|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-250 |
1.72e-92 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 272.25 E-value: 1.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQvSEQERLEYRRSVG 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLR-VRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:COG1126 81 MVFQQFNLFpHLTVLENVTLAPIkVKK-------------MSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
250
....*....|
gi 490326802 241 TDERTRKFIE 250
Cdd:COG1126 228 QHERTRAFLS 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-236 |
1.45e-83 |
|
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: 249.02 E-value: 1.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALF-----DAPDHGSIRYENEDVWQVSEqERLEY 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDV-DVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLFDASVRRNAEYGLRVRQSWidrLRHELSSIVGktngtgdaiEALDTVGL--REKANQDAASLSGGEA 155
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIK---LKEELDERVE---------EALRKAALwdEVKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRgIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKT 235
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 490326802 236 V 236
Cdd:cd03260 227 I 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-249 |
2.22e-77 |
|
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: 233.72 E-value: 2.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVG 82
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDA-SVRRNAEYGLRVRQSWIDRLRHELssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:COG1127 86 MLFQGGALFDSlTVFENVAFPLREHTDLSEAEIREL------------VLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRElRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
....*....
gi 490326802 241 tDERTRKFI 249
Cdd:COG1127 234 -DPWVRQFL 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-251 |
8.19e-71 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 217.60 E-value: 8.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLL----RLLALFD-APDHGSIRYENEDVWQvSEQERLEY 77
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMNDLIPgARVEGEILLDGEDIYD-PDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLFDASVRRNAEYGLRVRQswiDRLRHELSSIVgktngtgdaIEALDTVGL----REKANQDAASLSGG 153
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGLRLHG---IKSKSELDEIV---------EESLRKAALwdevKDRLKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 154 EAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRgIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDT 233
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPT 237
|
250
....*....|....*...
gi 490326802 234 KTVFDNPTDERTRKFIEG 251
Cdd:COG1117 238 EQIFTNPKDKRTEDYITG 255
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-248 |
3.38e-70 |
|
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: 215.44 E-value: 3.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDA-SVRRNAEYGLRVR----QSWIDRLrhelssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQR 157
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFPLREHtrlsEEEIREI----------------VLEKLEAVGLRGAEDLYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGdTKTV 236
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG-TPEE 223
|
250
....*....|..
gi 490326802 237 FDNPTDERTRKF 248
Cdd:cd03261 224 LRASDDPLVRQF 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-222 |
6.80e-70 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 213.91 E-value: 6.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvSEQERLEYRRSVG 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL---SAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDASVRRNAEYGLRVRQSWIDRLRhelssivgktngtgdAIEALDTVGLREKA-NQDAASLSGGEAQRVAFA 161
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDRER---------------ALELLERLGLPPDIlDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-240 |
1.01e-67 |
|
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: 208.73 E-value: 1.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvSEQERLEYRRSV 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQ--EASLFDASVRRNAEYGLR---VRQSWIDRLrhelssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:COG1122 78 GLVFQnpDDQLFAPTVEEDVAFGPEnlgLPREEIRER----------------VEEALELVGLEHLADRPPHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTV 236
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
....
gi 490326802 237 FDNP 240
Cdd:COG1122 222 FSDY 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-249 |
3.44e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 206.08 E-value: 3.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 9 HHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQEA 88
Cdd:COG1135 12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 89 SLFDA-SVRRNAEYGLRvrqswidrlrhelssIVGKtngTGDAIEA-----LDTVGLREKANQDAASLSGGEAQRVAFAR 162
Cdd:COG1135 92 NLLSSrTVAENVALPLE---------------IAGV---PKAEIRKrvaelLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAkNR--GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDI-NRelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
....*....
gi 490326802 241 TDERTRKFI 249
Cdd:COG1135 233 QSELTRRFL 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-250 |
4.09e-65 |
|
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: 210.92 E-value: 4.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAE-----PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEY 77
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQ--EASLFDA-SVRRNAEYGLRVRQSWIDRLRHELssivgktngtgdAIEALDTVGLREK-ANQDAASLSGG 153
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRmTVGDIIAEPLRLHGLLSRAERRER------------VAELLERVGLPPDlADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 154 EAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGD 232
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250
....*....|....*...
gi 490326802 233 TKTVFDNPTDERTRKFIE 250
Cdd:COG1123 489 TEEVFANPQHPYTRALLA 506
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-238 |
4.90e-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: 200.27 E-value: 4.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyRRSVG 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---ARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASL-FDASVRRNAEYGLRVRQSWIDRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRYPHLGLFGRPSAEDREAVE---------EALERTGLEHLADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTavIEdaVLE-----AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTV 236
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQ--LE--VLEllrrlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
..
gi 490326802 237 FD 238
Cdd:COG1120 226 LT 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-229 |
5.65e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 199.11 E-value: 5.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYG----AEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR 78
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 R-SVGMVFQEASLFDA-SVRRNAEYGLRVRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:COG1136 85 RrHIGFVFQFFNLLPElTALENVALPLLLAG-------------VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERiADRVaVLLGNGIIE 229
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVTHDPELAAR-ADRV-IRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-219 |
2.35e-63 |
|
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: 197.33 E-value: 2.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAE----PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR 78
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 R-SVGMVFQEASLF-DASVRRNAEYGLRVRQSwIDRLRHElssivgktngtgDAIEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:cd03255 81 RrHIGFVFQSFNLLpDLTALENVELPLLLAGV-PKKERRE------------RAEELLERVGLGDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMhQAERIADRV 219
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDP-ELAEYADRI 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-240 |
2.84e-63 |
|
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: 197.80 E-value: 2.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 13 GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQEASLFD 92
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 A-SVRRNAEYGLR---VRQSWIDRLRHELssivgktngtgdaieaLDTVGLREKANQDAASLSGGEAQRVAFARALAYEP 168
Cdd:cd03258 96 SrTVFENVALPLEiagVPKAEIEERVLEL----------------LELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 169 DILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-249 |
1.36e-62 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 199.94 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvseqERLE-YRRSV 81
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV------TGLPpEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLF-DASVRRNAEYGLRVRqswidRL-RHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:COG3842 80 GMVFQDYALFpHLTVAENVAFGLRMR-----GVpKAEIRARVA---------ELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRntaVIEDAVLEAKN----RGIGVVIATHDMHQAERIADRVAVlLGNGIIE-VGDTK 234
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAK---LREEMREELRRlqreLGITFIYVTHDQEEALALADRIAV-MNDGRIEqVGTPE 221
|
250
....*....|....*
gi 490326802 235 TVFDNPTDERTRKFI 249
Cdd:COG3842 222 EIYERPATRFVADFI 236
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-255 |
6.25e-62 |
|
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: 194.64 E-value: 6.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGA----EPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvSEQERLEYR 78
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQ--EASLfdasvrrNAeyglrvRQSwIDRLRHELSSIVGKTNGTGDAIEALDTVGLREK-ANQDAASLSGGEA 155
Cdd:COG1124 79 RRVQMVFQdpYASL-------HP------RHT-VDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKN-RGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTK 234
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250 260
....*....|....*....|.
gi 490326802 235 TVFDNPTDERTRKFIEGELIY 255
Cdd:COG1124 225 DLLAGPKHPYTRELLAASLAF 245
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-222 |
3.42e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 193.38 E-value: 3.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAE----PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqerleyr 78
Cdd:COG1116 8 LELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQEASLFD-ASVRRNAEYGLRVRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQR 157
Cdd:COG1116 80 PDRGVVFQEPALLPwLTVLDNVALGLELRG-------------VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-250 |
3.88e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.20 E-value: 3.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQvseqERLEYRRSVG 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDA-SVRRNAEYglrvrqswIDRLRHelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRF--------FARLYG-----LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVlLGNGiievgdtKTVFDNPT 241
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAI-IDKG-------RIVADGTP 215
|
....*....
gi 490326802 242 DERTRKFIE 250
Cdd:COG1131 216 DELKARLLE 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-255 |
6.50e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 189.50 E-value: 6.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSV 81
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLFD-ASVRRNAEYGLRVRQSWIDRLRHELSSIvgktngtgD---AIEALDTVGLREKANQDAASLSGGEAQR 157
Cdd:COG3638 83 GMIFQQFNLVPrLSVLTNVLAGRLGRTSTWRSLLGLFPPE--------DrerALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRvavllgngIIEVGDTKTV 236
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRiAREDGITVVVNLHQVDLARRYADR--------IIGLRDGRVV 226
|
250
....*....|....*....
gi 490326802 237 FDNPTDERTRKFIEGelIY 255
Cdd:COG3638 227 FDGPPAELTDAVLRE--IY 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-231 |
7.69e-60 |
|
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: 188.11 E-value: 7.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerleyRRSVG 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFD-ASVRRNAEYGLRVRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:cd03259 76 MVFQDYALFPhLTVAENIAFGLKLRG-------------VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVG 231
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-222 |
1.44e-59 |
|
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: 187.29 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAY--GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvSEQERLEYRRSVGMV 84
Cdd:cd03225 4 NLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL---TKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 85 FQ--EASLFDASVRRNAEYGLR---VRQSWIDRLrhelssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLEnlgLPEEEIEER----------------VEEALELVGLEGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-228 |
1.53e-57 |
|
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: 182.34 E-value: 1.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQvSEQERLEYRRSVG 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVRQSwidRLRHELSSIvgktngtgdAIEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLAPIKVKG---MSKAEAEER---------ALELLEKVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNGII 228
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRV-IFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-246 |
4.42e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 182.21 E-value: 4.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVseqerleyRRSVG 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--------RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASL---FDASVRRNAEYGLRVRQSWIDRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLMGRYGRRGLFRRPSRADREAVD---------EALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNGIIEVGDTKTVFDN 239
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEEVLTP 228
|
....*..
gi 490326802 240 PTDERTR 246
Cdd:COG1121 229 ENLSRAY 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-222 |
8.17e-57 |
|
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: 180.75 E-value: 8.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAE----PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqerleyr 78
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQEASLFD-ASVRRNAEYGLRVR-QSWIDRLRHelssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:cd03293 73 PDRGYVFQQDALLPwLTVLDNVALGLELQgVPKAEARER--------------AEELLELVGLSGFENAYPHQLSGGMRQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-253 |
3.42e-55 |
|
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: 177.36 E-value: 3.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYRRSVG 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----RKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDA-SVRRNAEYGLRVRQSWIDRLRHELSSIVGKtngtgdaiealdtVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIEL-------------LGLEEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNGiievgdtKTVFDNPT 241
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRV-VILHKG-------KVVAQGSL 216
|
250
....*....|..
gi 490326802 242 DERTRKFIEGEL 253
Cdd:COG4555 217 DELREEIGEENL 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-228 |
6.28e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 176.01 E-value: 6.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAE-PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSV 81
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASL-FDASVRRNAEYGLRVrqswIDRLRHELSSivgktngtgDAIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:COG2884 82 GVVFQDFRLlPDRTVYENVALPLRV----TGKSRKEIRR---------RVREVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNGII 228
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRV-LELEDGRL 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-231 |
2.94e-54 |
|
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: 174.62 E-value: 2.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY----GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR 78
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQEA--SLfdasvrrNAeyGLRVRQSWIDRLRHELSSIVGKTNGTGdAIEALDTVGLREK-ANQDAASLSGGEA 155
Cdd:cd03257 82 KEIQMVFQDPmsSL-------NP--RMTIGEQIAEPLRIHGKLSKKEARKEA-VLLLLVGVGLPEEvLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKN-RGIGVVIATHDMHQAERIADRVAVLLGNGIIEVG 231
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-222 |
3.91e-54 |
|
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: 174.55 E-value: 3.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleYRRSVG 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVRQS---WIDRLRHELSSIVGKtngtgdAIEALDTVGLREKANQDAASLSGGEAQRV 158
Cdd:cd03219 79 RTFQIPRLFpELTVLENVMVAAQARTGsglLLARARREEREARER------AEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-249 |
1.20e-53 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 176.49 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVW-QVSEQErleyrR 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 80 SVGMVFQEASLF-DASVRRNAEYGLRVR---QSWIDRLRHELssivgktngtgdaieaLDTVGLREKANQDAASLSGGEA 155
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFGLRVRppsKAEIRARVEEL----------------LELVQLEGLADRYPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDprnTAVIEDavLEA------KNRGIGVVIATHDMHQAERIADRVAVlLGNG-II 228
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALD---AKVRKE--LRRwlrrlhDELGGTTVFVTHDQEEALELADRVVV-MNQGrIE 213
|
250 260
....*....|....*....|.
gi 490326802 229 EVGDTKTVFDNPTDERTRKFI 249
Cdd:COG1118 214 QVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-222 |
7.04e-53 |
|
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: 169.29 E-value: 7.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwQVSEQERLEYRRSVG 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLrvrqswidrlrhelssivgktngtgdaiealdtvglrekanqdaaslSGGEAQRVAFA 161
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALGL-----------------------------------------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-249 |
7.78e-53 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 174.49 E-value: 7.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleyrRSV 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-----RNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLFDA-SVRRNAEYGLRVRqswiDRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:COG3839 78 AMVFQSYALYPHmTVYENIAFPLKLR----KVPKAEIDRRVR---------EAAELLGLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 161 ARALAYEPDILLLDEPTSDLDP--RNTAVIEDAVLEAKnRGIGVVIATHDMHQAERIADRVAVLLgNGIIE-VGDTKTVF 237
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAklRVEMRAEIKRLHRR-LGTTTIYVTHDQVEAMTLADRIAVMN-DGRIQqVGTPEELY 222
|
250
....*....|..
gi 490326802 238 DNPTDERTRKFI 249
Cdd:COG3839 223 DRPANLFVAGFI 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-228 |
2.11e-52 |
|
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: 169.25 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 4 EAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRyenedvwqVSEQERLEYRRSVGM 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR--------VFGKPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQEASL---FDASVRRNAEYGLRVRQSWIDRLRHELSSIVgktngtgdaIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKV---------DEALERVGLSELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNGII 228
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVV 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-253 |
1.38e-51 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 168.42 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFD--APD---HGSIRYENEDVWQvSEQERLEY 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIYS-PRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLFDASVRRNAEYGLRVRQSwidRLRHELSSIVGKTNgTGDAIeaLDTVglREKANQDAASLSGGEAQR 157
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVYGLRLKGI---KDKQVLDEAVEKSL-KGASI--WDEV--KDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRgIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
250
....*....|....*.
gi 490326802 238 DNPTDERTRKFIEGEL 253
Cdd:PRK14239 236 MNPKHKETEDYISGKF 251
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-231 |
2.77e-51 |
|
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: 165.30 E-value: 2.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyRRSVGMVFQ 86
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 easlfdasvrrnaeyglrvrqswidrlrhelssivgktngtgdaieALDTVGLREKANQDAASLSGGEAQRVAFARALAY 166
Cdd:cd03214 81 ----------------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 167 EPDILLLDEPTSDLDPRNtaviEDAVLE-----AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVG 231
Cdd:cd03214 115 EPPILLLDEPTSHLDIAH----QIELLEllrrlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-249 |
4.26e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 169.98 E-value: 4.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQEASLFDA-SVRR 97
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNLLSSrTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NAEYGLR---VRQSWIDRLRHELssivgktngtgdaieaLDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLD 174
Cdd:PRK11153 102 NVALPLElagTPKAEIKARVTEL----------------LELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 175 EPTSDLDPRNTAVIEDaVLEAKNR--GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERTRKFI 249
Cdd:PRK11153 166 EATSALDPATTRSILE-LLKDINRelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-250 |
5.74e-51 |
|
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: 166.59 E-value: 5.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAyGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSV 81
Cdd:cd03256 2 EVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLFD-ASVRRNAEYGLRVRQSWIDRLRHELSSIvgktnGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:cd03256 81 GMIFQQFNLIErLSVLENVLSGRLGRRSTWRSLFGLFPKE-----EKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRvavllgngIIEVGDTKTVFDN 239
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADR--------IVGLKDGRIVFDG 227
|
250
....*....|.
gi 490326802 240 PTDERTRKFIE 250
Cdd:cd03256 228 PPAELTDEVLD 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-228 |
7.96e-51 |
|
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: 163.72 E-value: 7.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQvseqERLEYRRSVG 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDasvrrnaeyGLRVRqswidrlrhelssivgktngtgdaiEALDtvglrekanqdaasLSGGEAQRVAFAR 162
Cdd:cd03230 77 YLPEEPSLYE---------NLTVR-------------------------ENLK--------------LSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVlLGNGII 228
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAI-LNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-244 |
2.51e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 164.80 E-value: 2.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDV---WQVSEQERLEY 77
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLF-DASVRRN-AEYGLRV----RQSWIDRlrhelssivgktngtgdAIEALDTVGLREKANQDAASLS 151
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENlIEAPCKVlglsKEQAREK-----------------AMKLLARLRLTDKADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVG 231
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
250
....*....|...
gi 490326802 232 DtKTVFDNPTDER 244
Cdd:COG4161 224 D-ASHFTQPQTEA 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-251 |
3.11e-50 |
|
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: 165.51 E-value: 3.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRR-SVGMVFQEASLF-DASVRRN 98
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQSFALLpHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 99 AEYGLRVRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTS 178
Cdd:cd03294 123 VAFGLEVQG-------------VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 179 DLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERTRKFIEG 251
Cdd:cd03294 190 ALDPLIRREMQDELLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-249 |
5.81e-50 |
|
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: 163.56 E-value: 5.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 8 VHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVseqerLEYRRSVGMVFQE 87
Cdd:cd03300 6 VSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 ASLF-DASVRRNAEYGLRVRQSWIDRLRHELSsivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAY 166
Cdd:cd03300 81 YALFpHLTVFENIAFGLRLKKLPKAEIKERVA-------------EALDLVQLEGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 167 EPDILLLDEPTSDLDPRntaVIEDAVLEAKN----RGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTD 242
Cdd:cd03300 148 EPKVLLLDEPLGALDLK---LRKDMQLELKRlqkeLGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
....*..
gi 490326802 243 ERTRKFI 249
Cdd:cd03300 225 RFVADFI 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-222 |
1.09e-49 |
|
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: 160.49 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 4 EAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqeRLEYRRSVGM 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQeaslfdasvrrnaeyglrvrqswidrlrhelssivgktngtgdaiealdtvglrekanqdaasLSGGEAQRVAFARA 163
Cdd:cd00267 78 VPQ---------------------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 164 LAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-250 |
1.35e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 162.95 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERlEYRRSVGMVFQ 86
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 EASLF-DASVRRNAEYG-LRVRQSwidrlrhelssivGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARAL 164
Cdd:PRK09493 85 QFYLFpHLTALENVMFGpLRVRGA-------------SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 165 AYEPDILLLDEPTSDLDP--RNTA--VIEDAVLEaknrGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPelRHEVlkVMQDLAEE----GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
250
....*....|
gi 490326802 241 TDERTRKFIE 250
Cdd:PRK09493 228 PSQRLQEFLQ 237
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
17-243 |
1.39e-49 |
|
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: 162.85 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQEASLFD-ASV 95
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRIGMIFQHYNLIErLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 96 RRNAEYGLRVRQSWIDRLRHELSSivgktNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDE 175
Cdd:TIGR02315 97 LENVLHGRLGYKPTWRSLLGRFSE-----EDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 176 PTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVaVLLGNGIIevgdtktVFDNPTDE 243
Cdd:TIGR02315 172 PIASLDPKTSKQVMDYLKRiNKEDGITVIINLHQVDLAKKYADRI-VGLKAGEI-------VFDGAPSE 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-240 |
2.23e-49 |
|
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: 164.84 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLR-LLALFDAP--DHGSIRYENEDVWQVSEQERLEYR-RSVGMVFQE--ASLfd 92
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKELRKIRgREIQMIFQDpmTSL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 asvrrNAEYglRVRQSWIDRLR-HElssIVGKTNGTGDAIEALDTVGLREkANQDAAS----LSGGEAQRVAFARALAYE 167
Cdd:COG0444 100 -----NPVM--TVGDQIAEPLRiHG---GLSKAEARERAIELLERVGLPD-PERRLDRypheLSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 168 PDILLLDEPTSDLDprntAVIEDAVLE-----AKNRGIGVVIATHDMHQAERIADRVAVL-LGNgIIEVGDTKTVFDNP 240
Cdd:COG0444 169 PKLLIADEPTTALD----VTIQAQILNllkdlQRELGLAILFITHDLGVVAEIADRVAVMyAGR-IVEEGPVEELFENP 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-253 |
3.24e-49 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 162.39 E-value: 3.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLR----LLALFDAPD-HGSIRYENEDVWQVseqERLEY 77
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKM---DVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEAS-LFDASVRRNAEYGLRVRQswIDRLRHELSSIVGktngtgdaiEALDTVGL----REKANQDAASLSG 152
Cdd:PRK14247 81 RRRVQMVFQIPNpIPNLSIFENVALGLKLNR--LVKSKKELQERVR---------WALEKAQLwdevKDRLDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 153 GEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGD 232
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
250 260
....*....|....*....|.
