrrigmvfqeaslfdasvrrnaeyglhvr 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQL------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 107 rswadrlrrevadlvglrngtsdamealetvgLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTA 186
Cdd:smart00382 50 --------------------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 909710455 187 VIENAVREAGD------RGIGVAIATHDMNQARRIAdqvAVILGDGIIEVG 231
Cdd:smart00382 98 LLLLLEELRLLlllkseKNLTVILTTNDEKDLGPAL---LRRRFDRRIVLL 145
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
149-225 |
3.24e-08 |
|
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: 51.80 E-value: 3.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909710455 149 SLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVA-IATHDMNQARRIADQVAVILGD 225
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAlVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-181 |
5.45e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfepprdGSLEYGGTDVwrasaqrRLECRRRIGMV------F 85
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILG-------GDLEPSAGNV-------SLDPNERLGKLrqdqfaF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 QEASLFD-----------ASVRRNAEY---------GLHVrrswADrLRREVADLVGLrNGTSDAMEALETVGLEdkLEQ 145
Cdd:PRK15064 77 EEFTVLDtvimghtelweVKQERDRIYalpemseedGMKV----AD-LEVKFAEMDGY-TAEARAGELLLGVGIP--EEQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 909710455 146 HAGSLSG---GEAQRVAFARALAYDPDFLLLDEPTSDLD 181
Cdd:PRK15064 149 HYGLMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-181 |
5.97e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdvWRasaqrrlecrrrIGMVFQEASLFD 92
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN--WQ------------LAWVNQETPALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVrrnAEYGLHVRRSWAdRLRREVAD--------LVGLRNGTSDAMEA----------LETVGL-EDKLEQHAGSLSGG 153
Cdd:PRK10636 78 QPA---LEYVIDGDREYR-QLEAQLHDanerndghAIATIHGKLDAIDAwtirsraaslLHGLGFsNEQLERPVSDFSGG 153
|
170 180
....*....|....*....|....*...
gi 909710455 154 EAQRVAFARALAYDPDFLLLDEPTSDLD 181
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-181 |
6.48e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.49 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 9 EHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPR---DGSLEYGGTDVWRASAQrrleCRRRIGMVF 85
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK----YPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 QE----ASLfdaSVRRNAEYGLHVRrswADRLRREVadlvglrngtsdamealetvgledkleqhagslSGGEAQRVAFA 161
Cdd:cd03233 90 EEdvhfPTL---TVRETLDFALRCK---GNEFVRGI---------------------------------SGGERKRVSIA 130
|
170 180
....*....|....*....|
gi 909710455 162 RALAYDPDFLLLDEPTSDLD 181
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLD 150
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
14-219 |
1.20e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPR--DGSLEYGGTDVWRASAQRRleCRRRIGMVFQ-EASL 90
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDR--AGEGIFMAFQyPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 91 FDASVRRNAEYGLHVRRSWADrlrREVADLVGLRNGTSDAMEALETVglEDKLEQHAG-SLSGGEAQRVAFARALAYDPD 169
Cdd:PRK09580 91 PGVSNQFFLQTALNAVRSYRG---QEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVNvGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 909710455 170 FLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHdmnqARRIADQV 219
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH----YQRILDYI 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-208 |
1.96e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 30 VVAIIGPSGVGKTTLLR--LLALF-EPPRDGSLEYGGTDVWRASaqrrlECRRRIGMVFQEASLFDASVRRNAEYGLHVr 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalKYALTgELPPNSKGGAHDPKLIREG-----EVRAQVKLAFENANGKKYTITRSLAILENV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 107 rswadrlrrevadlVGLRNGTSDAMealetvgledkLEQHAGSLSGGE------AQRVAFARALAYDPDFLLLDEPTSDL 180
Cdd:cd03240 98 --------------IFCHQGESNWP-----------LLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNL 152
|
170 180 190
....*....|....*....|....*....|...
gi 909710455 181 DPRNtavIENAVREA-----GDRGIGVAIATHD 208
Cdd:cd03240 153 DEEN---IEESLAEIieerkSQKNFQLIVITHD 182
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
32-222 |
2.01e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 50.35 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 32 AIIGPSGVGKTTLLR--LLALF-EPPRDGSLEygGTDVWRASAqrrlECRRRIGMVFQeaslfdasvRRNAEYglHVRRS 108
Cdd:cd03279 32 LICGPTGAGKSTILDaiTYALYgKTPRYGRQE--NLRSVFAPG----EDTAEVSFTFQ---------LGGKKY--RVERS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 109 W---ADRLRRevadLVGLRNGTSDAMealetvgledkLEQHAGSLSGGEAQRVAFARALA----------YDPDFLLLDE 175
Cdd:cd03279 95 RgldYDQFTR----IVLLPQGEFDRF-----------LARPVSTLSGGETFLASLSLALAlsevlqnrggARLEALFIDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 909710455 176 PTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:cd03279 160 GFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
150-216 |
2.69e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 2.69e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 150 LSGGEAQRVAFARALA---YDPD-FLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIA 216
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELAD 148
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-209 |
3.16e-07 |
|
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: 49.92 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLrLLALFePPRDGSLEYGGTDVWRASAQRRLECRRRIGMVFQE---------- 87
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI-NDTLY-PALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSpigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 ---ASLFD------ASVRRNAEYG---LHVR---RSWADRLRREVADLVGLRNG---TSDAMEALETVGLED-KLEQHAG 148
Cdd:cd03271 89 atyTGVFDeirelfCEVCKGKRYNretLEVRykgKSIADVLDMTVEEALEFFENipkIARKLQTLCDVGLGYiKLGQPAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909710455 149 SLSGGEAQRVAFARAL---AYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDM 209
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-208 |
4.90e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.85 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 30 VVAIIGPSGVGKTTLLR--LLALFEPPRDGS------LEYGGT----DVWRASAQRRLECRRRIGMvFQEASLFDASVRR 97
Cdd:COG0419 25 LNLIVGPNGAGKSTILEaiRYALYGKARSRSklrsdlINVGSEeasvELEFEHGGKRYRIERRQGE-FAEFLEAKPSERK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 98 NA---EYGLHVRRSWADRLRREVADLVGLRNgTSDAMEALETVGLEDKLE-QHAGSLSGGEAQRVAFARALAydpdfLLL 173
Cdd:COG0419 104 EAlkrLLGLEIYEELKERLKELEEALESALE-ELAELQKLKQEILAQLSGlDPIETLSGGERLRLALADLLS-----LIL 177
|
170 180 190
....*....|....*....|....*....|....*
gi 909710455 174 DepTSDLDPRNTAVIENAVREAgdrgigvAIATHD 208
Cdd:COG0419 178 D--FGSLDEERLERLLDALEEL-------AIITHV 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-235 |
7.86e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 146 HAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI--- 222
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMsng 467
|
90
....*....|...
gi 909710455 223 LGDGIIEVGETDR 235
Cdd:PRK10982 468 LVAGIVDTKTTTQ 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-222 |
8.12e-07 |
|
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: 49.44 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLR-LLALFEPPRDGSLEYGGTDVWRASAQRRL--------ECRRRIGMVFQEA 88
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIragiamvpEDRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 89 slfdasVRRNAEygLHVRRSWADRLR-REVADLVGLRNGtsdaMEALETVGLEDKLEqhAGSLSGGEAQRVAFARALAYD 167
Cdd:TIGR02633 356 ------VGKNIT--LSVLKSFCFKMRiDAAAELQIIGSA----IQRLKVKTASPFLP--IGRLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 168 PDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-208 |
1.47e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 11 GY-GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAlfepprdGSLEYGGTDVWRaSAQRRLEcrrrigmVFQEAs 89
Cdd:PLN03073 517 GYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS-------GELQPSSGTVFR-SAKVRMA-------VFSQH- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 90 lfdasvrrnaeyglHVrrswaDRLRREVADLVGLrngtsdaMEALETVgLEDKLEQHAGS--------------LSGGEA 155
Cdd:PLN03073 581 --------------HV-----DGLDLSSNPLLYM-------MRCFPGV-PEQKLRAHLGSfgvtgnlalqpmytLSGGQK 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 909710455 156 QRVAFARALAYDPDFLLLDEPTSDLDPRNT-AVIENAVREAGdrgiGVAIATHD 208
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLDLDAVeALIQGLVLFQG----GVLMVSHD 683
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-239 |
1.88e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 22 SLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVWRASaqrrLEcrrrigmvfQEASLFDASVRRNAEY 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS----FE---------QLQKLVSDEWQRNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 102 GLHVRRSWADRLRREVadlvgLRNGTSDA---MEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTS 178