gi 490326802 233 TKTVFDNPTDERTRKFIEGEL 253
Cdd:PRK14247 229 TREVFTNPRHELTEKYVTGRL 249
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-240 |
7.65e-49 |
|
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: 168.16 E-value: 7.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY--GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLR-LLALFDAPDH--GSIRYENEDVWQVSEQERley 77
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGGRisGEVLLDGRDLLELSEALR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQE--ASLFDASVRRNAEYGLRVRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEA 155
Cdd:COG1123 82 GRRIGMVFQDpmTQLNPVTVGDQIAEALENLG-------------LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTK 234
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
....*.
gi 490326802 235 TVFDNP 240
Cdd:COG1123 229 EILAAP 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-231 |
1.49e-48 |
|
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: 170.01 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYG--AEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqeRLEYRRSVGMV 84
Cdd:COG2274 478 NVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 85 FQEASLFDASVRRNaeygLRVRQSWIDRlrhelssivgktngtGDAIEALDTVGLREKANQ-----------DAASLSGG 153
Cdd:COG2274 555 LQDVFLFSGTIREN----ITLGDPDATD---------------EEIIEAARLAGLHDFIEAlpmgydtvvgeGGSNLSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 154 EAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAvLEAKNRGIGVVIATHDMHQAeRIADRVAVLLGNGIIEVG 231
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDG 691
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-249 |
2.14e-48 |
|
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: 159.81 E-value: 2.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleyrRS 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLF-DASVRRNAEYGLRVRQSwidRLRHELSSIVGKTNgtgdaiEALDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:cd03296 76 VGFVFQHYALFrHMTVFDNVAFGLRVKPR---SERPPEAEIRAKVH------ELLKLVQLDWLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFD 238
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 490326802 239 NPTDERTRKFI 249
Cdd:cd03296 227 HPASPFVYSFL 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-222 |
5.39e-48 |
|
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: 156.39 E-value: 5.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerlEYRRS 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE---SLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNaeyglrvrqswIdrlrhelssivgktngtgdaiealdtvglrekanqdaasLSGGEAQRVAF 160
Cdd:cd03228 78 IAYVPQDPFLFSGTIREN-----------I---------------------------------------LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnRGIGVVIATHDMHQAERiADRVAVL 222
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRD-ADRIIVL 167
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-219 |
7.27e-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: 157.39 E-value: 7.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRS-VGMVFQEASL 90
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREkLGYLFQNFAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 91 FDA-SVRRNAEYGLrvrqswidrlrhELSSIVGKTNGTgDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPD 169
Cdd:TIGR03608 88 IENeTVEENLDLGL------------KYKKLSKKEKRE-KKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490326802 170 ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERiADRV 219
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRV 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-208 |
1.74e-47 |
|
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: 156.49 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYRRS 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDA-SVRRNAEYGLRVRQSWIDRLRHElssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLRFWAALYGLRADREAID---------------EALEAVGLAGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHD 208
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-232 |
2.03e-47 |
|
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: 165.32 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAY--GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyRR 79
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 80 SVGMVFQEASLFDASVRRNaeygLRvrqswidrlrhelssiVGKTNGT-GDAIEALDTVGLREKANQ-----------DA 147
Cdd:COG4987 410 RIAVVPQRPHLFDTTLREN----LR----------------LARPDATdEELWAALERVGLGDWLAAlpdgldtwlgeGG 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 148 ASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRgiGVVIATHDMHQAERiADRVAVLLGNG 226
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlAGR--TVLLITHRLAGLER-MDRILVLEDGR 546
|
....*.
gi 490326802 227 IIEVGD 232
Cdd:COG4987 547 IVEQGT 552
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-244 |
3.69e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 156.71 E-value: 3.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHG--SIRYENEDVWQ-VSEQERLEY 77
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKtPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLF-DASVRRN-AEYGLRVRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEA 155
Cdd:PRK11124 81 RRNVGMVFQQYNLWpHLTVQQNlIEAPCRVLG-------------LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNG-IIEVGDtK 234
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRV-VYMENGhIVEQGD-A 225
|
250
....*....|
gi 490326802 235 TVFDNPTDER 244
Cdd:PRK11124 226 SCFTQPQTEA 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-231 |
7.20e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 163.80 E-value: 7.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRSVGMVF 85
Cdd:COG1132 344 NVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLFDASVRRNAEYGL------RVRQ--------SWIDRLRHELSSIVGktngtgdaiealdtvglrekanQDAASLS 151
Cdd:COG1132 421 QDTFLFSGTIRENIRYGRpdatdeEVEEaakaaqahEFIEALPDGYDTVVG----------------------ERGVNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRgIGVVIAtHDMHQAeRIADRVAVLLGNGIIEV 230
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlMKGR-TTIVIA-HRLSTI-RNADRILVLDDGRIVEQ 555
|
.
gi 490326802 231 G 231
Cdd:COG1132 556 G 556
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-232 |
8.56e-47 |
|
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: 163.39 E-value: 8.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyRRS 80
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNaeyglrvrqswidrLRhelssiVGKTNGTGDAI-EALDTVGLREKANQ-----------DAA 148
Cdd:COG4988 413 IAWVPQNPYLFAGTIREN--------------LR------LGRPDASDEELeAALEAAGLDEFVAAlpdgldtplgeGGR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnRGIGVVIATHDMHQAERiADRVAVLLGNGII 228
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIV 550
|
....
gi 490326802 229 EVGD 232
Cdd:COG4988 551 EQGT 554
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-253 |
1.43e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 155.73 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDV---------WQVSEQ 72
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgeLVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 73 ERLEYRRS-VGMVFQEASLFDAsvrrnaeygLRVRQSWIDRLRHELSsiVGKTNGTGDAIEALDTVGLREKANQDAASLS 151
Cdd:COG4598 88 RQLQRIRTrLGMVFQSFNLWSH---------MTVLENVIEAPVHVLG--RPKAEAIERAEALLAKVGLADKRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTA----VIEDAVLEaknrGIGVVIATHDMHQAERIADRVaVLLGNGI 227
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGevlkVMRDLAEE----GRTMLVVTHEMGFARDVSSHV-VFLHQGR 231
|
250 260
....*....|....*....|....*..
gi 490326802 228 I-EVGDTKTVFDNPTDERTRKFIEGEL 253
Cdd:COG4598 232 IeEQGPPAEVFGNPKSERLRQFLSSSL 258
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-250 |
2.33e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.91 E-value: 2.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIR---YENEDVWQVSEQERL--EYRRSVGMVFQEASLF 91
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgdITIDTARSLSQQKGLirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 -DASVRRNAEYGlrvrqswidrlrhelsSIVGKTNGTGDAI----EALDTVGLREKANQDAASLSGGEAQRVAFARALAY 166
Cdd:PRK11264 98 pHRTVLENIIEG----------------PVIVKGEPKEEATararELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 167 EPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERTR 246
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTR 241
|
....
gi 490326802 247 KFIE 250
Cdd:PRK11264 242 QFLE 245
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-222 |
6.25e-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: 6.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleYRRSVG 82
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--ARLGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGL--RVRQSWIDRLRHELSSIVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:COG0411 83 RTFQNPRLFpELTVLENVLVAAhaRLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVVL 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-240 |
6.56e-46 |
|
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: 156.80 E-value: 6.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEaIDVHHAYGAepvFD-GVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYeNEDVWQVSEQE--RLEY 77
Cdd:COG4148 1 MMLE-VDFRLRRGG---FTlDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL-GGEVLQDSARGifLPPH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLFD-ASVRRNAEYGLRVRQSWIDRLRHElssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:COG4148 76 RRRIGYVFQEARLFPhLSVRGNLLYGRKRAPRAERRISFD---------------EVVELLGIGHLLDRRPATLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLD-PRNTAVIEdaVLE--AKNRGIGVVIATHDMHQAERIADRVaVLLGNG-IIEVGD 232
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDlARKAEILP--YLErlRDELDIPILYVSHSLDEVARLADHV-VLLEQGrVVASGP 217
|
....*...
gi 490326802 233 TKTVFDNP 240
Cdd:COG4148 218 LAEVLSRP 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-222 |
6.97e-46 |
|
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: 152.45 E-value: 6.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 25 VTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYeNEDVWQVSEQERL--EYRRSVGMVFQEASLF-DASVRRNAEY 101
Cdd:cd03297 20 DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFDSRKKINlpPQQRKIGLVFQQYALFpHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 102 GLRVRQSWIDRLRHElssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLD 181
Cdd:cd03297 99 GLKRKRNREDRISVD---------------ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490326802 182 pRNTAVIEDAVLE--AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03297 164 -RALRLQLLPELKqiKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-249 |
1.14e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 152.60 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPV-FDgvsLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqerlEYRRSV 81
Cdd:COG3840 2 LRLDDLTYRYGDFPLrFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-----PAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLFDA-SVRRNAEYGLRvrqswiDRLRheLSSIVGKtngtgDAIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:COG3840 74 SMLFQENNLFPHlTVAQNIGLGLR------PGLK--LTAEQRA-----QVEQALERVGLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDG 220
|
250
....*....|
gi 490326802 240 PTDERTRKFI 249
Cdd:COG3840 221 EPPPALAAYL 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-254 |
1.14e-45 |
|
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: 152.87 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerleyRRSVGMVFQEASLF-DASVRR 97
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFpHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NAEYGLRVR---QSWIDRLRHELSSIVGktngtgdaIEALdtvglrekANQDAASLSGGEAQRVAFARALAYEPDILLLD 174
Cdd:cd03299 91 NIAYGLKKRkvdKKEIERKVLEIAEMLG--------IDHL--------LNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 175 EPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERTRKFIEGEL 253
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
|
.
gi 490326802 254 I 254
Cdd:cd03299 235 I 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-253 |
2.78e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 152.30 E-value: 2.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLR----LLALF-DAPDHGSIRYENEDVWQvSEQERLEY 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNeEARVEGEVRLFGRNIYS-PDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLF-DASVRRNAEYGLRVRQswIDRLRHELSSIVGktngtgdaiEALDTVGL----REKANQDAASLSG 152
Cdd:PRK14267 84 RREVGMVFQYPNPFpHLTIYDNVAIGVKLNG--LVKSKKELDERVE---------WALKKAALwdevKDRLNDYPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 153 GEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRgIGVVIATHDMHQAERIADRVAVLLGNGIIEVGD 232
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
250 260
....*....|....*....|.
gi 490326802 233 TKTVFDNPTDERTRKFIEGEL 253
Cdd:PRK14267 232 TRKVFENPEHELTEKYVTGAL 252
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-222 |
5.42e-45 |
|
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: 150.48 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSV 81
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLF-DASVRRNAEYGLRVRQSWIDRLRHELSsivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:TIGR02673 82 GVVFQDFRLLpDRTVYENVALPLEVRGKKEREIQRRVG-------------AALRQVGLEHKADAFPEQLSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:TIGR02673 149 ARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIIL 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-222 |
8.69e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 151.08 E-value: 8.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRrs 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 vGMVFQEASL-FDASVRRNAEYGLRVRQswidRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:PRK13548 79 -AVLPQHSSLsFPFTVEEVVAMGRAPHG----LSRAEDDALVA---------AALAQVDLAHLAGRDYPQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 160 FARALA------YEPDILLLDEPTSDLDPRNtaviEDAVLE-----AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAH----QHHVLRlarqlAHERGLAVIVVLHDLNLAARYADRIVLL 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-241 |
1.12e-44 |
|
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: 151.45 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVF-----DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSV 81
Cdd:TIGR04521 5 NVSYIYQPGTPFekkalDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQ--EASLFDASVRRNAEYGLR---VRQSWIDRLrhelssivgktngtgdAIEALDTVGLREK-ANQDAASLSGGEA 155
Cdd:TIGR04521 85 GLVFQfpEHQLFEETVYKDIAFGPKnlgLSEEEAEER----------------VKEALELVGLDEEyLERSPFELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTK 234
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPR 228
|
....*..
gi 490326802 235 TVFDNPT 241
Cdd:TIGR04521 229 EVFSDVD 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-236 |
7.81e-44 |
|
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: 147.97 E-value: 7.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY--GAEPV--FDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR 78
Cdd:COG4181 9 IELRGLTKTVgtGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 -RSVGMVFQEASLFDA-SVRRN----AEyglrvrqswidrlrhelssIVGKTNGTGDAIEALDTVGLREKANQDAASLSG 152
Cdd:COG4181 89 aRHVGFVFQSFQLLPTlTALENvmlpLE-------------------LAGRRDARARARALLERVGLGHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 153 GEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAvLEAKNRGIGV--VIATHDMHQAERiADRVaVLLGNGIIEV 230
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDL-LFELNRERGTtlVLVTHDPALAAR-CDRV-LRLRAGRLVE 226
|
....*.
gi 490326802 231 GDTKTV 236
Cdd:COG4181 227 DTAATA 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-249 |
3.86e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 147.11 E-value: 3.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPD-----HGSIRYENEDVWQVSEQ-ERLeyRRSVGMVF 85
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNlNRL--RRQVSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLFDASVRRNAEYGLRVrQSWIDRLrhELSSIVGKtngtgdAIEALDTVG-LREKANQDAASLSGGEAQRVAFARAL 164
Cdd:PRK14258 95 PKPNLFPMSVYDNVAYGVKI-VGWRPKL--EIDDIVES------ALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 165 AYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRG-IGVVIATHDMHQAERIADRVAVLLGN-----GIIEVGDTKTVFD 238
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGNenrigQLVEFGLTKKIFN 245
|
250
....*....|.
gi 490326802 239 NPTDERTRKFI 249
Cdd:PRK14258 246 SPHDSRTREYV 256
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-251 |
5.08e-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: 5.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDgVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRS-VGMVFQEASLF-DAS 94
Cdd:COG4175 43 VND-ASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRRKkMSMVFQHFALLpHRT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 VRRNAEYGLRVRQswIDRL-RHELssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLL 173
Cdd:COG4175 122 VLENVAFGLEIQG--VPKAeRRER------------AREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 174 DEPTSDLDP--RNtaviE--DAVLE--AK-NRGIgVVIaTHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERTR 246
Cdd:COG4175 188 DEAFSALDPliRR----EmqDELLElqAKlKKTI-VFI-THDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVA 261
|
....*
gi 490326802 247 KFIEG 251
Cdd:COG4175 262 DFVED 266
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-244 |
6.69e-43 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 146.41 E-value: 6.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErLEYRRSVg 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-LARRRAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 mVFQEASL-FDASVRRNAEYGLRVRQSWIDRLRHelssivgktngtgDAIEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:COG4559 80 -LPQHSSLaFPFTVEEVVALGRAPHGSSAAQDRQ-------------IVREALALVGLAHLAGRSYQTLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 162 RALA--YEPD-----ILLLDEPTSDLDPRNtaviEDAVLE-AKN---RGIGVVIATHDMHQAERIADRVAVLLGNGIIEV 230
Cdd:COG4559 146 RVLAqlWEPVdggprWLFLDEPTSALDLAH----QHAVLRlARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
250
....*....|....
gi 490326802 231 GDTKTVFDNPTDER 244
Cdd:COG4559 222 GTPEEVLTDELLER 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-251 |
1.13e-42 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 146.06 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVG 82
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVRQSWIDRLRHelSSIVGKtngtgdaieaLDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:PRK11831 88 MLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLH--STVMMK----------LEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAkNRGIGV--VIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISEL-NSALGVtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
250
....*....|..
gi 490326802 240 PtDERTRKFIEG 251
Cdd:PRK11831 235 P-DPRVRQFLDG 245
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-239 |
1.53e-42 |
|
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: 144.11 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSVG 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--RAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVRQswIDRLRHELssivgktngtgDAIEALDTVgLREKANQDAASLSGGEAQRVAFA 161
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLGAYARR--RAKRKARL-----------ERVYELFPR-LKERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-240 |
4.17e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.03 E-value: 4.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQE--ASLfdasvr 96
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDpyASL------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 rNAeyglrvrqswidrlRHELSSIVG---KTNGTGD-------AIEALDTVGLR-EKANQDAASLSGGEAQRVAFARALA 165
Cdd:COG4608 109 -NP--------------RMTVGDIIAeplRIHGLASkaerrerVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 166 YEPDILLLDEPTSDLDprntaV-IEDAVL----EAKNR-GIGVVIATHDMHQAERIADRVAVL-LGNgIIEVGDTKTVFD 238
Cdd:COG4608 174 LNPKLIVCDEPVSALD-----VsIQAQVLnlleDLQDElGLTYLFISHDLSVVRHISDRVAVMyLGK-IVEIAPRDELYA 247
|
..
gi 490326802 239 NP 240
Cdd:COG4608 248 RP 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-228 |
4.25e-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: 142.40 E-value: 4.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 4 EAIDVHHAYGAEP-VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvSEQERleyRRSVG 82
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKER---RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEAS--LFDASVRRNAEYGLRvrqswidrlrhelssivGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:cd03226 75 YVMQDVDyqLFTDSVREELLLGLK-----------------ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNGII 228
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV-LLLANGAI 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-251 |
6.95e-42 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 143.77 E-value: 6.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLR-------LLALFDApdHGSIRYENEDVWQvSEQERL 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYA-PDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 76 EYRRSVGMVFQEASLFDASVRRNAEYGLRvrqswIDRLRHELSSIVGKtngtgdaieALDTVGL----REKANQDAASLS 151
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGAR-----INGYKGDMDELVER---------SLRQAALwdevKDKLKQSGLSLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRgIGVVIATHDMHQAERIADRVA---VLLGNG-- 226
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAffnVELTEGgg 232
|
250 260
....*....|....*....|....*....
gi 490326802 227 ----IIEVGDTKTVFDNPTDERTRKFIEG 251
Cdd:PRK14243 233 rygyLVEFDRTEKIFNSPQQQATRDYVSG 261
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-249 |
2.26e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 145.36 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqerlEYRRSVG 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-----PYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVrqswiDRL-RHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:PRK11607 95 MMFQSYALFpHMTVEQNIAFGLKQ-----DKLpKAEIASRVN---------EMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
250
....*....|
gi 490326802 240 PTDERTRKFI 249
Cdd:PRK11607 241 PTTRYSAEFI 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-253 |
2.98e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 142.03 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDV---------WQVSEQE 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 74 RLEYRRS-VGMVFQEASLFD-ASVRRNaeyglrVRQSWIDRLRhelssiVGKTNGTGDAIEALDTVGLREKANQD-AASL 150
Cdd:PRK10619 86 QLRLLRTrLTMVFQHFNLWShMTVLEN------VMEAPIQVLG------LSKQEARERAVKYLAKVGIDERAQGKyPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 151 SGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEV 230
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250 260
....*....|....*....|...
gi 490326802 231 GDTKTVFDNPTDERTRKFIEGEL 253
Cdd:PRK10619 234 GAPEQLFGNPQSPRLQQFLKGSL 256
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-233 |
3.69e-41 |
|
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: 141.87 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY---------GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQE 73
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 74 RLEYRRSVGMVFQEA-SLFDAsvRRNaeyglrVRQSWIDRLRHELSsiVGKTNGTGDAIEALDTVGLR-EKANQDAASLS 151
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSpSAVNP--RMT------VRQIIGEPLRHLTS--LDESEQKARIAELLDMVGLRsEDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEV 230
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
...
gi 490326802 231 GDT 233
Cdd:TIGR02769 233 CDV 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-222 |
5.21e-41 |
|
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: 140.24 E-value: 5.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAE-PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSV 81
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLF-DASVRRNAEYGLRVrqswIDRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVAFALEV----TGVPPREIRKRVP---------AALELVGLSHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-240 |
6.09e-41 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 141.36 E-value: 6.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY---------GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQE 73
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 74 RLEYRRSVGMVFQEA-SLFDAsvRRnaeyglRVRQSWIDRLRHELSsiVGKTNGTGDAIEALDTVGLR-EKANQDAASLS 151
Cdd:PRK10419 84 RKAFRRDIQMVFQDSiSAVNP--RK------TVREIIREPLRHLLS--LDKAERLARASEMLRAVDLDdSVLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIE- 229
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVEt 233
|
250
....*....|...
gi 490326802 230 --VGDTKTvFDNP 240
Cdd:PRK10419 234 qpVGDKLT-FSSP 245
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-178 |
6.29e-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: 137.78 E-value: 6.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 18 FDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQvseQERLEYRRSVGMVFQEASLF-DASVR 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD---DERKSLRKEIGYVFQDPQLFpRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 RNAEYGLRVRqswiDRLRHELSSivgktngtgDAIEALDTVGLREKANQ----DAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:pfam00005 78 ENLRLGLLLK----GLSKREKDA---------RAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 490326802 173 LDEPTS 178
Cdd:pfam00005 145 LDEPTA 150
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-240 |
2.07e-40 |
|
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: 139.22 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSVG 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--RLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVRQSWIDRLRHELSSIvgktngtgdaieaLDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:cd03218 79 YLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEEL-------------LEEFHITHLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-237 |
3.32e-40 |
|
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: 139.49 E-value: 3.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY--GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLL-ALFDaPDHGSIRYENEDVwqVSEQERLEYRR 79
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnGLLL-PTSGKVTVDGLDT--LDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 80 SVGMVFQ--EASLFDASVRRNAEYGLRVRQswIDRlrHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQR 157
Cdd:TIGR04520 78 KVGMVFQnpDNQFVGATVEDDVAFGLENLG--VPR--EEMRKRVD---------EALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERiADRVAVLLGNGIIEVGDTKTV 236
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
.
gi 490326802 237 F 237
Cdd:TIGR04520 224 F 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-240 |
4.69e-40 |
|
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: 138.19 E-value: 4.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRS 80
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA--RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLF-DASVRRNAEYGLRVRqswidrlrhelssivgktNGTGDAIEALDTVG-----LREKANQDAASLSGGE 154
Cdd:COG0410 80 IGYVPEGRRIFpSLTVEENLLLGAYAR------------------RDRAEVRADLERVYelfprLKERRRQRAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 155 AQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVlLGNG-IIEVGDT 233
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYV-LERGrIVLEGTA 220
|
....*..
gi 490326802 234 KTVFDNP 240
Cdd:COG0410 221 AELLADP 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-254 |
5.22e-40 |
|
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: 140.22 E-value: 5.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqVSEQERLeyRRSVGMVFQEASLF 91
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRKV--RRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 DA-SVRRNAE-----YGLrvrQSWIDRLRhelssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQRVAFARALA 165
Cdd:TIGR01188 79 EDlTGRENLEmmgrlYGL---PKDEAEER---------------AEELLELFELGEAADRPVGTYSGGMRRRLDIAASLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 166 YEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTK---------TV 236
Cdd:TIGR01188 141 HQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEelkrrlgkdTL 220
|
250
....*....|....*...
gi 490326802 237 FDNPTDERTRKFIEGELI 254
Cdd:TIGR01188 221 ESRPRDIQSLKVEVSMLI 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-249 |
5.83e-40 |
|
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: 138.20 E-value: 5.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 13 GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDvwqVSEQERLEYRRSVGMVFQEASLF- 91
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED---IREQDPVELRRKIGYVIQQIGLFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 DASVRRNAEYGLRVrQSW----IDRLRHELSSIVGktngtgdaieaLDTVGLREKAnqdAASLSGGEAQRVAFARALAYE 167
Cdd:cd03295 89 HMTVEENIALVPKL-LKWpkekIRERADELLALVG-----------LDPAEFADRY---PHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 168 PDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERTR 246
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
...
gi 490326802 247 KFI 249
Cdd:cd03295 234 EFV 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-222 |
9.67e-40 |
|
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: 143.97 E-value: 9.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyRRS 80
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNAEYGLRvrqswiDRLRHELSSIVGKTnGTGDAIEALDTvGLREKANQDAASLSGGEAQRVAF 160
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARP------DASDAEIREALERA-GLDEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnRGIGVVIATHDMHQAERiADRVAVL 222
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-222 |
1.93e-39 |
|
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: 134.65 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqeRLEYRRSVG 82
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDASVRRNAeyglrvrqswidrlrhelssivgktngtgdaiealdtvglrekanqdaasLSGGEAQRVAFAR 162
Cdd:cd03246 80 YLPQDDELFSGSIAENI--------------------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERiADRVAVL 222
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVL 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-252 |
5.52e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 138.93 E-value: 5.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerleyRRSVGMVFQ 86
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 EASLF-DASVRRNAEYGLRVRQswidRLRHELSSIVgktngtgdaIEALDTVGLREKANQDAASLSGGEAQRVAFARALA 165
Cdd:PRK09452 94 SYALFpHMTVFENVAFGLRMQK----TPAAEITPRV---------MEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 166 YEPDILLLDEPTSDLDP--RNTAVIEDAVLEAKnRGIGVVIATHDMHQAERIADRVAVlLGNGIIE-VGDTKTVFDNPTD 242
Cdd:PRK09452 161 NKPKVLLLDESLSALDYklRKQMQNELKALQRK-LGITFVFVTHDQEEALTMSDRIVV-MRDGRIEqDGTPREIYEEPKN 238
|
250
....*....|
gi 490326802 243 ERTRKFIeGE 252
Cdd:PRK09452 239 LFVARFI-GE 247
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-252 |
5.69e-39 |
|
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: 141.75 E-value: 5.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 6 IDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKS----TLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR-RS 80
Cdd:COG4172 14 VAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQE--ASLfdasvrrN---------AE-----YGLRVRQSwidRLRhelssivgktngtgdAIEALDTVGLREKAN 144
Cdd:COG4172 94 IAMIFQEpmTSL-------NplhtigkqiAEvlrlhRGLSGAAA---RAR---------------ALELLERVGIPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 145 QDAA---SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDprntAVIEDAVLE-----AKNRGIGVVIATHDMHQAERIA 216
Cdd:COG4172 149 RLDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAQILDllkdlQRELGMALLLITHDLGVVRRFA 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 490326802 217 DRVAVLLGNGIIEVGDTKTVFDNPTDERTRKFIEGE 252
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLLAAE 260
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-240 |
6.06e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 135.54 E-value: 6.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvseqERLE-YRR 79
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI------THLPmHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 80 S---VGMVFQEASLF-DASVRRN-------AEYGLRVRQSWIDRLRHELSsivgktngtgdaIEALdtvglrekANQDAA 148
Cdd:COG1137 76 ArlgIGYLPQEASIFrKLTVEDNilavlelRKLSKKEREERLEELLEEFG------------ITHL--------RKSKAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGII 228
Cdd:COG1137 136 SLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVL 215
|
250
....*....|..
gi 490326802 229 EVGDTKTVFDNP 240
Cdd:COG1137 216 AEGTPEEILNNP 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-250 |
1.38e-38 |
|
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: 140.98 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTL----LRLLalfdaPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQE--ASLfd 92
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpfGSL-- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 aSVRRN-----AEyGLRVRQSWIDRL-RHELssivgktngtgdAIEALDTVGLrekanqDAASL-------SGGEAQRVA 159
Cdd:COG4172 376 -SPRMTvgqiiAE-GLRVHGPGLSAAeRRAR------------VAEALEEVGL------DPAARhryphefSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDprntAVIEDAVLE-----AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTK 234
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALD----VSVQAQILDllrdlQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTE 511
|
250
....*....|....*.
gi 490326802 235 TVFDNPTDERTRKFIE 250
Cdd:COG4172 512 QVFDAPQHPYTRALLA 527
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-243 |
1.54e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.01 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDvwqvseqerleyrrsv 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 gmvfqeaslFDASVRRN-----AEYGLRVRQSWIDRLR-----HELSSIVGKTNgtgdAIEALDTVGLREKANQDAASLS 151
Cdd:COG4152 65 ---------LDPEDRRRigylpEERGLYPKMKVGEQLVylarlKGLSKAEAKRR----ADEWLERLGLGDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNGiievg 231
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRI-VIINKG----- 205
|
250
....*....|..
gi 490326802 232 dtKTVFDNPTDE 243
Cdd:COG4152 206 --RKVLSGSVDE 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-229 |
2.10e-38 |
|
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: 133.15 E-value: 2.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleyrRSVG 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVR---QSWIDRLRHELSSIVGktngtgdaIEALdtvgLREKANQdaasLSGGEAQRV 158
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRkvpKDEIDERVREVAELLQ--------IEHL----LDRKPKQ----LSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDP--RNTAVIEDAVLEaKNRGIGVVIATHDMHQAERIADRVAVlLGNGIIE 229
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAklRVQMRAELKRLQ-QRLGTTTIYVTHDQVEAMTMADRIAV-MNDGQIQ 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-222 |
2.30e-38 |
|
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: 133.17 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwQVSEQERLEYrrsvg 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIGY----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 mvFQEaslfdasvrrnaEYGLRVRQSWIDRLRHeLSSIVG--KTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:cd03269 75 --LPE------------ERGLYPKMKVIDQLVY-LAQLKGlkKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-222 |
3.03e-38 |
|
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: 140.27 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyRRSV 81
Cdd:COG4618 332 SVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLFDASVRRNaeyglrvrqswIDRLR----------------HELssIVGKTNGtgdaieaLDT-VGlrekan 144
Cdd:COG4618 409 GYLPQDVELFDGTIAEN-----------IARFGdadpekvvaaaklagvHEM--ILRLPDG-------YDTrIG------ 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 145 QDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMhQAERIADRVAVL 222
Cdd:COG4618 463 EGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVL 539
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-231 |
3.09e-38 |
|
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: 133.51 E-value: 3.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAE-PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeQERLeyRRSVGMVF 85
Cdd:cd03253 5 NVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSL--RRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLFDASVRRNAEYGlRVRQSWIDRLRhelssiVGKTNGTGDAIEAL----DTV----GLRekanqdaasLSGGEAQR 157
Cdd:cd03253 82 QDTVLFNDTIGYNIRYG-RPDATDEEVIE------AAKAAQIHDKIMRFpdgyDTIvgerGLK---------LSGGEKQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERI--ADRVAVLLGNGIIEVG 231
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA----HRLSTIvnADKIIVLKDGRIVERG 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-240 |
5.39e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 135.98 E-value: 5.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyrrS 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLF-DASVRRNAEYGLRVRQswidrlRHELSSivgktngtGDAIEA-----LDTVGLREKANQDAASLSGGE 154
Cdd:PRK10851 76 VGFVFQHYALFrHMTVFDNIAFGLTVLP------RRERPN--------AAAIKAkvtqlLEMVQLAHLADRYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 155 AQRVAFARALAYEPDILLLDEPTSDLDprnTAV-------IEDAVLEAKNRGigvVIATHDMHQAERIADRVaVLLGNGI 227
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALD---AQVrkelrrwLRQLHEELKFTS---VFVTHDQEEAMEVADRV-VVMSQGN 214
|
250
....*....|....
gi 490326802 228 IE-VGDTKTVFDNP 240
Cdd:PRK10851 215 IEqAGTPDQVWREP 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-219 |
6.85e-38 |
|
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: 132.56 E-value: 6.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 9 HHAYGAE-PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVW----QVSEQERLEYRRS-VG 82
Cdd:COG4778 17 HLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaQASPREILALRRRtIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQeaslFdasvrrnaeygLRV--RQSWIDrlrhelssIVgktngtgdaIEALDTVGL-REKANQDAASL--------- 150
Cdd:COG4778 97 YVSQ----F-----------LRVipRVSALD--------VV---------AEPLLERGVdREEARARARELlarlnlper 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 151 ---------SGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRV 219
Cdd:COG4778 145 lwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRV 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-237 |
7.05e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.99 E-value: 7.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAY-----GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIR-----YENEDVWQVs 70
Cdd:PRK13635 1 MKEEIIRVEHISfrypdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvLSEETVWDV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 71 eqerleyRRSVGMVFQ--EASLFDASVRRNAEYGLR----VRQSWIDRLRhelssivgktngtgdaiEALDTVGLREKAN 144
Cdd:PRK13635 80 -------RRQVGMVFQnpDNQFVGATVQDDVAFGLEnigvPREEMVERVD-----------------QALRQVGMEDFLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 145 QDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKN-RGIGVVIATHDMHQAERiADRVAVLL 223
Cdd:PRK13635 136 REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMN 214
|
250
....*....|....
gi 490326802 224 GNGIIEVGDTKTVF 237
Cdd:PRK13635 215 KGEILEEGTPEEIF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-253 |
8.29e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 133.25 E-value: 8.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLL----RLLALFDAPDH--GSIRYENEDVWQVseqERLEYRRSVGMVFQEASL 90
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnRLIEIYDSKIKvdGKVLYFGKDIFQI---DAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 91 F-DASVRRNAEYGLRvrqSWIDRLRHELSSIVGktngtgdaiEALDTVGL----REKANQDAASLSGGEAQRVAFARALA 165
Cdd:PRK14246 102 FpHLSIYDNIAYPLK---SHGIKEKREIKKIVE---------ECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 166 YEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRgIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERT 245
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
....*...
gi 490326802 246 RKFIEGEL 253
Cdd:PRK14246 249 EKYVIGRI 256
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-232 |
9.68e-38 |
|
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: 132.28 E-value: 9.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEP---VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRSVGM 83
Cdd:cd03249 5 NVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQEASLFDASVRRNAEYGLRvrqswiDRLRHELSSIVGKTNGTgDAIEAL----DT-VGLRekanqdAASLSGGEAQRV 158
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKP------DATDEEVEEAAKKANIH-DFIMSLpdgyDTlVGER------GSQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnRGIGVVIATHDMHqAERIADRVAVLLGNGIIEVGD 232
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGT 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-222 |
2.30e-37 |
|
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: 130.70 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAE--PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYRRS 80
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDA-SVRRNAEYGLRVRqswidrlrhelssivGKTNGTGDAI--EALDTVGLREKANQDAASLSGGEAQR 157
Cdd:cd03263 77 LGYCPQFDALFDElTVREHLRFYARLK---------------GLPKSEIKEEveLLLRVLGLTDKANKRARTLSGGMKRK 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIM 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-222 |
3.18e-37 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 129.66 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 11 AYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENedvwqvseqerleyRRSVGMVFQEASL 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------------GARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 91 ---FDASVRRNAEYGLRVRQSWIDRLRHELSSIVgktngtgdaIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYE 167
Cdd:NF040873 67 pdsLPLTVRDLVAMGRWARRGLWRRLTRDDRAAV---------DDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 168 PDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAeRIADRVAVL 222
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-231 |
4.03e-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: 129.64 E-value: 4.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRyenedVWQVSEQERLEYRRSVGMVFQEASLF 91
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-----FDGKSYQKNIEALRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 DA-SVRRNAEYGLRVRQswIDRLRHElssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDI 170
Cdd:cd03268 85 PNlTARENLRLLARLLG--IRKKRID---------------EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 171 LLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVG 231
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-240 |
1.44e-36 |
|
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: 129.32 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSV 81
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERA--RLGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLF-DASVRRNAEYGLRVRQSWI-DRLRHELSSIvgktngtgdaieaLDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:TIGR04406 79 GYLPQEASIFrKLTVEENIMAVLEIRKDLDrAEREERLEAL-------------LEEFQISHLRDNKAMSLSGGERRRVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:TIGR04406 146 IARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVAN 225
|
.
gi 490326802 240 P 240
Cdd:TIGR04406 226 E 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-228 |
1.51e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.80 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyrrsvgMVFQ 86
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR--------LMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 EASLFD-ASVRRNAeyGLRVRQSWIDRlrhelssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQRVAFARALA 165
Cdd:PRK11247 89 DARLLPwKKVIDNV--GLGLKGQWRDA-----------------ALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 166 YEPDILLLDEPTSDLDPRNTAVIEDaVLEA--KNRGIGVVIATHDMHQAERIADRVaVLLGNGII 228
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQD-LIESlwQQHGFTVLLVTHDVSEAVAMADRV-LLIEEGKI 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-222 |
2.02e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRrsVG 82
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG--IA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYG-LRVRQSWIDR--LRHElssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQRV 158
Cdd:COG1129 83 IIHQELNLVpNLSVAENIFLGrEPRRGGLIDWraMRRR-------------ARELLARLGLDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-208 |
2.40e-36 |
|
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: 134.80 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerlEYRRS 80
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD---EVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNaeygLRvrqswidrlrhelssiVGKTNGTGDAI-EALDTVGLRE-----------KANQDAA 148
Cdd:TIGR02868 411 VSVCAQDAHLFDTTVREN----LR----------------LARPDATDEELwAALERVGLADwlralpdgldtVLGEGGA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRN-TAVIEDavLEAKNRGIGVVIATHD 208
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELLED--LLAALSGRTVVLITHH 529
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-213 |
2.84e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 127.60 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 11 AYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPD---HGSIRYENEDVWQVSEQerleyRRSVGMVFQE 87
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE-----QRRIGILFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 ASLFD-ASVRRNAEYGLRVRqswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAY 166
Cdd:COG4136 85 DLLFPhLSVGENLAFALPPT--------------IGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490326802 167 EPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAE 213
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEEDAP 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-251 |
4.45e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 129.06 E-value: 4.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGsIRYENEDVWQ----VSEQERLEYR 78
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGgrsiFNYRDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQEASLFDASVRRNAEYGLRVRQswidrlrhelssIVGKTNGTGDAIEALDTVGL----REKANQDAASLSGGE 154
Cdd:PRK14271 101 RRVGMLFQRPNPFPMSIMDNVLAGVRAHK------------LVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 155 AQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRgIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTK 234
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
250
....*....|....*..
gi 490326802 235 TVFDNPTDERTRKFIEG 251
Cdd:PRK14271 248 QLFSSPKHAETARYVAG 264
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-222 |
7.93e-36 |
|
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: 126.71 E-value: 7.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEP----VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYR 78
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQEASLFD-ASVRRNAEY-----GLRvrqswidrlRHELSsivgktngtgDAIEAL-DTVGLREKANQDAASLS 151
Cdd:cd03266 78 RRLGFVSDSTGLYDrLTARENLEYfaglyGLK---------GDELT----------ARLEELaDRLGMEELLDRRVGGFS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03266 139 TGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-231 |
1.34e-35 |
|
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: 126.33 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYRRSVGMVFQEASLF 91
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 DA-SVRRNAE-----YGLRvRQSWIDRLRhelssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALA 165
Cdd:cd03265 86 DElTGWENLYiharlYGVP-GAERRERID-----------------ELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 166 YEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVG 231
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-238 |
1.36e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 127.44 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerlEYRRS 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR---QLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQE-ASLFDASVRRNAEYGlrvRQSWID---RLRHELSSIVGKtngtgdAIEALDTVGLrekANQDAASLSGGEAQ 156
Cdd:PRK11231 78 LALLPQHhLTPEGITVRELVAYG---RSPWLSlwgRLSAEDNARVNQ------AMEQTRINHL---ADRRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGD---- 232
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTpeev 225
|
250
....*....|.
gi 490326802 233 -----TKTVFD 238
Cdd:PRK11231 226 mtpglLRTVFD 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-241 |
2.86e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 132.92 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEP---VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDvwqVSEQERLEYRRSVGM 83
Cdd:TIGR00958 483 DVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP---LVQYDHHYLHRQVAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQEASLFDASVRRNAEYGLrvrqswiDRLRHELSSIVGKTNGTGDAIEAL----DTVgLREKANQdaasLSGGEAQRVA 159
Cdd:TIGR00958 560 VGQEPVLFSGSVRENIAYGL-------TDTPDEEIMAAAKAANAHDFIMEFpngyDTE-VGEKGSQ----LSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDprntAVIEDAVLEAKNR-GIGVVIATHDMHQAERiADRVAVLLGNGIIEVGDTKTVFD 238
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALD----AECEQLLQESRSRaSRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
...
gi 490326802 239 NPT 241
Cdd:TIGR00958 703 DQG 705
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-231 |
3.19e-35 |
|
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: 125.42 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRSVGMVF 85
Cdd:cd03254 7 NVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLFDASVRRNAEYGLrvrqswiDRLRHELSSIVGKTNGTGDAIEALdTVGLREKANQDAASLSGGEAQRVAFARALA 165
Cdd:cd03254 84 QDTFLFSGTIMENIRLGR-------PNATDEEVIEAAKEAGAHDFIMKL-PNGYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 166 YEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERI--ADRVAVLLGNGIIEVG 231
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA----HRLSTIknADKILVLDDGKIIEEG 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-228 |
5.64e-35 |
|
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: 124.62 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyRRSVGMVFQEASLFDASV 95
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 96 RRNAEYGlrvRQSWIDRLRHELSSIVGKTNGTGDAIEALDT-VGLRekanqdAASLSGGEAQRVAFARALAYEPDILLLD 174
Cdd:cd03245 95 RDNITLG---APLADDERILRAAELAGVTDFVNKHPNGLDLqIGER------GRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 175 EPTSDLDPRNtaviEDAVLEAKNRGIG---VVIATHDMhQAERIADRVAVLLGNGII 228
Cdd:cd03245 166 EPTSAMDMNS----EERLKERLRQLLGdktLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-241 |
5.77e-35 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 129.19 E-value: 5.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRS 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---ASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASL-FDASVRRNAEYGlrvrqswidrlRHELSSIVGKTNGTGDAI--EALDTVGLREKANQDAASLSGGEAQR 157
Cdd:PRK09536 79 VASVPQDTSLsFEFDVRQVVEMG-----------RTPHRSRFDTWTETDRAAveRAMERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
....