Cdd:PRK10938 90 MLSPGEDDTGRTTAEI-----IQDEVKDParcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 909710455 179 DLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFED 239
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-213 |
1.98e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTdvwrasaqrrlecrrrigmvfqeASLFDASVRR 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------------------AALIAISSGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 98 NAEY-GLhvrrswadrlrrEVADLVGLRNGTSDAM------EALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDF 170
Cdd:PRK13545 97 NGQLtGI------------ENIELKGLMMGLTKEKikeiipEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 909710455 171 LLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQAR 213
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVK 207
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-180 |
2.06e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 2.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 909710455 131 MEALETVGLED-KLEQHAGSLSGGEAQRVAFARAL---AYDPDFLLLDEPTSDL 180
Cdd:TIGR00630 810 LQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL 863
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
131-177 |
5.95e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 5.95e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 909710455 131 MEALETVGLED-KLEQHAGSLSGGEAQRVAFARALA--------YdpdflLLDEPT 177
Cdd:COG0178 807 LQTLQDVGLGYiKLGQPATTLSGGEAQRVKLASELSkrstgktlY-----ILDEPT 857
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-207 |
6.12e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 14 DETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLEYGGTDVwraSAQRRLECrrriGMVFQEASL-FD 92
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI---NNIAKPYC----TYIGHNLGLkLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 93 ASVRRNAEYglhvrrsWADrlrrevadlvgLRNGTSDAMEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLL 172
Cdd:PRK13541 85 MTVFENLKF-------WSE-----------IYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
170 180 190
....*....|....*....|....*....|....*
gi 909710455 173 LDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATH 207
Cdd:PRK13541 147 LDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-181 |
9.41e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 8 VEHGYGDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLeYGGTDVwrasaqrrlecrrrigmvfqE 87
Cdd:PRK11147 325 VNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKL--------------------E 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 88 ASLFDasvrrnaEYglhvrRSWADrLRREVADLVGlrNGTSDAMealetVG---------LEDKL------EQHAGSLSG 152
Cdd:PRK11147 384 VAYFD-------QH-----RAELD-PEKTVMDNLA--EGKQEVM-----VNgrprhvlgyLQDFLfhpkraMTPVKALSG 443
|
170 180
....*....|....*....|....*....
gi 909710455 153 GEAQRVAFARALAYDPDFLLLDEPTSDLD 181
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-252 |
9.45e-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: 46.54 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 134 LETVGLED-KLEQHAGSLSGGEAQRVAFARALA-------YdpdflLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIA 205
Cdd:TIGR00630 472 LIDVGLDYlSLSRAAGTLSGGEAQRIRLATQIGsgltgvlY-----VLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVV 546
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 909710455 206 THDmNQARRIADQV------AVILGDGIIEVGETDRIFEDPeDDRTQQFIDGE 252
Cdd:TIGR00630 547 EHD-EDTIRAADYVidigpgAGEHGGEVVASGTPEEILANP-DSLTGQYLSGR 597
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-181 |
1.25e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEP---PRDGSL-----EYGGTD------VWRASAQRRLECR 78
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQIlhveqEVVGDDttalqcVLNTDIERTQLLE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 79 RRIGMVFQEASLFDASVRRN---AEYGLHVRRSWADRLRREVADLVGLRNGTSDAMEALETVGLE---DKLEQHAGSLSG 152
Cdd:PLN03073 268 EEAQLVAQQRELEFETETGKgkgANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSftpEMQVKATKTFSG 347
|
170 180
....*....|....*....|....*....
gi 909710455 153 GEAQRVAFARALAYDPDFLLLDEPTSDLD 181
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-49 |
1.42e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 1.42e-05
10 20 30
....*....|....*....|....*....|....*..
gi 909710455 13 GDETILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLA 49
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA 54
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
144-222 |
2.78e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 2.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 144 EQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVI 222
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-237 |
5.31e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 143 LEQHAGSLSGGEAQRVAFARALAYDPDFL--LLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIATHDmnqarriaDQVa 220
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--------EQM- 540
|
90
....*....|....*..