gi 490326802 238 DNPT 241
Cdd:PRK09536 228 TADT 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-228 |
5.89e-35 |
|
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: 124.53 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPV-FDgvsLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyrrSVGMVF 85
Cdd:cd03298 5 KIRFSYGEQPMhFD---LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-----PVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLF-DASVRRNAEYGLRVRQswidRLRHELSSIVGKtngtgdaieALDTVGLREKANQDAASLSGGEAQRVAFARAL 164
Cdd:cd03298 77 QENNLFaHLTVEQNVGLGLSPGL----KLTAEDRQAIEV---------ALARVGLAGLEKRLPGELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 165 AYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVaVLLGNGII 228
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRV-VFLDNGRI 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-220 |
3.64e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.64 E-value: 3.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIryenedvwQVSEQERleyrrsVGMVFQ 86
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLR------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 EASLFD-ASVRRNAEYGLRVRQSWIDRLrHELSSIVGKTNGTGDAIEALDTV------------------GLR---EKAN 144
Cdd:COG0488 69 EPPLDDdLTVLDTVLDGDAELRALEAEL-EELEAKLAEPDEDLERLAELQEEfealggweaearaeeilsGLGfpeEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 145 QDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDprntaviEDAV--LEA--KNRGIGVVIATHDMHQAERIADRVA 220
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIewLEEflKNYPGTVLVVSHDRYFLDRVATRIL 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-222 |
4.49e-34 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 120.61 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSVG 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR--RAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQeaslfdasvrrnaeyglrvrqswidrlrhelssivgktngtgdaiealdtvglrekanqdaasLSGGEAQRVAFAR 162
Cdd:cd03216 79 MVYQ---------------------------------------------------------------LSVGERQMVEIAR 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-243 |
1.08e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 121.61 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 22 SLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerleyRRSVGMVFQEASLFD-ASVRRNAE 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQENNLFShLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 101 YGLRVRQSWIDRLRHELSSIVGKtngtgdaiealdtVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDL 180
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQ-------------MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 181 DP--RNTAV-IEDAVLEakNRGIGVVIATHDMHQAERIADRvAVLLGNGIIevgdtktVFDNPTDE 243
Cdd:PRK10771 161 DPalRQEMLtLVSQVCQ--ERQLTLLMVSHSLEDAARIAPR-SLVVADGRI-------AWDGPTDE 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-226 |
1.12e-33 |
|
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: 121.42 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQ--ERLeyrrsvgMVFQEASLFD-ASV 95
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITEPgpDRM-------VVFQNYSLLPwLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 96 RRNAeyGLRVRQSWIDRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDE 175
Cdd:TIGR01184 72 RENI--ALAVDRVLPDLSKSERRAIVE---------EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490326802 176 PTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVaVLLGNG 226
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQiWEEHRVTVLMVTHDVDEALLLSDRV-VMLTNG 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-240 |
1.63e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.49 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY--GAEpVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwQVSEQERLEYRRS 80
Cdd:PRK13639 2 LETRDLKYSYpdGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQ--EASLFDASVRRNAEYG-LRVRQSwidrlRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQR 157
Cdd:PRK13639 80 VGIVFQnpDDQLFAPTVEEDVAFGpLNLGLS-----KEEVEKRVK---------EALKAVGMEGFENKPPHHLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
...
gi 490326802 238 DNP 240
Cdd:PRK13639 226 SDI 228
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-208 |
3.14e-33 |
|
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: 119.06 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwQVSEQERLEYRRSVGMVFQEA--SLFDAS 94
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERRQRVGLVFQDPddQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 VRRNAEYGLRVRQSWIDRLRHELssivgktngtGDAIEALDTVGLREKANQdaaSLSGGEAQRVAFARALAYEPDILLLD 174
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERRV----------REALTAVGASGLRERPTH---CLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....
gi 490326802 175 EPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHD 208
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-232 |
3.44e-33 |
|
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: 120.41 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAE--PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRSVGMV 84
Cdd:cd03251 5 NVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 85 FQEASLFDASVRRNAEYGLR------VRQSwiDRLRHELSSIVGKTNGtgdaieaLDT-VGLRekanqdAASLSGGEAQR 157
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPgatreeVEEA--ARAANAHEFIMELPEG-------YDTvIGER------GVKLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRgIGVVIAthdmHQAERI--ADRVAVLLGNGIIEVGD 232
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERlMKNR-TTFVIA----HRLSTIenADRIVVLEDGKIVERGT 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-240 |
4.88e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 122.91 E-value: 4.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleyrRSVG 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVrqswIDRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:PRK11432 82 MVFQSYALFpHMSLGENVGYGLKM----LGVPKEERKQRVK---------EALELVDLAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-253 |
8.27e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 121.61 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYgaePV-------------FDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQV 69
Cdd:PRK11308 6 LQAIDLKKHY---PVkrglfkperlvkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 70 SEQERLEYRRSVGMVFQE--ASLfdasvrrNAeyglrvrqswidrlRHELSSIVG---KTNGTGDAIE-------ALDTV 137
Cdd:PRK11308 83 DPEAQKLLRQKIQIVFQNpyGSL-------NP--------------RKKVGQILEeplLINTSLSAAErrekalaMMAKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 138 GLR-EKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDprntAVIEDAVLE-----AKNRGIGVVIATHDMHQ 211
Cdd:PRK11308 142 GLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD----VSVQAQVLNlmmdlQQELGLSYVFISHDLSV 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 212 AERIADRVAVLLGNGIIEVGDTKTVFDNP-----------------TDERTRKFIEGEL 253
Cdd:PRK11308 218 VEHIADEVMVMYLGRCVEKGTKEQIFNNPrhpytqallsatprlnpDDRRERIKLTGEL 276
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-222 |
1.80e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.20 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYG----AEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwQVSEQERle 76
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 77 yrrsvGMVFQEASLFD-ASVRRNAEYGLRVRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEA 155
Cdd:COG4525 79 -----GVVFQKDALLPwLNVLDNVAFGLRLRG-------------VPKAERRARAEELLALVGLADFARRRIWQLSGGMR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVL 222
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-251 |
3.33e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 121.68 E-value: 3.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 22 SLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRS-VGMVFQEASLF-DASVRRNA 99
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 100 EYGLrvrqswidrlrhELSSIVGKTNGTgDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSD 179
Cdd:PRK10070 128 AFGM------------ELAGINAEERRE-KALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490326802 180 LDPRNTAVIEDAV--LEAKNRGIgVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERTRKFIEG 251
Cdd:PRK10070 195 LDPLIRTEMQDELvkLQAKHQRT-IVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-222 |
3.79e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 120.32 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQERLEyRRS 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---PVPARARLA-RAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQeaslFDasvrrNAEYGLRVRQSWIdrlrhelssIVGKTNG-TGDAIEA-----LDTVGLREKANQDAASLSGGE 154
Cdd:PRK13536 116 IGVVPQ----FD-----NLDLEFTVRENLL---------VFGRYFGmSTREIEAvipslLEFARLESKADARVSDLSGGM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 155 AQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-229 |
5.93e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.48 E-value: 5.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYeNEDVwQVS----EQERLEYr 78
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-KIGyfdqHQEELDP- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 rsvgmvfqEASLFDAsVRRNAEYGLRVrqswidrlrhELSSIVGKTNGTGDaiealdtvglreKANQDAASLSGGEAQRV 158
Cdd:COG0488 393 --------DKTVLDE-LRDGAPGGTEQ----------EVRGYLGRFLFSGD------------DAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnrgiG-VVIATHDMHQAERIADRVAVLLGNGIIE 229
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP----GtVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-222 |
7.80e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.74 E-value: 7.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerlEYRRS 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNAEYGLRVRQSWIDRlrhelssivgktngtgDAIEA-LDTVGLREKA-NQDAASLSGGEAQRV 158
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDP----------------AIFLDdLERFALPDTIlTKNIAELSGGEKQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERiADRVAVL 222
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-222 |
8.00e-32 |
|
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: 119.83 E-value: 8.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIrYENEDVWQVSEQERL--EYRRSVGMVFQEASLF-DASVRR 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-VLNGRTLFDSRKGIFlpPEKRRIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NAEYGLRvrqswidRLRHELssivgkTNGTGDAIeaLDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPT 177
Cdd:TIGR02142 95 NLRYGMK-------RARPSE------RRISFERV--IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490326802 178 SDLD-PRNTAVIedAVLE--AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:TIGR02142 160 AALDdPRKYEIL--PYLErlHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-222 |
2.24e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 117.60 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHA---YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErley 77
Cdd:PRK13537 3 MSVAPIDFRNVekrYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLF-DASVRRNaeygLRVRQSWIDRLRHELSSIVGKTngtgdaieaLDTVGLREKANQDAASLSGGEAQ 156
Cdd:PRK13537 79 RQRVGVVPQFDNLDpDFTVREN----LLVFGRYFGLSAAAARALVPPL---------LEFAKLENKADAKVGELSGGMKR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-219 |
2.35e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 115.68 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR-RSVGMVFQEASLF-DAS 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQFHHLLpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 VRRNAEYGLrvrqswidrlrhelssIVGKTN---GTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDIL 171
Cdd:PRK11629 104 ALENVAMPL----------------LIGKKKpaeINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490326802 172 LLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRV 219
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQL 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-242 |
3.63e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDG-----VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLE-YRRS 80
Cdd:PRK13634 7 KVEHRYQYKTPFERralydVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKpLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQ--EASLFDASVRRNAEYGlrvrqswidrlrhELSSIVGKTNGTGDAIEALDTVGLREKA-NQDAASLSGGEAQR 157
Cdd:PRK13634 87 VGIVFQfpEHQLFEETVEKDICFG-------------PMNFGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTV 236
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
....*.
gi 490326802 237 FDNPTD 242
Cdd:PRK13634 234 FADPDE 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-231 |
3.96e-31 |
|
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: 114.21 E-value: 3.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGeVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDvwqVSEQeRLEYRRSVG 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD---VLKQ-PQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDA-SVRRNAEYglrvrQSWIDRLRH-ELSSIVgktngtgdaIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDY-----IAWLKGIPSkEVKARV---------DEVLELVNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRgiGVVIATHDMHQAERIADRVAVLLGNGIIEVG 231
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSElGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-222 |
3.98e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 114.59 E-value: 3.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 8 VHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQ 86
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 EASLF-DASVRRNAEYGLRVRQSWIDRLRHELSSivgktngtgdaieALDTVGLREKANQDAASLSGGEAQRVAFARALA 165
Cdd:PRK10908 87 DHHLLmDRTVYDNVAIPLIIAGASGDDIRRRVSA-------------ALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 166 YEPDILLLDEPTSDLDprnTAVIEDA--VLEAKNR-GIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK10908 154 NKPAVLLADEPTGNLD---DALSEGIlrLFEEFNRvGVTVLMATHDIGLISRRSYRMLTL 210
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-231 |
5.90e-31 |
|
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: 120.31 E-value: 5.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAE-PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeQERLeyRRSVGMVF 85
Cdd:COG5265 362 NVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT-QASL--RAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLFDASVRRNAEYGlRVRQSwIDRLRH--ELSSIvgktngtGDAIEAL----DTV----GLRekanqdaasLSGGEA 155
Cdd:COG5265 439 QDTVLFNDTIAYNIAYG-RPDAS-EEEVEAaaRAAQI-------HDFIESLpdgyDTRvgerGLK---------LSGGEK 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIgVVIAthdmHQAERI--ADRVAVLLGNGIIEVG 231
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREvARGRTT-LVIA----HRLSTIvdADEILVLEAGRIVERG 574
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
7-231 |
6.51e-31 |
|
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: 120.19 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEP---VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerlEYRRSVGM 83
Cdd:TIGR02204 342 QVNFAYPARPdqpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPA---ELRARMAL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQEASLFDASVRRNAEYGL------RVRQSWIDRLRHELssivgktngtgdaIEALDTvGLREKANQDAASLSGGEAQR 157
Cdd:TIGR02204 419 VPQDPVLFAASVMENIRYGRpdatdeEVEAAARAAHAHEF-------------ISALPE-GYDTYLGERGVTLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERI--ADRVAVLLGNGIIEVG 231
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA----HRLATVlkADRIVVMDQGRIVAQG 556
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
8.82e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 115.95 E-value: 8.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAE-----PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSI---------------- 59
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 60 -RYENEDVWQVSEQERL----EYRRSVGMVFQ--EASLFDASVRRNAEYGLRvrqswidrlrhelSSIVGKTNGTGDAIE 132
Cdd:PRK13651 81 eKVLEKLVIQKTRFKKIkkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPV-------------SMGVSKEEAKKRAAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 133 ALDTVGLREKANQDAA-SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQ 211
Cdd:PRK13651 148 YIELVGLDESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDN 227
|
250 260
....*....|....*....|....*...
gi 490326802 212 AERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PRK13651 228 VLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-222 |
1.73e-30 |
|
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: 113.33 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEP---VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQERLEYRRSVGM 83
Cdd:cd03248 16 NVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK---PISQYEHKYLHSKVSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQEASLFDASVRRNAEYGLrvrQSWIDRLRHELSSivgkTNGTGDAIEALDTvGLREKANQDAASLSGGEAQRVAFARA 163
Cdd:cd03248 93 VGQEPVLFARSLQDNIAYGL---QSCSFECVKEAAQ----KAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 164 LAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAtHDMHQAERiADRVAVL 222
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA-HRLSTVER-ADQILVL 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-237 |
2.31e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.17 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY--GAEpVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwQVSEQERLEYRRS 80
Cdd:PRK13636 6 LKVEELNYNYsdGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEA--SLFDASVRRNAEYGLRVRQSWIDRLRHELSSIVGKTngtgdaiealdtvGLREKANQDAASLSGGEAQRV 158
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRT-------------GIEHLKDKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
2.73e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.93 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 4 EAIDVHHAYGAE--PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEY-RRS 80
Cdd:PRK13632 9 KVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKENLKEiRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQ--EASLFDASVRRNAEYGLRVRQswIDRlrHELSSIVgktngtgdaIEALDTVGLREKANQDAASLSGGEAQRV 158
Cdd:PRK13632 85 IGIIFQnpDNQFIGATVEDDIAFGLENKK--VPP--KKMKDII---------DDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIA-THDMHQAeRIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
..
gi 490326802 238 DN 239
Cdd:PRK13632 231 NN 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-240 |
1.69e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 111.17 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENE-----DVWQVSEQE-RLE 76
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAErRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 77 YRRSVGMVFQeaslfdasvrrNAEYGLRVRQSW----IDRL-----RHelssiVGKTNGTgdAIEALDTVGLREKANQDA 147
Cdd:PRK11701 87 LRTEWGFVHQ-----------HPRDGLRMQVSAggniGERLmavgaRH-----YGDIRAT--AGDWLERVEIDAARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 148 -ASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGN 225
Cdd:PRK11701 149 pTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250
....*....|....*
gi 490326802 226 GIIEVGDTKTVFDNP 240
Cdd:PRK11701 229 RVVESGLTDQVLDDP 243
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-232 |
1.84e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 111.75 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRSVGMVFQEA--SLFDASVR 96
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSKVGLVFQDPddQVFSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 RNAEYG---LRVRQSWIDRlRHElssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLL 173
Cdd:PRK13647 99 DDVAFGpvnMGLDKDEVER-RVE---------------EALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 174 DEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGD 232
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-240 |
2.52e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.84 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVF-----DGVSLSVTPGEVVGIIGPSGVGKSTLLRLlalFDA---PDHGSIRYENEDVW-QVSE 71
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMekkglDNISFELEEGSFVALVGHTGSGKSTLMQH---FNAllkPSSGTITIAGYHITpETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 72 QERLEYRRSVGMVFQ--EASLFDASVRRNAEYGLRVRQSWIDRLRHElssivgktngtgdAIEALDTVGLREK-ANQDAA 148
Cdd:PRK13641 78 KNLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK-------------ALKWLKKVGLSEDlISKSPF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGII 228
Cdd:PRK13641 145 ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
250
....*....|..
gi 490326802 229 EVGDTKTVFDNP 240
Cdd:PRK13641 225 KHASPKEIFSDK 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-239 |
3.72e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWqvSEQERL-EYRRSVGMVFQ--EASLFDASV 95
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVKLsDIRKKVGLVFQypEYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 96 RRNAEYGLRvrqswidRLRHELSSIVGKTngtgdaIEALDTVGLREKANQDAA--SLSGGEAQRVAFARALAYEPDILLL 173
Cdd:PRK13637 102 EKDIAFGPI-------NLGLSEEEIENRV------KRAMNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 174 DEPTSDLDPRNtaviEDAVLEA-----KNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PRK13637 169 DEPTAGLDPKG----RDEILNKikelhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-231 |
3.73e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.06 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqeRLEYRRSVGMVF 85
Cdd:PRK13657 339 DVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLFDASVRRNaeyglrvrqswidrLRhelssiVGKTNGT-------GDAIEALDTV-----GLREKANQDAASLSGG 153
Cdd:PRK13657 416 QDAGLFNRSIEDN--------------IR------VGRPDATdeemraaAERAQAHDFIerkpdGYDTVVGERGRQLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 154 EAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRgIGVVIAthdmHQAE--RIADRVAVLLGNGIIEV 230
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmKGR-TTFIIA----HRLStvRNADRILVFDNGRVVES 550
|
.
gi 490326802 231 G 231
Cdd:PRK13657 551 G 551
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-238 |
3.83e-29 |
|
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: 109.88 E-value: 3.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerlEYRRS 80
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA---WLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRN---AEYGLRVRQSwidrlrHELSSIVGKTNGTGDAIEALDTVglrekANQDAASLSGGEAQR 157
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNialADPGMSMERV------IEAAKLAGAHDFISELPEGYDTI-----VGEQGAGLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAvLEAKNRGIGVVIATHDMhQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRN-MHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELL 224
|
.
gi 490326802 238 D 238
Cdd:cd03252 225 A 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-236 |
8.43e-29 |
|
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: 113.74 E-value: 8.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDA--PDHGSIRY------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 62 -----------ENEDVWQVSEQERLEYRRSVGMVFQeaslfdasvRRNAEYGlrvRQSWIDRLRHELSSIVGK-TNGTGD 129
Cdd:TIGR03269 81 pcpvcggtlepEEVDFWNLSDKLRRRIRKRIAIMLQ---------RTFALYG---DDTVLDNVLEALEEIGYEgKEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 130 AIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHD 208
Cdd:TIGR03269 149 AVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*....
gi 490326802 209 MHQAERIADRvAVLLGNG-IIEVGDTKTV 236
Cdd:TIGR03269 229 PEVIEDLSDK-AIWLENGeIKEEGTPDEV 256
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-212 |
1.12e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.02 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwQVSEQERleyrrsvG 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAER-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQ-EASLFDASVRRNAEYGLRVRQswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQLAG-------------VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQA 212
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEA 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-207 |
1.32e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 107.65 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYrrs 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VG----MvfqEASLfdaSVRRNAEYglrvrqsWIDRLRHELSSIVgktngtgdaiEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:PRK13539 78 LGhrnaM---KPAL---TVAENLEF-------WAAFLGGEELDIA----------AALEAVGLAPLAHLPFGYLSAGQKR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATH 207
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-241 |
1.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.50 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 15 EPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQ--EASLFD 92
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQnpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 ASVRRNAEYGLRVRQSwidrLRHELSSIVGKtngtgdaieALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:PRK13640 100 ATVGDDVAFGLENRAV----PRPEMIKIVRD---------VLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 173 LDEPTSDLDPRNTAVIEDAVLEAKN-RGIGVVIATHDMHQAErIADRVAVLLGNGIIEVGDTKTVFDNPT 241
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-252 |
4.47e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.29 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSV 81
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLFDA-SVRRNAEYGLRVRQSWIDRLRHELSSivgktngtgDAIEALDTVGLREKANQdaaSLSGGEAQRVAF 160
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMAVLQIRDDLSAEQREDRAN---------ELMEEFHIEHLRDSMGQ---SLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFdnp 240
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL--- 225
|
250
....*....|..
gi 490326802 241 TDERTRKFIEGE 252
Cdd:PRK10895 226 QDEHVKRVYLGE 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-231 |
5.58e-28 |
|
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: 111.73 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAE--PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRS 80
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS---LRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNAEYGlRVRQswIDRLRHElsSIVGKTNGTgDAIEALDTvGLREKANQDAASLSGGEAQRVAF 160
Cdd:TIGR02203 408 VALVSQDVVLFNDTIANNIAYG-RTEQ--ADRAEIE--RALAAAYAQ-DFVDKLPL-GLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAvLEA--KNRgIGVVIAtHDMHQAERiADRVAVLLGNGIIEVG 231
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAA-LERlmQGR-TTLVIA-HRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-237 |
6.68e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDG-----VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERL 75
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 76 EY-RRSVGMVFQ--EASLFDASVRRNAEYGLR---VRQSWIDRLrhelssivgktngtgdAIEALDTVGLREKA-NQDAA 148
Cdd:PRK13649 81 KQiRKKVGLVFQfpESQLFEETVLKDVAFGPQnfgVSQEEAEAL----------------AREKLALVGISESLfEKNPF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGII 228
Cdd:PRK13649 145 ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
....*....
gi 490326802 229 EVGDTKTVF 237
Cdd:PRK13649 225 LSGKPKDIF 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
21-250 |
9.37e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 106.85 E-value: 9.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwqvseqeRLEYR------RSVGMVFQEAS----- 89
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---------KLEYGdykyrcKHIRMIFQDPNtslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 90 ------LFDASVRRNAEYGLRVRQSWIdrlrhelssivgktngtgdaIEALDTVGL-REKANQDAASLSGGEAQRVAFAR 162
Cdd:COG4167 103 rlnigqILEEPLRLNTDLTAEEREERI--------------------FATLRLVGLlPEHANFYPHMLSSGQKQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPT 241
Cdd:COG4167 163 ALILQPKIIIADEALAALDMSVRSQIINLMLElQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQ 242
|
....*....
gi 490326802 242 DERTRKFIE 250
Cdd:COG4167 243 HEVTKRLIE 251
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-231 |
1.89e-27 |
|
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: 105.32 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 23 LSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRyenedvwqVSEQERLEYRRSVGMVFQEASL---FDASVRRNA 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVK--------VAGASPGKGWRHIGYVPQRHEFawdFPISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 100 EYGLRVRQSWIDRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSD 179
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVADFAAVR---------DALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490326802 180 LDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNGIIEVG 231
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADG 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-250 |
2.52e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.79 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKST----LLRLLAlfdapDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQE--ASL 90
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 91 fdaSVRRNA----EYGLRVRQSWIDRLRHELSsivgktngtgdAIEALDTVGLR-EKANQDAASLSGGEAQRVAFARALA 165
Cdd:PRK15134 376 ---NPRLNVlqiiEEGLRVHQPTLSAAQREQQ-----------VIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 166 YEPDILLLDEPTSDLDPRNTAVIEDAV--LEAKNRgIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDE 243
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLksLQQKHQ-LAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQE 520
|
....*..
gi 490326802 244 RTRKFIE 250
Cdd:PRK15134 521 YTRQLLA 527
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-238 |
3.25e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.78 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVseqerleyrrSVGMVFQEaslfDASVR 96
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL----------ELGAGFHP----ELTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 RNAE-----YGLRVRQswIDRLRhelssivgktngtgDAIEALdtVGLREKANQDAASLSGGEAQRVAFARALAYEPDIL 171
Cdd:COG1134 107 ENIYlngrlLGLSRKE--IDEKF--------------DEIVEF--AELGDFIDQPVKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 172 LLDEPTS--DLDPRNTAviEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFD 238
Cdd:COG1134 169 LVDEVLAvgDAAFQKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-222 |
1.39e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 103.18 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 8 VHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWqvseQERLEYRRSVGMVF-Q 86
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW----KRRKKFLRRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 EASL-FDASVRRNAEYGLRVRQSWIDRLRHELSSIVgktngtgdaiEALDtvgLREKANQDAASLSGGEAQRVAFARALA 165
Cdd:cd03267 103 KTQLwWDLPVIDSFYLLAAIYDLPPARFKKRLDELS----------ELLD---LEELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 166 YEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-229 |
1.42e-26 |
|
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: 101.62 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYG--AEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerleYRRS 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNaeyglrvrqswidrlrhelssivgktngtgdaiealdtVGLRekanqdaasLSGGEAQRVAF 160
Cdd:cd03247 77 ISVLNQRPYLFDTTLRNN--------------------------------------LGRR---------FSGGERQRLAL 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIgvVIATHDMHQAERiADRVaVLLGNGIIE 229
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvLKDKTL--IWITHHLTGIEH-MDKI-LFLENGKII 175
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
12-237 |
1.67e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.43 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDgVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLE-YRRSVGMVFQ--EA 88
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpVRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 89 SLFDASVRRNAEYGLRvrqswidrlrhelSSIVGKTNGTGDAIEALDTVGL-REKANQDAASLSGGEAQRVAFARALAYE 167
Cdd:PRK13643 96 QLFEETVLKDVAFGPQ-------------NFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 168 PDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-236 |
1.68e-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: 107.20 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVW----QVSEQERLEYRRSVGMVFQEaslfdas 94
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWvdmtKPGPDGRGRAKRYIGILHQE------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 vrrnaeYGLRVRQSWIDRLRHELSSIVGKTNGTGDAIEALDTVGLREKA-----NQDAASLSGGEAQRVAFARALAYEPD 169
Cdd:TIGR03269 374 ------YDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 170 ILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTV 236
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-252 |
1.68e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.48 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKS-TLLRLLALFDAPD----HGSIRYENEDVWQVSEQERLEYR-RSVGMVFQEAS 89
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 90 lfdasVRRNAEYGlrvrqswIDRLRHELSSI---VGKTNGTGDAIEALDTVGLREKANQDAA---SLSGGEAQRVAFARA 163
Cdd:PRK15134 103 -----VSLNPLHT-------LEKQLYEVLSLhrgMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 164 LAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTD 242
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTH 250
|
250
....*....|
gi 490326802 243 ERTRKFIEGE 252
Cdd:PRK15134 251 PYTQKLLNSE 260
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
7-238 |
2.20e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.29 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVF--DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQERLEYRRSVGMV 84
Cdd:PRK13648 12 NVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 85 FQ--EASLFDASVRRNAEYGLRVRQSWIDRLRHELSsivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFAR 162
Cdd:PRK13648 89 FQnpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVS-------------EALKQVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAK-NRGIGVVIATHDMHQAERiADRVAVLLGNGIIEVGDTKTVFD 238
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-232 |
2.84e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.83 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY--GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRS 80
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNaeyglrvrqswidrLRhelssiVGKTNGTGDA-IEALDTVGLREKANQDAA----------S 149
Cdd:PRK11160 416 ISVVSQRVHLFSATLRDN--------------LL------LAAPNASDEAlIEVLQQVGLEKLLEDDKGlnawlgeggrQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 150 LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRgiGVVIATHDMHQAERIaDRVAVLLGNGII 228
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhAQNK--TVLMITHRLTGLEQF-DRICVMDNGQII 552
|
....
gi 490326802 229 EVGD 232
Cdd:PRK11160 553 EQGT 556
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-224 |
2.90e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.16 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR-RSVGMVFQEASLFDA-S 94
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 VRRNAEY-----GLRVRQSwidrlrhelssivgktngTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPD 169
Cdd:PRK10584 105 ALENVELpallrGESSRQS------------------RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 170 ILLLDEPTSDLDPRNTAVIEDaVLEAKNR--GIGVVIATHDMHQAERIADRVAVLLG 224
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIAD-LLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-218 |
3.80e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.47 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEqerleYRRS--VGMVFQEASL---F 91
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-----YKRAkyIGRVFQDPMMgtaP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 DASV--------RRNAEYGLR--VRQSWIDRLRHELSSivgktngtgdaieaLDtVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:COG1101 96 SMTIeenlalayRRGKRRGLRrgLTKKRRELFRELLAT--------------LG-LGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRnTAvieDAVLEAKNR-----GIGVVIATHDMHQAERIADR 218
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPK-TA---ALVLELTEKiveenNLTTLMVTHNMEQALDYGNR 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-236 |
4.80e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 102.37 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 11 AYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerlEYRRSVGMVFQEASL 90
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK---EVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 91 -FDASVRRNAEYGLRVRQSWIDRLRHELSSIVGKtngtgdaieALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPD 169
Cdd:PRK10253 93 pGDITVQELVARGRYPHQPLFTRWRKEDEEAVTK---------AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 170 ILLLDEPTSDLD-PRNTAVIEdaVLEAKNRGIGVVIAT--HDMHQAERIADRVAVLLGNGIIEVGDTKTV 236
Cdd:PRK10253 164 IMLLDEPTTWLDiSHQIDLLE--LLSELNREKGYTLAAvlHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-240 |
5.49e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 104.15 E-value: 5.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERleyrrS 80
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR-----D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLF-DASVRRNAEYGLRVR---QSWIDRLRHELSSIVGktngtgdaIEALdtvgLREKANQdaasLSGGEAQ 156
Cdd:PRK11650 78 IAMVFQNYALYpHMSVRENMAYGLKIRgmpKAEIEERVAEAARILE--------LEPL----LDRKPRE----LSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDP--RNTAVIEdavLEAKNRGIGV--VIATHDMHQAERIADRVAVLLGnGIIE-VG 231
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAklRVQMRLE---IQRLHRRLKTtsLYVTHDQVEAMTLADRVVVMNG-GVAEqIG 217
|
....*....
gi 490326802 232 DTKTVFDNP 240
Cdd:PRK11650 218 TPVEVYEKP 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-231 |
7.25e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.96 E-value: 7.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleyrRSVGMVFQ 86
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 EASLF-DASVRRNAEYGLR---VRQSWID-RLRHelssivgktngtgdAIEALDTVGLREKANQDaasLSGGEAQRVAFA 161
Cdd:PRK11000 83 SYALYpHLSVAENMSFGLKlagAKKEEINqRVNQ--------------VAEVLQLAHLLDRKPKA---LSGGQRQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 162 RALAYEPDILLLDEPTSDLDP--RNTAVIEDAVLEaKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVG 231
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAalRVQMRIEISRLH-KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-241 |
8.39e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.01 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYEN---------EDVWQVSEQERL----EYRRSVGM 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnHELITNPYSKKIknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQ--EASLFDASVRRNAEYG-LRVRQSWIDRlrHELssivgktngtgdAIEALDTVGLREK-ANQDAASLSGGEAQRVA 159
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGpVALGVKKSEA--KKL------------AKFYLNKMGLDDSyLERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD 266
|
..
gi 490326802 240 PT 241
Cdd:PRK13631 267 QH 268
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-246 |
8.69e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.25 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLR-LLALFDAPDhGSIRYENEDVWQVSEQERLEYRRSVGMVFQE--ASLfdaSV 95
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVKATD-GEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASL---NP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 96 RRN-----AEyGLRV------RQSWIDRLRhelssivgktngtgdaiEALDTVGLREKA-NQDAASLSGGEAQRVAFARA 163
Cdd:PRK15079 114 RMTigeiiAE-PLRTyhpklsRQEVKDRVK-----------------AMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 164 LAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVL-LGNGiIEVGDTKTVFDNPT 241
Cdd:PRK15079 176 LILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREMGLSLIFIAHDLAVVKHISDRVLVMyLGHA-VELGTYDEVYHNPL 254
|
....*
gi 490326802 242 DERTR 246
Cdd:PRK15079 255 HPYTK 259
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-244 |
1.27e-25 |
|
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: 100.93 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGS------IRYENEDVWQVseqerle 76
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVWEL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 77 yRRSVGMV-------FQE--------ASLFDASVRRNAEYglrvrqSWIDRLRhelssivgktngtgdAIEALDTVGLRE 141
Cdd:COG1119 77 -RKRIGLVspalqlrFPRdetvldvvLSGFFDSIGLYREP------TDEQRER---------------ARELLELLGLAH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 142 KANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHdmHQAERIA--DR 218
Cdd:COG1119 135 LADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTH--HVEEIPPgiTH 212
|
250 260
....*....|....*....|....*.
gi 490326802 219 VAVLLGNGIIEVGDTKTVFdnpTDER 244
Cdd:COG1119 213 VLLLKDGRVVAAGPKEEVL---TSEN 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-238 |
1.28e-25 |
|
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: 105.21 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYG-AEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqeRLEYRRSV 81
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQEASLFDASVRRNAEYGLR--VRQSWIDRLRhELSSIvgktngtGDAIEALdTVGLREKANQDAASLSGGEAQRVA 159
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLLLGAKenVSQDEIWAAC-EIAEI-------KDDIENM-PLGYQTELSEEGSSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIgVVIAtHDMHQAERiADRVAVLLGNGIIEVGDTKTVFD 238
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTI-IFVA-HRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-222 |
1.41e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.83 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSVGMVFQEASLF-DASVRR 97
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RMGVVRTFQHVRLFrEMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NaeygLRVRQSwidrlRHELSSIVG---KTNG----TGDAIEA----LDTVGLREKANQDAASLSGGEAQRVAFARALAY 166
Cdd:PRK11300 100 N----LLVAQH-----QQLKTGLFSgllKTPAfrraESEALDRaatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 167 EPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-229 |
3.24e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.58 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 15 EPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQERLEYRRSVGMVFQ--EASLFD 92
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIRHKIGMVFQnpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 ASVRRNAEYGLRVRQSwidrlrhELSSIVGKTNgtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:PRK13650 97 ATVEDDVAFGLENKGI-------PHEEMKERVN------EALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 173 LDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAErIADRVAVlLGNGIIE 229
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLV-MKNGQVE 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-237 |
4.34e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.08 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwQVSEQERLEYRRSVG 82
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQ--EASLFDASVRRNAEYGLR---VRQSWIDRLrhelssivgktngTGDAIEALDTVGLREKANQdaaSLSGGEAQR 157
Cdd:PRK13638 81 TVFQdpEQQIFYTDIDSDIAFSLRnlgVPEAEITRR-------------VDEALTLVDAQHFRHQPIQ---CLSHGQKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-244 |
5.72e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 103.27 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY--GAEP--VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR 78
Cdd:PRK10535 5 LELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RS-VGMVFQEASLFD-ASVRRNAEYGlrvrqswidrlrhELSSIVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:PRK10535 85 REhFGFIFQRYHLLShLTAAQNVEVP-------------AVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMH---QAERiadrvavllgngIIEVGDT 233
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQvaaQAER------------VIEIRDG 219
|
250
....*....|.
gi 490326802 234 KTVFDNPTDER 244
Cdd:PRK10535 220 EIVRNPPAQEK 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-248 |
1.07e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.78 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLA--LFdaPDHGSIRYENEDVWqvseQERLEYRRSVGMVF-QEASLF---- 91
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTgiLV--PTSGEVRVLGYVPF----KRRKEFARRIGVVFgQRSQLWwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 --DaSVRRNAE-YglRVRQSWIDRLRHELssivgktngtgdaIEALDtvgLREKANQDAASLSGGEAQRVAFARALAYEP 168
Cdd:COG4586 113 aiD-SFRLLKAiY--RIPDAEYKKRLDEL-------------VELLD---LGELLDTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 169 DILLLDEPTSDLDprntAVIEDAVLEA-----KNRGIGVVIATHDMHQAERIADRVaVLLGNGiievgdtKTVFDNPTDE 243
Cdd:COG4586 174 KILFLDEPTIGLD----VVSKEAIREFlkeynRERGTTILLTSHDMDDIEALCDRV-IVIDHG-------RIIYDGSLEE 241
|
....*
gi 490326802 244 RTRKF 248
Cdd:COG4586 242 LKERF 246
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-239 |
1.10e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 98.93 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERL-----EYRRSVGMVFQEASLFDA-S 94
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLardirKSRANTGYIFQQFNLVNRlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 VRRNAEYGL-------RVRQSWIDRLRHElssivgktngtgDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYE 167
Cdd:PRK09984 103 VLENVLIGAlgstpfwRTCFSWFTREQKQ------------RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 168 PDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTvFDN 239
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FDN 242
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-207 |
2.09e-24 |
|
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: 96.27 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVseqeRLEYRRSVG 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ----RDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDA-SVRRNAEYglrvrqsWIDRLRHELSSIvgktngtgdaIEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:TIGR01189 77 YLGHLPGLKPElSALENLHF-------WAAIHGGAQRTI----------EDALAAVGLTGFEDLPAAQLSAGQQRRLALA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATH 207
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-222 |
2.25e-24 |
|
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: 95.96 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSVGMV----FQEASLFD 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI--RAGIAYVpedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 ASVRRNAeyglrvrqswidrlrhelssivgktngtgdAIEALdtvglrekanqdaasLSGGEAQRVAFARALAYEPDILL 172
Cdd:cd03215 93 LSVAENI------------------------------ALSSL---------------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490326802 173 LDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVM 177
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-240 |
5.63e-24 |
|
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: 95.64 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 13 GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLlrLLALFD--APDHGSIRYENEDVWQVSeqeRLEYRRSVGMVFQEASL 90
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSL--LLALFRlvELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 91 FDASVRRNaeyglrvrqswIDRLrHELSSivgktngtGDAIEALDTVGLREKANQDA-----------ASLSGGEAQRVA 159
Cdd:cd03244 90 FSGTIRSN-----------LDPF-GEYSD--------EELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIgVVIAthdmHQAERIA--DRVAVLLGNGIIEvgdtktv 236
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIREAfKDCTV-LTIA----HRLDTIIdsDRILVLDKGRVVE------- 217
|
....
gi 490326802 237 FDNP 240
Cdd:cd03244 218 FDSP 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-239 |
9.23e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.70 E-value: 9.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvSEQERL-EYRRSVGMVFQ--EASLFD 92
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT---SDEENLwDIRNKAGMVFQnpDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 ASVRRNAEYG---LRVRQSWIdRLRHElssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPD 169
Cdd:PRK13633 101 TIVEEDVAFGpenLGIPPEEI-RERVD---------------ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 170 ILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERiADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKElNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-240 |
1.04e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 97.50 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEP--VFDGVSLSVTPGEVVGIIGPSGVGKS-TLLRLLALFDAPDH---GSIRYENEDVWQVSEQER 74
Cdd:PRK11022 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRvmaEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 75 leyRRSVG----MVFQeaslfDASVRRNAEY--------GLRVRQSWIDRLRHElssivgktngtgDAIEALDTVGLREK 142
Cdd:PRK11022 84 ---RNLVGaevaMIFQ-----DPMTSLNPCYtvgfqimeAIKVHQGGNKKTRRQ------------RAIDLLNQVGIPDP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 143 ANQDAA---SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADR 218
Cdd:PRK11022 144 ASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHK 223
|
250 260
....*....|....*....|..