gi 909710455 221 VILGDGIIEVGETDRIF 237
Cdd:PRK00635 541 ISLADRIIDIGPGAGIF 557
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-241 |
9.34e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 18 LENVSLAVPPGEVVAIIGPSGVGKTTLLRLLALFEPPRDGSLE-YGGTDVWRASAqrrlecrrriGMVFQEASLfdasvr 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrNGEVSVIAISA----------GLSGQLTGI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 97 RNAEYGLHVrrswADRLRREVADLVGlrngtsdamEALETVGLEDKLEQHAGSLSGGEAQRVAFARALAYDPDFLLLDEP 176
Cdd:PRK13546 104 ENIEFKMLC----MGFKRKEIKAMTP---------KIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909710455 177 TSDLDPRNTAVIENAVREAGDRGIGVAIATHDMNQARRIADQVAVILGDGIIEVGETDRIFEDPE 241
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
131-180 |
1.08e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 1.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 909710455 131 MEALETVGLED-KLEQHAGSLSGGEAQRVAFARALA--------YdpdflLLDEPTSDL 180
Cdd:PRK00349 811 LQTLVDVGLGYiKLGQPATTLSGGEAQRVKLAKELSkrstgktlY-----ILDEPTTGL 864
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-194 |
1.70e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 16 TILENVSLAVPPGEVVAIIGPSGVGKTTLLRLLAL----FEPPRDGSLEYGGTDvwrasaQRRLECRRRIGMVF------ 85
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGIT------PEEIKKHYRGDVVYnaetdv 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 86 -------QEASLFDASVRRNAEYGLHV-RRSWADRLRREVADLVGLRNgTSDAmealeTVGLEdkleqHAGSLSGGEAQR 157
Cdd:TIGR00956 149 hfphltvGETLDFAARCKTPQNRPDGVsREEYAKHIADVYMATYGLSH-TRNT-----KVGND-----FVRGVSGGERKR 217
|
170 180 190
....*....|....*....|....*....|....*..
gi 909710455 158 VAFARALAYDPDFLLLDEPTSDLDPRNTAVIENAVRE 194
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKT 254
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
144-181 |
1.83e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.83e-04
10 20 30
....*....|....*....|....*....|....*...
gi 909710455 144 EQHAGSLSGGEAQRVAFARALAYDPDFLLLDEPTSDLD 181
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
149-230 |
2.29e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 149 SLSGGE------AQRVAFARALAYDPDFLLLDEPTS--DLDPRNTA--VIENAVREAGDRGIGVAIATH-DMNQARRIAD 217
Cdd:PRK01156 801 SLSGGEktavafALRVAVAQFLNNDKSLLIMDEPTAflDEDRRTNLkdIIEYSLKDSSDIPQVIMISHHrELLSVADVAY 880
|
90
....*....|...
gi 909710455 218 QVAVILGDGIIEV 230
Cdd:PRK01156 881 EVKKSSGSSKVIP 893
|
|
| Dck |
COG1428 |
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]; |
26-56 |
5.12e-04 |
|
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
Pssm-ID: 441037 [Multi-domain] Cd Length: 205 Bit Score: 40.16 E-value: 5.12e-04
10 20 30
....*....|....*....|....*....|....*...
gi 909710455 26 PPGEVVAIIGPSGVGKTTLLRLLA-------LFEPPRD 56
Cdd:COG1428 1 MKPRYIAVEGNIGAGKTTLARLLAehlgaelLLEPVED 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-219 |
8.50e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909710455 131 MEALETVGLED-KLEQHAGSLSGGEAQRVAFARALAY---DPDFLLLDEPTSDLDPRNTAVIENAVREAGDRGIGVAIAT 206
Cdd:PRK00635 790 IHALCSLGLDYlPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIE 869
|
90
....*....|...
gi 909710455 207 HDMNQArRIADQV 219
Cdd:PRK00635 870 HNMHVV-KVADYV 881
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
25-48 |
2.00e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 38.47 E-value: 2.00e-03
10 20
....*....|....*....|....
gi 909710455 25 VPPGEVVAIIGPSGVGKTTLLRLL 48
Cdd:cd01882 36 EPPPLVVVVVGPPGVGKSTLIRSL 59
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
12-49 |
4.56e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.74 E-value: 4.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 909710455 12 YGDETILENVSLAV--PPGEVVAIIGPSGVGKTTLLRLLA 49
Cdd:cd00009 1 VGQEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIA 40
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-49 |
6.15e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 6.15e-03
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
138-186 |
6.57e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.90 E-value: 6.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909710455 138 GLEDKLEQHAGSLSGGEAQR---VAFARALAY----------DPDFLLLDEPTSDLDPRNTA 186
Cdd:pfam13558 21 GSEVETYRRSGGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIR 82
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
30-51 |
8.73e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 35.93 E-value: 8.73e-03
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
20-55 |
9.13e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 9.13e-03
10 20 30
....*....|....*....|....*....|....*..
gi 909710455 20 NVSLAVPPGEVVAIIGPSGVGKTTLL-RLLALFEPPR 55
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLdAIQTLLVPAK 50
|
|
| |