gi 490326802 219 VAVLLGNGIIEVGDTKTVFDNP 240
Cdd:PRK11022 224 IIVMYAGQVVETGKAHDIFRAP 245
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-234 |
1.38e-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: 92.51 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIryenedvwQVSEQERLEYrrsvg 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTVKIGY----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 mvfqeaslfdasvrrnaeyglrVRQswidrlrhelssivgktngtgdaiealdtvglrekanqdaasLSGGEAQRVAFAR 162
Cdd:cd03221 68 ----------------------FEQ------------------------------------------LSGGEKMRLALAK 83
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNrgiGVVIATHDMHQAERIADRvavllgngIIEVGDTK 234
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATK--------IIELEDGK 144
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-207 |
1.65e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.77 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 13 GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLA--LFDAPDHGSIRYENEDVwqvseqERLEYRRSVGMVFQEASL 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 91 FDAsvrrnaeygLRVRqswidrlrhelssivgktngtgdaiEALD-TVGLRekanqdaaSLSGGEAQRVAFARALAYEPD 169
Cdd:cd03213 94 HPT---------LTVR-------------------------ETLMfAAKLR--------GLSGGERKRVSIALELVSNPS 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 490326802 170 ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATH 207
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-219 |
1.85e-23 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 94.10 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYRRSVG 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEAslfdasvrrnaeyGLRVRQSWIDRLR--HELssivgktNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:cd03231 77 YLGHAP-------------GIKTTLSVLENLRfwHAD-------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVAL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATH-DMHQAERIADRV 219
Cdd:cd03231 137 ARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-222 |
2.05e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 30 VVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYeNEDVWQVSEQE---RLEYRRsVGMVFQEASLF-DASVRRNAEYGL-R 104
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKGiclPPEKRR-IGYVFQDARLFpHYKVRGNLRYGMaK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 105 VRQSWIDRLRHELssivgktngtgdAIEALdtvglrekANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLD-PR 183
Cdd:PRK11144 104 SMVAQFDKIVALL------------GIEPL--------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490326802 184 NTAVIedAVLE--AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK11144 164 KRELL--PYLErlAREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-249 |
2.58e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQE--ASLfdaSVRRN 98
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASL---DPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 99 AEYglrvrqSWIDRLR-HELssivgktnGTGDAIEA-----LDTVGLR-EKANQDAASLSGGEAQRVAFARALAYEPDIL 171
Cdd:PRK10261 420 VGD------SIMEPLRvHGL--------LPGKAAAArvawlLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 172 LLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDERTRKFI 249
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDlQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-222 |
3.84e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 13 GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYrrsvGMVF-----QE 87
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA----GIAYvpedrKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 ASLF-DASVRRN---AEYGLRVRQSWIDRlRHELSSivgktngTGDAIEALDTvglreKA---NQDAASLSGGEAQRVAF 160
Cdd:COG1129 339 EGLVlDLSIRENitlASLDRLSRGGLLDR-RRERAL-------AEEYIKRLRI-----KTpspEQPVGNLSGGNQQKVVL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVM 467
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-222 |
4.77e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.40 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSVGMVFQEASLFDA-SVRR 97
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAI--ALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NAEYGLRVRQSWI---DRLRHELSsivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLD 174
Cdd:COG3845 100 NIVLGLEPTKGGRldrKAARARIR-------------ELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490326802 175 EPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:COG3845 167 EPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-232 |
5.12e-23 |
|
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: 92.59 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDA--PDHGSIRYENEDVWQVSEQERLeyRRS 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERA--RLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDasvrrnaeyGLRVrqswIDRLRhelssivgktngtgdaiealdtvGLREkanqdaaSLSGGEAQRVAF 160
Cdd:cd03217 79 IFLAFQYPPEIP---------GVKN----ADFLR-----------------------YVNE-------GFSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERI-ADRVAVLLGNGIIEVGD 232
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-253 |
6.96e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 93.61 E-value: 6.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKS-TLLRLLALFDA---PDHGSIRYENEDVwqVSEQERleyRRSVGMVFQE 87
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPV--APCALR---GRKIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 A-SLFDAsVRRNAEYGLrvrqswidrlrhELSSIVGKTNGTGDAIEALDTVGLREKA---NQDAASLSGGEAQRVAFARA 163
Cdd:PRK10418 88 PrSAFNP-LHTMHTHAR------------ETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 164 LAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTD 242
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
250
....*....|.
gi 490326802 243 ERTRKFIEGEL 253
Cdd:PRK10418 235 AVTRSLVSAHL 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-208 |
7.45e-23 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 96.93 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGsiryenedvwqvseQERLEYRRSVGMVFQEASLfDAS- 94
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPGIKVGYLPQEPQL-DPTk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 -VRRNAEYGLRVRQSWIDRLrHELSSIVGKTNGTGDAI--------EALDTVGLREKANQ---------------DAASL 150
Cdd:TIGR03719 84 tVRENVEEGVAEIKDALDRF-NEISAKYAEPDADFDKLaaeqaelqEIIDAADAWDLDSQleiamdalrcppwdaDVTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 151 SGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnrgiGVVIA-THD 208
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP----GTVVAvTHD 217
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-228 |
1.12e-22 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 92.46 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDvWQVSEQerleyrRSVG 82
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP-WTRKDL------HKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNaeygLRVRqswidrlrhelSSIVGKTNGTGDaiEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:TIGR03740 74 SLIESPPLYeNLTAREN----LKVH-----------TTLLGLPDSRID--EVLNIVDLTNTGKKKAKQFSLGMKQRLGIA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVlLGNGII 228
Cdd:TIGR03740 137 IALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGI-ISEGVL 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-240 |
1.46e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY-GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQERLEYRRSV 81
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 82 GMVFQ--EASLFDASVRRNAEYGLRVRQSWIDRLRHELSsivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVA 159
Cdd:PRK13652 81 GLVFQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVS-------------SALHMLGLEELRDRVPHHLSGGEKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFD 238
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
..
gi 490326802 239 NP 240
Cdd:PRK13652 228 QP 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-222 |
7.81e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.86 E-value: 7.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYRRSVg 82
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQDL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 mvfqeasLF---DASVRR--NAEYGLRvrqsWIDRLRHELSsivgktngTGDAIEALDTVGLREKANQDAASLSGGEAQR 157
Cdd:PRK13538 77 -------LYlghQPGIKTelTALENLR----FYQRLHGPGD--------DEALWEALAQVGLAGFEDVPVRQLSAGQQRR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIgVVIATHdmHQAERIADRVAVL 222
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGM-VILTTH--QDLPVASDKVRKL 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-241 |
8.19e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErlEYRRSVGMVFQ--EASLFDA 93
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ--GIRKLVGIVFQnpETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 94 SVRRNAEYG--------LRVRQSwIDRlrhelssivgktngtgdaieALDTVGLREKANQDAASLSGGEAQRVAFARALA 165
Cdd:PRK13644 94 TVEEDLAFGpenlclppIEIRKR-VDR--------------------ALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 166 YEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAErIADRVAVLLGNGIIEVGDTKTVFDNPT 241
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-232 |
1.00e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.76 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFdAPDHGSIRYENEdvwQVSEQERLEYRRSVGMVFQEASLFDASVRRN-- 98
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGI---ELRELDPESWRKHLSWVGQNPQLPHGTLRDNvl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 99 --------AEYGLRVRQSWI----DRLRHELSSIVGktngtgdaiealdtvglrekanQDAASLSGGEAQRVAFARALAY 166
Cdd:PRK11174 445 lgnpdasdEQLQQALENAWVseflPLLPQGLDTPIG----------------------DQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 167 EPDILLLDEPTSDLDPRNtaviEDAVLEAKN---RGIGVVIATHDMHQAERIaDRVAVLLGNGIIEVGD 232
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHS----EQLVMQALNaasRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-231 |
1.37e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.16 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAY-GAE-PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvSEQERLEYRRSVGMV 84
Cdd:PRK11176 346 NVTFTYpGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQVALV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 85 FQEASLFDASVRRNAEYGLRVRQSWID-----RLRHELSSIVGKTNGtgdaieaLDTVglrekANQDAASLSGGEAQRVA 159
Cdd:PRK11176 423 SQNVHLFNDTIANNIAYARTEQYSREQieeaaRMAYAMDFINKMDNG-------LDTV-----IGENGVLLSGGQRQRIA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 160 FARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIgVVIAtHDMHQAERiADRVAVLLGNGIIEVG 231
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDElQKNRTS-LVIA-HRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-237 |
1.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEY-RRSVGMVFQ--EASLFDASVRR 97
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvRKRIGMVFQfpESQLFEDTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NAEYGLRVRQSWIDRLRHelssivgktngtgDAIEALDTVGL-REKANQDAASLSGGEAQRVAFARALAYEPDILLLDEP 176
Cdd:PRK13646 106 EIIFGPKNFKMNLDEVKN-------------YAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 177 TSDLDPRN----TAVIEDAVLEaKNRGIgvVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:PRK13646 173 TAGLDPQSkrqvMRLLKSLQTD-ENKTI--ILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-239 |
1.58e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.84 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVF-----DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYEN----EDVWQVSEQERLey 77
Cdd:PRK13645 11 NVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQ--EASLFDASVRRNAEYGlrvrqswidrlrhELSSIVGKTNGTGDAIEALDTVGL-REKANQDAASLSGGE 154
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQETIEKDIAFG-------------PVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 155 AQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDT 233
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
....*.
gi 490326802 234 KTVFDN 239
Cdd:PRK13645 236 FEIFSN 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-242 |
1.62e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.54 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 18 FDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQERLEYRRSVGMVFQ--EASLFDASV 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRKIGMVFQnpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 96 RRNAEYGLR----VRQSWIDRLRhelssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDIL 171
Cdd:PRK13642 100 EDDVAFGMEnqgiPREEMIKRVD-----------------EALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 172 LLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERiADRVAVLLGNGIIEVGDTKTVFDNPTD 242
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-230 |
2.78e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 88.74 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVseqerleyrrSVGMVFQEaslfDASVR 96
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL----------GLGGGFNP----ELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 RNAE-----YGLRVRQswIDRLRHELSSIvgktNGTGDAIEaldtvgLREKanqdaaSLSGGEAQRVAFARALAYEPDIL 171
Cdd:cd03220 103 ENIYlngrlLGLSRKE--IDEKIDEIIEF----SELGDFID------LPVK------TYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 172 LLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRvAVLLGNGIIEV 230
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDR-ALVLEKGKIRF 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-207 |
2.94e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.48 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLL--ALFDAPDHGSIRYENEDVWqvseqerleyrrs 80
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 vgmvfQEASLFDAsvrrnaeyglrvrqswidrlrhelssiVGKTNGTGDAIEALDTVGLREKANQDA--ASLSGGEAQRV 158
Cdd:COG2401 98 -----REASLIDA---------------------------IGRKGDFKDAVELLNAVGLSDAVLWLRrfKELSTGQKFRF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATH 207
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKlARRAGITLVVATH 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-216 |
4.79e-21 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 91.54 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRY-ENEDVWQVsEQER--LEYRR 79
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYV-DQSRdaLDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 80 SvgmVFQEASlfdasvrrnaeYGLRVrqswIDRLRHELSS--IVGKTNGTGDAIEALdtVGlrekanqdaaSLSGGEAQR 157
Cdd:TIGR03719 402 T---VWEEIS-----------GGLDI----IKLGKREIPSraYVGRFNFKGSDQQKK--VG----------QLSGGERNR 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 158 VAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnrGIGVVIaTHDMHQAERIA 216
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVVI-SHDRWFLDRIA 507
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-239 |
7.42e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerLEYRRSVG 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLRVRQSWIDRLRHELSSIvgktngtgdaiealdtvGLREKANQDAASLSGGEAQRVAFA 161
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQLLAAL-----------------GCQLDLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-224 |
7.96e-21 |
|
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: 91.00 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 18 FDGVSLSVTPG-----EVVGIIGPSGVGKSTLLRLLALFDAPDHGSiryenedvwqVSEQERLEYRRsvgmvfQEASlfd 92
Cdd:COG1245 351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGE----------VDEDLKISYKP------QYIS--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 asvrrnAEYGLRVRQSWIDRLRHELSSIVGKTngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:COG1245 412 ------PDYDGTVEEFLRSANTDDFGSSYYKT-------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 173 LDEPTSDLDprntavIEDAVLEAK-------NRGIGVVIATHDMHQAERIADRVAVLLG 224
Cdd:COG1245 479 LDEPSAHLD------VEQRLAVAKairrfaeNRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-243 |
8.57e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.83 E-value: 8.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLL----RLLalfdAPDHGSIRYENEDvwqVSEQERLEYRRSVG 82
Cdd:COG4604 6 NVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLsmisRLL----PPDSGEVLVDGLD---VATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLfdaSVRrnaeygLRVRQswidrL----RHELSSivGKTNGTGDAI--EALDTVGLREKANQDAASLSGGEAQ 156
Cdd:COG4604 79 ILRQENHI---NSR------LTVRE-----LvafgRFPYSK--GRLTAEDREIidEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNtAVIEDAVLE--AKNRGIGVVIATHDMHQAERIADRVaVLLGNGIIevgdtk 234
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKH-SVQMMKLLRrlADELGKTVVIVLHDINFASCYADHI-VAMKDGRV------ 214
|
....*....
gi 490326802 235 tVFDNPTDE 243
Cdd:COG4604 215 -VAQGTPEE 222
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-232 |
1.65e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.04 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDA--PDHGSIRYENEDVWQVSEQERLeyRRS 80
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERA--RAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQeaslfdasvrrnaeY-----GLRVRqswiDRLRHELSSIVGKTNGTGDAI----EALDTVGLREK-ANQDA-AS 149
Cdd:COG0396 79 IFLAFQ--------------YpveipGVSVS----NFLRTALNARRGEELSAREFLkllkEKMKELGLDEDfLDRYVnEG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 150 LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHdmHQaeRI-----ADRVAVLLG 224
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH--YQ--RIldyikPDFVHVLVD 216
|
....*...
gi 490326802 225 NGIIEVGD 232
Cdd:COG0396 217 GRIVKSGG 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-226 |
3.30e-20 |
|
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: 85.21 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 14 AEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIryenedvwqvseqerlEYRRSVGMVFQEASLFDA 93
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV----------------SVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 94 SVRRNAEYGLRVRQSWIDR------LRHELSSIVGktngtGDAIEaldtVGlrEKAnqdaASLSGGEAQRVAFARALAYE 167
Cdd:cd03250 81 TIRENILFGKPFDEERYEKvikacaLEPDLEILPD-----GDLTE----IG--EKG----INLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 168 PDILLLDEPTSDLDPrNTA--VIEDAVLEAKNRGIGVVIATHDMHQAERiADRVaVLLGNG 226
Cdd:cd03250 146 ADIYLLDDPLSAVDA-HVGrhIFENCILGLLLNNKTRILVTHQLQLLPH-ADQI-VVLDNG 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-222 |
5.40e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.55 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVfDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEY----- 77
Cdd:COG3845 260 VENLSVRDDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 ---RRSVGMVfQEASLFDASV---RRNAEYGlrvRQSWIDRlrhelSSIVGKTNgtgDAIEALD--TVGlrekANQDAAS 149
Cdd:COG3845 339 pedRLGRGLV-PDMSVAENLIlgrYRRPPFS---RGGFLDR-----KAIRAFAE---ELIEEFDvrTPG----PDTPARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 150 LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVM 475
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-210 |
6.69e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.55 E-value: 6.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVhhAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRyenedvwqvsEQERLEyrrs 80
Cdd:PRK09544 5 VSLENVSV--SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLR---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLfDASVRRNAEYGLRVRQSwidrlrhelssiVGKtngtGDAIEALDTVGLREKANQDAASLSGGEAQRVAF 160
Cdd:PRK09544 69 IGYVPQKLYL-DTTLPLTVNRFLRLRPG------------TKK----EDILPALKRVQAGHLIDAPMQKLSGGETQRVLL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490326802 161 ARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMH 210
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLH 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-243 |
7.39e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.99 E-value: 7.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRSV-----------GMVFQEAs 89
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA---FARKVaylpqqlpaaeGMTVREL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 90 lfdASVRRNAEYGLRVRQSWIDRLRHElssivgktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPD 169
Cdd:PRK10575 106 ---VAIGRYPWHGALGRFGAADREKVE---------------EAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 170 ILLLDEPTSDLD-PRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPTDE 243
Cdd:PRK10575 168 CLLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-224 |
8.25e-20 |
|
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: 85.15 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPG-----EVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvseqerlEYRRsvgmvfQEASlfda 93
Cdd:cd03237 11 GEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---------SYKP------QYIK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 94 svrrnAEYGLRVRQSwidrlrheLSSIV-GKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:cd03237 72 -----ADYEGTVRDL--------LSSITkDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 173 LDEPTSDLDP----RNTAVIEDAVLEAKNrgiGVVIATHDMHQAERIADRVAVLLG 224
Cdd:cd03237 139 LDEPSAYLDVeqrlMASKVIRRFAENNEK---TAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-208 |
1.45e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 87.48 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPdhgsirYENEDVWQVSeqerleyrRSVGMVFQEASLfDAS- 94
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARPAPG--------IKVGYLPQEPQL-DPEk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 -VRRNAEYGLRVRQSWIDRLrHELSSIVGKTNGTGDAI--------EALDTVGLREKANQ-----DA----------ASL 150
Cdd:PRK11819 86 tVRENVEEGVAEVKAALDRF-NEIYAAYAEPDADFDALaaeqgelqEIIDAADAWDLDSQleiamDAlrcppwdakvTKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 151 SGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnrgiGVVIA-THD 208
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP----GTVVAvTHD 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-231 |
1.61e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 84.24 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 20 GVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDaPDHGSIRyenEDVWQVSEQ-ERLEYRRSVGMVFQeaslFDASVRrn 98
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGGTTS---GQILFNGQPrKPDQFQKCVAYVRQ----DDILLP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 99 aeyGLRVRQSW----IDRLRHELSSIVGKTNgtgDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLD 174
Cdd:cd03234 95 ---GLTVRETLtytaILRLPRKSSDAIRKKR---VEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 175 EPTSDLDPR--NTAVIEDAVLEAKNRGigvVIAThdMHQAE----RIADRVAVLLGNGIIEVG 231
Cdd:cd03234 169 EPTSGLDSFtaLNLVSTLSQLARRNRI---VILT--IHQPRsdlfRLFDRILLLSSGEIVYSG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-236 |
2.40e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEqeRLEYRRSVGMVFQEASLFDA-SVRR 97
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDH--KLAAQLGIGIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NAEYG-LRVRQSW-IDrlrhelssIVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDE 175
Cdd:PRK09700 100 NLYIGrHLTKKVCgVN--------IIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 176 PTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTV 236
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-224 |
2.43e-19 |
|
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: 84.34 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAepvfDGVSL----SVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGsiRYENEDVWQvseqERLEYRRsvG 82
Cdd:cd03236 5 EPVHRYGP----NSFKLhrlpVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWD----EILDEFR--G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQE--ASLFDASVRrnaeygLRVRQSWIDRLRHELSSIVG----KTNGTGDAIEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:cd03236 73 SELQNyfTKLLEGDVK------VIVKPQYVDLIPKAVKGKVGellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLG 224
Cdd:cd03236 147 RVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-231 |
2.76e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 83.23 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVsEQERLeyRRSVG 82
Cdd:cd03369 9 VENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDL--RSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDASVRRNaeygLRVRQSWIDRlrhelssivgktngtgDAIEALdtvglreKANQDAASLSGGEAQRVAFAR 162
Cdd:cd03369 86 IIPQDPTLFSGTIRSN----LDPFDEYSDE----------------EIYGAL-------RVSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERIA--DRVAVLLGNGIIEVG 231
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIA----HRLRTIIdyDKILVMDAGEVKEYD 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-238 |
2.82e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 20 GVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFdAPDHGSIRYENEDV--WQVSEQERleyRRSV---------GM-VFQE 87
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLsdWSAAELAR---HRAYlsqqqsppfAMpVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 ASLFDASVrrnaeyglrVRQSWIDRLRHELSsivgktngtgdaiEALdtvGLREKANQDAASLSGGEAQRVAFARAL--- 164
Cdd:COG4138 90 LALHQPAG---------ASSEAVEQLLAQLA-------------EAL---GLEDKLSRPLTQLSGGEWQRVRLAAVLlqv 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 165 --AYEPD--ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNG-IIEVGDTKTVFD 238
Cdd:COG4138 145 wpTINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRV-WLLKQGkLVASGETAEVMT 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-224 |
2.93e-19 |
|
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: 86.38 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 27 PGEVVGIIGPSGVGKSTLLRLLALFDAPDHGsiRYENEDVWQvseqERLEYrrsvgmvFQEASLFDaSVRRNAEYGLRVR 106
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG--DYDEEPSWD----EVLKR-------FRGTELQD-YFKKLANGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 107 Q--SWIDRLRHELSSIVG----KTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDL 180
Cdd:COG1245 164 HkpQYVDLIPKVFKGTVRelleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490326802 181 DPR---NTA-VIEDAVLEAKNrgigVVIATHDMHQAERIADRVAVLLG 224
Cdd:COG1245 244 DIYqrlNVArLIRELAEEGKY----VLVVEHDLAILDYLADYVHILYG 287
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
3.52e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHhaYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDV--WQVSEQerleYR 78
Cdd:PRK11614 6 LSFDKVSAH--YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdWQTAKI----MR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQEASLFDasvRRNAEYGLRVRQSWIDRLRHElssivgktngtgDAIEALDTV--GLREKANQDAASLSGGEAQ 156
Cdd:PRK11614 80 EAVAIVPEGRRVFS---RMTVEENLAMGGFFAERDQFQ------------ERIKWVYELfpRLHERRIQRAGTMSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 157 RVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVlLGNGIIEVGDT 233
Cdd:PRK11614 145 MLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYV-LENGHVVLEDT 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-224 |
8.01e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 85.25 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 18 FDGVSLSVTPG-----EVVGIIGPSGVGKSTLLRLLALFDAPDHGSiryenedvwqVSEQERLEYRRsvgmvfQEASlfd 92
Cdd:PRK13409 350 LGDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE----------VDPELKISYKP------QYIK--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 asvrrnAEYGLRVRQSwidrlrheLSSIVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:PRK13409 411 ------PDYDGTVEDL--------LRSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 173 LDEPTSDLDprntavIEDAVLEAK-------NRGIGVVIATHDMHQAERIADRVAVLLG 224
Cdd:PRK13409 477 LDEPSAHLD------VEQRLAVAKairriaeEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-252 |
9.06e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEP---VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALF-DAPDHGSIRYENEDVWQVS--EQERLE 76
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTneQDYQGD 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 77 YRRSVGM------------------------------------------------VFQEASLFDASVRRNAEYGLRvrqs 108
Cdd:PTZ00265 1246 EEQNVGMknvnefsltkeggsgedstvfknsgkilldgvdicdynlkdlrnlfsiVSQEPMLFNMSIYENIKFGKE---- 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 109 wiDRLRHELSSiVGKTNGTGDAIEAL----DT-VGLREKanqdaaSLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPR 183
Cdd:PTZ00265 1322 --DATREDVKR-ACKFAAIDEFIESLpnkyDTnVGPYGK------SLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 184 NTAVIEDAVLEAKNRGIGVVIAthdmhqaerIADRVAVllgngiIEVGDTKTVFDNPtdERTRKFIEGE 252
Cdd:PTZ00265 1393 SEKLIEKTIVDIKDKADKTIIT---------IAHRIAS------IKRSDKIVVFNNP--DRTGSFVQAH 1444
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-195 |
1.47e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGaEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLAlfdapdhgsiryeneDVWQvSEQERLEYRRS 80
Cdd:COG4178 363 LALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---------------GLWP-YGSGRIARPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVF--QEASLFDASVRRNAEYGLRVRQSWIDRLRHELSSIvgktnGTGDAIEALDTVGLREKanqdaaSLSGGEAQRV 158
Cdd:COG4178 426 ARVLFlpQRPYLPLGTLREALLYPATAEAFSDAELREALEAV-----GLGHLAERLDEEADWDQ------VLSLGEQQRL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNtaviEDAVLEA 195
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEEN----EAALYQL 527
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-224 |
2.25e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.09 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 25 VTPGEVVGIIGPSGVGKSTLLRLLAlfdapdhGSI-----RYENEDVWQvseqERLEYrrsvgmvFQEASLFDaSVRRNA 99
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------GELipnlgDYEEEPSWD----EVLKR-------FRGTELQN-YFKKLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 100 EYGLRVRQ--SWIDRLRHELSSIVG----KTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLL 173
Cdd:PRK13409 157 NGEIKVVHkpQYVDLIPKVFKGKVRellkKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490326802 174 DEPTSDLDPRNTAVIEDAVLE-AKNRgiGVVIATHDMHQAERIADRVAVLLG 224
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRElAEGK--YVLVVEHDLAVLDYLADNVHIAYG 286
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-246 |
2.40e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 6 IDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKS-TLLRLLALFDAP------DHGSIRYENEDVWQVSEQERLEYR 78
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvqcDKMLLRRRSRQVIELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVG----MVFQE--ASLFDA-SVRRNAEYGLRVRQSwidrlrhelssiVGKTNGTGDAIEALDTVGLREKA---NQDAA 148
Cdd:PRK10261 100 HVRGadmaMIFQEpmTSLNPVfTVGEQIAESIRLHQG------------ASREEAMVEAKRMLDQVRIPEAQtilSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIED--AVLEaKNRGIGVVIATHDMHQAERIADRVAVLLGNG 226
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQ-KEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260
....*....|....*....|
gi 490326802 227 IIEVGDTKTVFDNPTDERTR 246
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTR 266
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-181 |
2.52e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 83.79 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRY-ENEDVW---QVSEQErleyr 78
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsENANIGyyaQDHAYD----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 rsvgmvF-QEASLFDasvrrnaeyglrvrqsWIDRLRHE------LSSIVGKTNGTGDAIealdtvglrekaNQDAASLS 151
Cdd:PRK15064 395 ------FeNDLTLFD----------------WMSQWRQEgddeqaVRGTLGRLLFSQDDI------------KKSVKVLS 440
|
170 180 190
....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLD 181
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-251 |
4.00e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.99 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIryenedvwqVSEQERLEY----RRS--VGMVFQEAS----- 89
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL---------LIDDHPLHFgdysYRSqrIRMIFQDPStslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 90 ------LFDASVRRNAEYGLRVRQSWIdrlrhelssivgktngtgdaIEALDTVGLR-EKANQDAASLSGGEAQRVAFAR 162
Cdd:PRK15112 103 rqrisqILDFPLRLNTDLEPEQREKQI--------------------IETLRQVGLLpDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPT 241
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
250
....*....|
gi 490326802 242 DERTRKFIEG 251
Cdd:PRK15112 243 HELTKRLIAG 252
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-214 |
8.84e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYR-------- 78
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRiaympqgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 -RsvgmvfqeaSLF-DASVRRNAE-----YGL--RVRQSWIDRLrhelssivgktngtgdaieaLDTVGLREKANQDAAS 149
Cdd:NF033858 86 gK---------NLYpTLSVFENLDffgrlFGQdaAERRRRIDEL--------------------LRATGLAPFADRPAGK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 150 LSGGEAQRVAFARALAYEPDILLLDEPTSDLDP--RNT--AVIEDavLEAKNRGIGVVIATHDMHQAER 214
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsRRQfwELIDR--IRAERPGMSVLVATAYMEEAER 203
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
3-232 |
1.08e-17 |
|
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: 79.61 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLAlfDAPD----HGSIRYENEDVWQVSEQERLeyR 78
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIA--GHPSyevtSGTILFKGQDLLELEPDERA--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQeASLFDASVRrNAEYglrvrqswidrLRHELSSIVGKTNGtgDAIEALDTVGL----REKANQDAASL---- 150
Cdd:TIGR01978 77 AGLFLAFQ-YPEEIPGVS-NLEF-----------LRSALNARRSARGE--EPLDLLDFEKLlkekLALLDMDEEFLnrsv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 151 ----SGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIA-DRVAVLLGN 225
Cdd:TIGR01978 142 negfSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDG 221
|
....*..
gi 490326802 226 GIIEVGD 232
Cdd:TIGR01978 222 RIVKSGD 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-249 |
1.23e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 80.62 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 6 IDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFdAPDHGSI-----RYENEDVWQVSEQERleyRRS 80
Cdd:PRK15093 11 IEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVtadrmRFDDIDLLRLSPRER---RKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VG----MVFQEA-SLFDASVRrnaeYGLRVRQS---------WIDRLRHELSSivgktngtgdAIEALDTVGLreKANQD 146
Cdd:PRK15093 87 VGhnvsMIFQEPqSCLDPSER----VGRQLMQNipgwtykgrWWQRFGWRKRR----------AIELLHRVGI--KDHKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 147 AAS-----LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA-KNRGIGVVIATHDMHQAERIADRVA 220
Cdd:PRK15093 151 AMRsfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKIN 230
|
250 260
....*....|....*....|....*....
gi 490326802 221 VLLGNGIIEVGDTKTVFDNPTDERTRKFI 249
Cdd:PRK15093 231 VLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-222 |
1.24e-17 |
|
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: 82.37 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 6 IDVHHAYGaEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYRRSVGMVF 85
Cdd:TIGR01257 935 VKIFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLFD-ASVRRNAEYGLRVR-QSWiDRLRHELSSIvgktngtgdaieaLDTVGLREKANQDAASLSGGEAQRVAFARA 163
Cdd:TIGR01257 1010 QHNILFHhLTVAEHILFYAQLKgRSW-EEAQLEMEAM-------------LEDTGLHHKRNEEAQDLSGGMQRKLSVAIA 1075
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 164 LAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNrGIGVVIATHDMHQAERIADRVAVL 222
Cdd:TIGR01257 1076 FVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAII 1133
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-216 |
1.33e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 81.70 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYeNEDVwQVS--EQER--LEYR 78
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-KLAyvDQSRdaLDPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSvgmVFQEASlfdasvrrnaeYGLRVrqswIDRLRHELSS--IVGKTNGTGdaiealdtvglrekANQD--AASLSGGE 154
Cdd:PRK11819 403 KT---VWEEIS-----------GGLDI----IKVGNREIPSraYVGRFNFKG--------------GDQQkkVGVLSGGE 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 155 AQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKnrGIGVVIaTHDMHQAERIA 216
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFP--GCAVVI-SHDRWFLDRIA 509
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-226 |
2.66e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLL-RLLALFDAPdhGSIRYENEDV--WQVSEQERleYR-------RSVGM--VFQEA 88
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLLPGS--GSIQFAGQPLeaWSAAELAR--HRaylsqqqTPPFAmpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 89 SLFDASVRRNAEyglrvrqswidrLRHELSSIVGKtngtgdaiealdtVGLREKANQDAASLSGGEAQRVAFARA-LAYE 167
Cdd:PRK03695 91 TLHQPDKTRTEA------------VASALNEVAEA-------------LGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVW 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 168 PDI------LLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVaVLLGNG 226
Cdd:PRK03695 146 PDInpagqlLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRV-WLLKQG 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-222 |
3.74e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEyrRSVGMVFQEASLFDA-SVRR 97
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--AGIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NAEYGLRVRQSW--IDRlrhelssivGKTNGTGDAIeaLDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDE 175
Cdd:PRK10762 99 NIFLGREFVNRFgrIDW---------KKMYAEADKL--LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490326802 176 PTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK10762 168 PTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-240 |
4.16e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.18 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRllALFDAPDHGSI------RYENEDVWQVSEQERLEY-RRSVGMVFQEA-SL 90
Cdd:COG4170 24 DRVSLTLNEGEIRGLVGESGSGKSLIAK--AICGITKDNWHvtadrfRWNGIDLLKLSPRERRKIiGREIAMIFQEPsSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 91 FDASVR---------RNAEYGLRVRQSWIDRLRHelssivgktngtgdAIEALDTVGLRE-KA--NQDAASLSGGEAQRV 158
Cdd:COG4170 102 LDPSAKigdqlieaiPSWTFKGKWWQRFKWRKKR--------------AIELLHRVGIKDhKDimNSYPHELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVF 237
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247
|
...
gi 490326802 238 DNP 240
Cdd:COG4170 248 KSP 250
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-219 |
6.41e-17 |
|
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: 79.46 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAY---GAEPVFD-G-VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQERLE 76
Cdd:COG4615 327 TLELRGVTYRYpgeDGDEGFTlGpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 77 YRR--SVgmVFQEASLFDasvrRNaeYGL-------RVRQsWIDRLrhELSSIVGKTNGtgdaieALDTVglrekanqda 147
Cdd:COG4615 404 YRQlfSA--VFSDFHLFD----RL--LGLdgeadpaRARE-LLERL--ELDHKVSVEDG------RFSTT---------- 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 148 aSLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVL-EAKNRGIGVVIATHDmhqaER---IADRV 219
Cdd:COG4615 457 -DLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELLpELKARGKTVIAISHD----DRyfdLADRV 527
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-222 |
1.85e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLL-ALFdaPdHGSirYENEDVWQVSEQE----RLEY 77
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsGVY--P-HGT--YEGEIIFEGEELQasniRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 78 RRSVGMVFQEASLF-DASVRRNAEYGlrvrqswidrlrHELSsivgkTNGTGD-------AIEALDTVGLREKANQDAAS 149
Cdd:PRK13549 81 RAGIAIIHQELALVkELSVLENIFLG------------NEIT-----PGGIMDydamylrAQKLLAQLKLDINPATPVGN 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 150 LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVI 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-222 |
2.18e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.85 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEyrRSVGMVFQEASLfdasvrrn 98
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE--NGISMVHQELNL-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 99 aeyglrVRQ-SWIDRL---RHELSSI-VGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLL 173
Cdd:PRK10982 85 ------VLQrSVMDNMwlgRYPTKGMfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490326802 174 DEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-231 |
2.26e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.40 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAepVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLA-LFDAPDH-------GSIRYENEDVWQVSEQ 72
Cdd:PRK13547 2 LTADHLHVARRHRA--ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 73 eRLEYRRSVgMVFQEASLFDASVRRNAEYGlrvrqswidRLRHELSSIVGKTNGTGDAIEALDTVGLREKANQDAASLSG 152
Cdd:PRK13547 80 -RLARLRAV-LPQAAQPAFAFSAREIVLLG---------RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 153 GEAQRVAFARALAY---------EPDILLLDEPTSDLDPRNTAVIEDAVLE-AKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK13547 149 GELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRlARDWNLGVLAIVHDPNLAARHADRIAML 228
|
....*....
gi 490326802 223 LGNGIIEVG 231
Cdd:PRK13547 229 ADGAIVAHG 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-222 |
2.38e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 18 FDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEyrrsVGMVF-----QEASLF- 91
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA----RGLVYlpedrQSSGLYl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 DASVRRNAeYGLRVRQS--WIDRlrhelssivGKTNGTGDAIEAldTVGLR-EKANQDAASLSGGEAQRVAFARALAYEP 168
Cdd:PRK15439 355 DAPLAWNV-CALTHNRRgfWIKP---------ARENAVLERYRR--ALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490326802 169 DILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-222 |
2.93e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEyrRSVGMVFQEASLF-DASVRR 97
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA--AGVAIIYQELHLVpEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 NAEYG-LRVRQSWIDR--LRHElssivgktngtgdAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLD 174
Cdd:PRK11288 99 NLYLGqLPHKGGIVNRrlLNYE-------------AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490326802 175 EPTSDLDPRNT----AVIEDavLEAKNRGIGVViaTHDMHQAERIADRVAVL 222
Cdd:PRK11288 166 EPTSSLSAREIeqlfRVIRE--LRAEGRVILYV--SHRMEEIFALCDAITVF 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-241 |
4.74e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.32 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAY--GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSeqeRLEYRRSVGMV 84
Cdd:PLN03232 1239 DVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSII 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 85 FQEASLFDASVRRNAEYGLRVRQS--WIDRLRHELSSIVGKtngtgdaiealDTVGLREKANQDAASLSGGEAQRVAFAR 162
Cdd:PLN03232 1316 PQSPVLFSGTVRFNIDPFSEHNDAdlWEALERAHIKDVIDR-----------NPFGLDAEVSEGGENFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERI--ADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA----HRLNTIidCDKILVLSSGQVLEYDSPQELLSRD 1460
|
.
gi 490326802 241 T 241
Cdd:PLN03232 1461 T 1461
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-205 |
6.51e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYEneDVWQVSEQERLEYRRSVGMVFQEASLFDASVR 96
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 RNAEY------------------------GLRVRQSWIDRLRHELSSIVGKTNGTG--------DAIEALDTVGLREKA- 143
Cdd:PTZ00265 478 NNIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAGDLNDMSNTTDSNEliemrknyQTIKDSEVVDVSKKVl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 144 ----------------NQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAV--LEAKNRGIGVVIA 205
Cdd:PTZ00265 558 ihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIA 637
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-231 |
6.66e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 7 DVHHAYGAE-PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRSVGMVF 85
Cdd:PRK10790 345 NVSFAYRDDnLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV---LRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 86 QEASLFDASVRRNAEYGLRVR--QSWIDRLRHELSSIVgktNGTGDAIEALdtvgLREKANqdaaSLSGGEAQRVAFARA 163
Cdd:PRK10790 422 QDPVVLADTFLANVTLGRDISeeQVWQALETVQLAELA---RSLPDGLYTP----LGEQGN----NLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 164 LAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERI--ADRVAVLLGNGIIEVG 231
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA----HRLSTIveADTILVLHRGQAVEQG 556
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-181 |
8.06e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.53 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 11 AYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqVSeqeRLEY---RRSVGMVFQE 87
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI--VA---RLQQdppRNVEGTVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 ASlfdASVRRNAEY-------GLRVRQSWIDRLRHELSSIVGKTNGTG-----DAI-EALDTVGLreKANQDAASLSGGE 154
Cdd:PRK11147 87 VA---EGIEEQAEYlkryhdiSHLVETDPSEKNLNELAKLQEQLDHHNlwqleNRInEVLAQLGL--DPDAALSSLSGGW 161
|
170 180
....*....|....*....|....*..
gi 490326802 155 AQRVAFARALAYEPDILLLDEPTSDLD 181
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-241 |
1.00e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.15 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 24 SVTPGEVVGIIGPSGVGKS-TLLRLLALFDAPDH--GSIRYENEDVWQVSEQERLEYR-RSVGMVFQeaslfDASVRRNA 99
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPEKELNKLRaEQISMIFQ-----DPMTSLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 100 eYgLRVRQSWIDRLRheLSSIVGKTNGTGDAIEALDTVGL---REKANQDAASLSGGEAQRVAFARALAYEPDILLLDEP 176
Cdd:PRK09473 113 -Y-MRVGEQLMEVLM--LHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490326802 177 TSDLDPRNTAVIEDAVLEAKNR-GIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDNPT 241
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-222 |
1.71e-15 |
|
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: 75.25 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLAlfDAPDHGSirYENEDVWQVSEQE----RLEYR 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS--GVYPHGT--WDGEIYWSGSPLKasniRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQEASLF-DASVRRNAEYGlrvrqswidrlrHELSSIVGKTNG---TGDAIEALDTVGLREKAN-QDAASLSGG 153
Cdd:TIGR02633 78 AGIVIIHQELTLVpELSVAENIFLG------------NEITLPGGRMAYnamYLRAKNLLRELQLDADNVtRPVGDYGGG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 154 EAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-240 |
2.01e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.13 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLA-LFDAPDhGSIRYENEDVWQVseqeRL-EYRRSVGMVFQEASLFDA 93
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDVSE-GDIRFHDIPLTKL----QLdSWRSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 94 SVRRNAEyglrvrqswidrlrhelssiVGKTNGTGDAIEA---LDTV---------GLREKANQDAASLSGGEAQRVAFA 161
Cdd:PRK10789 404 TVANNIA--------------------LGRPDATQQEIEHvarLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAvLEAKNRGIGVVIATHDMhQAERIADRVAVLLGNGIIEVGDTKTVFDNP 240
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
12-222 |
1.60e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.08 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLlRLLALFDAPDHGSiRYENEDVWQVSeqeRLEYRRSVGMvfqeaslf 91
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR-RPWRF*TWCAN---RRALRRTIG*-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 DASVR--RNAEYGLRVRQSWIDRLRHelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPD 169
Cdd:NF000106 90 HRPVR*gRRESFSGRENLYMIGR*LD-----LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490326802 170 ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVI 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-222 |
2.26e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLAlfDAPDHGSirYENEDVWQVSEQERLEYRRS--VGMVF--QEASLF-DA 93
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLS--GVYPHGS--YEGEILFDGEVCRFKDIRDSeaLGIVIihQELALIpYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 94 SVRRNAEYG-LRVRQSWIDRLRhelssivgkTNGtgDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:NF040905 94 SIAENIFLGnERAKRGVIDWNE---------TNR--RARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490326802 173 LDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVL 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-184 |
3.06e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.58 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRL------------LALFdapdhGSIRYENEDVWQ-------VSEQ 72
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLF-----GRRRGSGETIWDikkhigyVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 73 ERLEYR-----RSVGMvfqeASLFDAsvrrnaeygLRVRQSWIDRLRHElssivgktngtgdAIEALDTVGLREK-ANQD 146
Cdd:PRK10938 345 LHLDYRvstsvRNVIL----SGFFDS---------IGIYQAVSDRQQKL-------------AQQWLDILGIDKRtADAP 398
|
170 180 190
....*....|....*....|....*....|....*....
gi 490326802 147 AASLSGGEaQRVAF-ARALAYEPDILLLDEPTSDLDPRN 184
Cdd:PRK10938 399 FHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLN 436
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-218 |
3.40e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 2 TLEAIDVHHAYGaEPVFD--GVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvwQVSEQERLEYRR 79
Cdd:PRK10522 322 TLELRNVTFAYQ-DNGFSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 80 SVGMVFQEASLFDASVRRNAEYGLRVR-QSWIDRLrhELSSIVGKTNGtgdaiEALDTvglrekanqdaaSLSGGEAQRV 158
Cdd:PRK10522 398 LFSAVFTDFHLFDQLLGPEGKPANPALvEKWLERL--KMAHKLELEDG-----RISNL------------KLSKGQKKRL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 159 AFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVL-EAKNRGIGVVIATHDMHQAERiADR 218
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRREFYQVLLpLLQEMGKTIFAISHDDHYFIH-ADR 518
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-181 |
3.95e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 20 GVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPD---HGSIRYENE--DVWQVseQERLEYRRSVGMVF-----QEAS 89
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpiDAKEM--RAISAYVQQDDLFIptltvREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 90 LFDASVRRNAEYGLRVRQSWIDrlrhelssivgktngtgdaiEALDTVGLREKAN------QDAASLSGGEAQRVAFARA 163
Cdd:TIGR00955 121 MFQAHLRMPRRVTKKEKRERVD--------------------EVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASE 180
|
170
....*....|....*...
gi 490326802 164 LAYEPDILLLDEPTSDLD 181
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLD 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-229 |
6.50e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLR-LLALFDApDHGSiryenedVWQvseqerleyRRSVGMVFQEASLFDASVRRNA 99
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEI-SEGR-------VWA---------ERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 100 EY-----------GLRVRQswidrLRHELSSIVGktngtgdaiealdtvGLREKANQDAASLSGGEAQRVAFARALAYEP 168
Cdd:PTZ00243 742 LFfdeedaarladAVRVSQ-----LEADLAQLGG---------------GLETEIGEKGVNLSGGQKARVSLARAVYANR 801
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 169 DILLLDEPTSDLDPR-NTAVIEDAVLEAKnRGIGVVIATHDMHQAERiADRVaVLLGNGIIE 229
Cdd:PTZ00243 802 DVYLLDDPLSALDAHvGERVVEECFLGAL-AGKTRVLATHQVHVVPR-ADYV-VALGDGRVE 860
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-238 |
7.50e-14 |
|
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: 71.13 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 5 AIDVHH-----AYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLalfdapdhgsiryenedvwqVSEQERLE--- 76
Cdd:TIGR00957 636 SITVHNatftwARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--------------------LAEMDKVEghv 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 77 -YRRSVGMVFQEASLFDASVRRNAEYGLRVRQSWIDRLRHELSSIVGktngtgdaIEALDTvGLREKANQDAASLSGGEA 155
Cdd:TIGR00957 696 hMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPD--------LEILPS-GDRTEIGEKGVNLSGGQK 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAV------LEAKNRgigvVIATHDMHQAERIaDRVAVLLGNGIIE 229
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpegvLKNKTR----ILVTHGISYLPQV-DVIIVMSGGKISE 841
|
....*....
gi 490326802 230 VGDTKTVFD 238
Cdd:TIGR00957 842 MGSYQELLQ 850
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-226 |
1.01e-13 |
|
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: 67.18 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 22 SLSVTPGEVVGIIGPSGVGKSTLLRLLAlfdapdhgsiryeneDVWQVseqerleYRRSVGMVFQEASLFDAsvrrnaey 101
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALA---------------GLWPW-------GSGRIGMPEGEDLLFLP-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 102 glrvRQSWIdrlrhelssivgkTNGTgdaiealdtvgLREKAN---QDAasLSGGEAQRVAFARALAYEPDILLLDEPTS 178
Cdd:cd03223 71 ----QRPYL-------------PLGT-----------LREQLIypwDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490326802 179 DLDPRNtaviEDAVLEA-KNRGIGVVIATHDmHQAERIADRVAVLLGNG 226
Cdd:cd03223 121 ALDEES----EDRLYQLlKELGITVISVGHR-PSLWKFHDRVLDLDGEG 164
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-244 |
1.35e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 22 SLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQEASLFDASVRRNAEY 101
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 102 GlrvRQSWIDRLRHELSSIVGktngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLD 181
Cdd:PRK15056 107 G---HMGWLRRAKKRDRQIVT---------AALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 182 PRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNgIIEVGDTKTVFDNPTDER 244
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGT-VLASGPTETTFTAENLEL 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-223 |
2.42e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 14 AEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVW-QVSEqerleYRRSVGMVFQEASLFD 92
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILtNISD-----VHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 ASVRRNAEYglrvrqsWIDRLRHELSSIVGKTNGTGdaieaLDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:TIGR01257 2026 LLTGREHLY-------LYARLRGVPAEEIEKVANWS-----IQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490326802 173 LDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLL 223
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMV 2144
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-188 |
4.15e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.78 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLaLFDAPDHGSIRYENEDVWQVSEQerlEYRRS 80
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL-LRLLSTEGEIQIDGVSWNSVTLQ---TWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQEASLFDASVRRNaeygLRVRQSWIDRlrhELSSIVgktngtgdaiealDTVGLREKANQ-----------DAAS 149
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKN----LDPYEQWSDE---EIWKVA-------------EEVGLKSVIEQfpdkldfvlvdGGYV 1353
|
170 180 190
....*....|....*....|....*....|....*....
gi 490326802 150 LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVI 188
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQII 1392
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-195 |
4.22e-13 |
|
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: 67.19 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLR-LLALFDApdHGSIRYENEDVWQVSEQerlEYRR 79
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLNT--EGDIQIDGVSWNSVPLQ---KWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 80 SVGMVFQEASLFDASVRRNAE-YGlrvrqSWIDRlrhELSSIVgktngtgdaiealDTVGLREKANQ-----------DA 147
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDpYG-----KWSDE---EIWKVA-------------EEVGLKSVIEQfpgqldfvlvdGG 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490326802 148 ASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEA 195
Cdd:cd03289 137 CVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQA 184
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-241 |
6.04e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 15 EPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRllALFDAPDHgsiryenedvwqvSEQERLEYRRSVGMVFQEASLFDAS 94
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS--AMLGELSH-------------AETSSVVIRGSVAYVPQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 VRRNAEYGLRVRQS--W--ID--RLRHELSSIVGKTngtgdaieaLDTVGLRekanqdAASLSGGEAQRVAFARALAYEP 168
Cdd:PLN03232 695 VRENILFGSDFESEryWraIDvtALQHDLDLLPGRD---------LTEIGER------GVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 169 DILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMH---QAERIadrvaVLLGNGII-EVGDTKTVFDNPT 241
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHflpLMDRI-----ILVSEGMIkEEGTFAELSKSGS 831
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-224 |
6.73e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVG 82
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLFDASVRRNAEYGLRVRQswidrlrhelssivgkTNGTgdaieALDTVGLREKANQDAASLSGGEAQRVAFAR 162
Cdd:PRK13543 92 GLKADLSTLENLHFLCGLHGRRAKQ----------------MPGS-----ALAIVGLAGYEDTLVRQLSAGQKKRLALAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 163 ALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLG 224
Cdd:PRK13543 151 LWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-220 |
1.57e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLL-----------ALFDAP-DHGSIryenedvwqvseqerlEYRRSVGMVFQ 86
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtgllpasegeaWLFGQPvDAGDI----------------ATRRRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 87 EASLfdasvrrnaeYG-LRVRQSwID---RLRHelssiVGKTNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFAR 162
Cdd:NF033858 347 AFSL----------YGeLTVRQN-LElhaRLFH-----LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 163 ALAYEPDILLLDEPTSDLDPrntaVIEDAVLE-----AKNRGIGVVIATHDMHQAERiADRVA 220
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDP----VARDMFWRllielSREDGVTIFISTHFMNEAER-CDRIS 468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-240 |
3.27e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 4 EAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQErleYRRSVGM 83
Cdd:PTZ00243 1312 EGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQEASLFDASVRRNAEYGLrvrqswidrlrhELSSivgktngtGDAIEALDTVGLREKANQ-----DAASLSGG----- 153
Cdd:PTZ00243 1389 IPQDPVLFDGTVRQNVDPFL------------EASS--------AEVWAALELVGLRERVASesegiDSRVLEGGsnysv 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 154 -EAQRVAFARALAYE-PDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAtHDMHQAERIaDRVAVLLGNGIIEVG 231
Cdd:PTZ00243 1449 gQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIA-HRLHTVAQY-DKIIVMDHGAVAEMG 1526
|
....*....
gi 490326802 232 DTKTVFDNP 240
Cdd:PTZ00243 1527 SPRELVMNR 1535
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-222 |
8.05e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLL--ALfdAPDHGSIRYENEDVWQVSEQERL--------EYRRSVGMVFqea 88
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLygAL--PRTSGYVTLDGHEVVTRSPQDGLangivyisEDRKRDGLVL--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 89 slfDASVRRNAEyglrvrqswIDRLRHeLSSIVGKTNGTGDAIEALDTVGL----REKANQDAASLSGGEAQRVAFARAL 164
Cdd:PRK10762 344 ---GMSVKENMS---------LTALRY-FSRAGGSLKHADEQQAVSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGL 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 165 AYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-239 |
1.04e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDvwqVSEQERLEYRRSVGMVFQEASLFDASV 95
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCD---ISKFGLMDLRKVLGIIPQAPVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 96 RRN---------AEYglrvrqsWIDRLRHELSSIVGKtngtgdaiealDTVGLREKANQDAASLSGGEAQRVAFARALAY 166
Cdd:PLN03130 1330 RFNldpfnehndADL-------WESLERAHLKDVIRR-----------NSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 167 EPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERI--ADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIA----HRLNTIidCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-219 |
1.07e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.42 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 13 GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEdvWQVS---------EQERLEYRRSVGM 83
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN--WQLAwvnqetpalPQPALEYVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 84 VFQ--EASLFDASVRRNAeyglrvrqswidrlrHELSSIVGKTngtgDAIEA----------LDTVGL-REKANQDAASL 150
Cdd:PRK10636 90 EYRqlEAQLHDANERNDG---------------HAIATIHGKL----DAIDAwtirsraaslLHGLGFsNEQLERPVSDF 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 151 SGGEAQRVAFARALAYEPDILLLDEPTSDLDprntaviEDAV--LEA--KNRGIGVVIATHDMHQAERIADRV 219
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAViwLEKwlKSYQGTLILISHDRDFLDPIVDKI 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-222 |
1.25e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERL--------EYRRSVGMVfQEASLFD 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIragimlcpEDRKAEGII-PVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 ---ASVRRN-AEYGLRVRQSWIDRL-RHELSSIVGKTNGtgdaiealdtvglrekANQDAASLSGGEAQRVAFARALAYE 167
Cdd:PRK11288 351 ninISARRHhLRAGCLINNRWEAENaDRFIRSLNIKTPS----------------REQLIMNLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 168 PDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-228 |
2.53e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAY------GAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLR-LLALFDAPDHGSIryenedvwqvseqerl 75
Cdd:PLN03130 612 LPAISIKNGYfswdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASV---------------- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 76 EYRRSVGMVFQEASLFDASVRRNAEYGLRVRQSWIDR------LRHELSSIVGktngtGDAIEaldtVGLRekanqdAAS 149
Cdd:PLN03130 676 VIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERaidvtaLQHDLDLLPG-----GDLTE----IGER------GVN 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 150 LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMH---QAERIadrvaVLLGNG 226
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHflsQVDRI-----ILVHEG 815
|
..
gi 490326802 227 II 228
Cdd:PLN03130 816 MI 817
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-207 |
7.19e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVwqvsEQERLEYRRSVG 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 83 MVFQEASLF-DASVRRNAEYGLrvrqswidrlrHELSSIVGKTngtgdaiEALDTVGLREKANQDAASLSGGEAQRVAFA 161
Cdd:PRK13540 78 FVGHRSGINpYLTLRENCLYDI-----------HFSPGAVGIT-------ELCRLFSLEHLIDYPCGLLSSGQKRQVALL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490326802 162 RALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATH 207
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-210 |
1.18e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 8 VHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYRRSVGMVFQE 87
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 ASlfdasvrRNAEyglrvrqswiDRLRHELSSIVGKTNGTGDaiealdtvglreKANQDAASLSGGEAQRVAFARALAYE 167
Cdd:PRK10636 398 LA-------RLAP----------QELEQKLRDYLGGFGFQGD------------KVTEETRRFSGGEKARLVLALIVWQR 448
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490326802 168 PDILLLDEPTSDLDPRNTAVIEDAVLEAKNrgiGVVIATHDMH 210
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEG---ALVVVSHDRH 488
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-211 |
1.42e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLAlfdapdhGSIRYENEDVWQVSEQERL--EYRRSVGMVFQEASLFDAs 94
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIQGNNFTGTILANNRKPtkQILKRTGFVTQDDILYPH- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 vrrnaeygLRVRQSWIDRLRHELSSIVGKTNGTGDAIEALDTVGLREKANQDAAS-----LSGGEAQRVAFARALAYEPD 169
Cdd:PLN03211 155 --------LTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490326802 170 ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdMHQ 211
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTS---MHQ 265
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-232 |
1.07e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFD--APDHGSIRYENEDVWQVSEQERLEyrRS 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAG--EG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFQE-------ASLFDASVRRNAEYGLRvRQSWIDRLRHElssivgktNGTGDAIEALDTVG--LREKANqdaASLS 151
Cdd:PRK09580 80 IFMAFQYpveipgvSNQFFLQTALNAVRSYR-GQEPLDRFDFQ--------DLMEEKIALLKMPEdlLTRSVN---VGFS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 152 GGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIA-DRVAVLLGNGIIEV 230
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKS 227
|
..
gi 490326802 231 GD 232
Cdd:PRK09580 228 GD 229
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-218 |
1.62e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 27 PGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYenedvwqvseqerleyrrsvgmvfqeaslfdasvrrnaeyglrvr 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 107 qswIDrlrhelssivgktngTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTA 186
Cdd:smart00382 36 ---ID---------------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190
....*....|....*....|....*....|....*...
gi 490326802 187 VIEDAV------LEAKNRGIGVVIATHDMHQAERIADR 218
Cdd:smart00382 98 LLLLLEelrlllLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-210 |
2.67e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 12 YGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENedvwqvseQERLEYRRSVGMVFQEASLF 91
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDP--------NERLGKLRQDQFAFEEFTVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 D-----------ASVRRNAEY---------GLRVRqswidrlrhELSSIVGKTNG-TGD--AIEALDTVGLREKANQDAA 148
Cdd:PRK15064 83 DtvimghtelweVKQERDRIYalpemseedGMKVA---------DLEVKFAEMDGyTAEarAGELLLGVGIPEEQHYGLM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490326802 149 S-LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDaVLEAKNRGIgvVIATHDMH 210
Cdd:PRK15064 154 SeVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLED-VLNERNSTM--IIISHDRH 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-229 |
5.24e-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: 55.30 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTL----LRLLALFDapdhGSIRYENEDVWQVSEQerlE 76
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLH---T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 77 YRRSVGMVFQEASLFDASVRRNAEYGLRVRQS--W----IDRLRHELSSIVGktngtgdaiealdtvGLREKANQDAASL 150
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLDPECKCTDDrlWealeIAQLKNMVKSLPG---------------GLDAVVTEGGENF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 151 SGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERI--ADRVAVLLGNGII 228
Cdd:cd03288 158 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIA----HRVSTIldADLVLVLSRGILV 233
|
.
gi 490326802 229 E 229
Cdd:cd03288 234 E 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-181 |
6.76e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLAL----FDAPDhGSIRYENEDVWQVSEQerleYRRSVGMVFQEaslf 91
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVE-GDIHYNGIPYKEFAEK----YPGEIIYVSEE---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 dasvrrnaeyglrvrqswiDRLRHELSsiVGKTngtgdaieaLDTVgLREKANQDAASLSGGEAQRVAFARALAYEPDIL 171
Cdd:cd03233 92 -------------------DVHFPTLT--VRET---------LDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 490326802 172 LLDEPTSDLD 181
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-181 |
8.79e-09 |
|
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: 54.26 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLrlLALFDAPD--HGSIRYENEDVWQVS-EQERLEYRRSVGMVFQEASLFD 92
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQtlEGKVHWSNKNESEPSfEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 93 ASVRRNAEYGlrvrqSWIDRLRHELSSIVGKTNGTGDAIEALDTVGLREKAnqdaASLSGGEAQRVAFARALAYEPDILL 172
Cdd:cd03290 93 ATVEENITFG-----SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERG----INLSGGQRQRICVARALYQNTNIVF 163
|
....*....
gi 490326802 173 LDEPTSDLD 181
Cdd:cd03290 164 LDDPFSALD 172
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-232 |
1.06e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 3 LEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLAlfDAPDH----GSIRYENEDVWQVSEQERleYR 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPAYkileGDILFKGESILDLEPEER--AH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 79 RSVGMVFQ----------EASLFDASVRRNAEYGLrvrqSWIDRLrhELSSIVGktngtgdaiEALDTVGLREK-----A 143
Cdd:CHL00131 84 LGIFLAFQypieipgvsnADFLRLAYNSKRKFQGL----PELDPL--EFLEIIN---------EKLKLVGMDPSflsrnV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 144 NQdaaSLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIA-DRVAVL 222
Cdd:CHL00131 149 NE---GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVM 225
|
250
....*....|
gi 490326802 223 LGNGIIEVGD 232
Cdd:CHL00131 226 QNGKIIKTGD 235
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-239 |
1.45e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENedvwqvseqerleyrrsvgmvfqEASLFDASVrrnae 100
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------------------SAALIAISS----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 101 yGLRVRQSWIDRLrhELSSI-VGKTNGTGDAI--EALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEPT 177
Cdd:PRK13545 95 -GLNGQLTGIENI--ELKGLmMGLTKEKIKEIipEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490326802 178 SDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTVFDN 239
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
149-233 |
3.34e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL---LGN 225
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMsngLVA 470
|
....*...
gi 490326802 226 GIIEVGDT 233
Cdd:PRK10982 471 GIVDTKTT 478
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-231 |
3.85e-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: 53.80 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQerlEYRRSVGMVFQEASLFDASVR 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH---DLRFKITIIPQDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 RN----AEYGlrVRQSWIDRlrhELSSIVGKTNGTGDaiealdtvGLREKANQDAASLSGGEAQRVAFARALAYEPDILL 172
Cdd:TIGR00957 1378 MNldpfSQYS--DEEVWWAL---ELAHLKTFVSALPD--------KLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 173 LDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAthdmHQAERIAD--RVAVLLGNGIIEVG 231
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIA----HRLNTIMDytRVIVLDKGEVAEFG 1501
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-222 |
7.74e-08 |
|
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: 52.52 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLR-LLALFDAPDHGSIRYENEDVWQVSEQERLeyRRSVGMVFQeaslfdasvrr 97
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAI--RAGIAMVPE----------- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 98 naeyglrvrqswiDRLRHELSSI--VGKtNGTGDAIEALDTVG-LREKANQDA-------------------ASLSGGEA 155
Cdd:TIGR02633 344 -------------DRKRHGIVPIlgVGK-NITLSVLKSFCFKMrIDAAAELQIigsaiqrlkvktaspflpiGRLSGGNQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 156 QRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-188 |
9.02e-08 |
|
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: 50.70 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALfdapdhgsiryenedvwqvseqerleyRRSVGMVFQEASL----FDAS 94
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAG---------------------------RKTAGVITGEILIngrpLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 VRRNAEYglrVRQSWIdrlrHELSSIVgktngtgdaIEALD-TVGLREkanqdaasLSGGEAQRVAFARALAYEPDILLL 173
Cdd:cd03232 77 FQRSTGY---VEQQDV----HSPNLTV---------REALRfSALLRG--------LSVEQRKRLTIGVELAAKPSILFL 132
|
170
....*....|....*
gi 490326802 174 DEPTSDLDPRNTAVI 188
Cdd:cd03232 133 DEPTSGLDSQAAYNI 147
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-207 |
1.35e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDgVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEqerlEYRRSVGMvfqeaslfdasvr 96
Cdd:PRK13541 16 LFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK----PYCTYIGH------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 rnaEYGLRVRQSWIDRLRHeLSSIVgktNGTGDAIEALDTVGLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDEP 176
Cdd:PRK13541 78 ---NLGLKLEMTVFENLKF-WSEIY---NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
170 180 190
....*....|....*....|....*....|.
gi 490326802 177 TSDLDPRNTAVIEDAVLEAKNRGIGVVIATH 207
Cdd:PRK13541 151 ETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
149-224 |
2.25e-07 |
|
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: 49.49 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRN----TAVIEDAVLEAKNRgigVVIATHDMHQAERIADRVAVLLG 224
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQrlnaARAIRRLSEEGKKT---ALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-222 |
3.50e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 21 VSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENEDVWQVSEQERLEYrrsvGMVF-----QEASLF-DAS 94
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK----GMAYitesrRDNGFFpNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 95 VRRNAEyglrvrqswIDRlrhelSSIVGKTNGTGDAIEALDTVGLREKA-----------NQDAASLSGGEAQRVAFARA 163
Cdd:PRK09700 358 IAQNMA---------ISR-----SLKDGGYKGAMGLFHEVDEQRTAENQrellalkchsvNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 164 LAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-207 |
4.31e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 20 GVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDH--GSIRY-----ENEDVWQVS---EQERLEyrrSVGMVFQEAS 89
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYieGDIRIsgfpkKQETFARISgycEQNDIH---SPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 90 LFDASVRRNAEYGLRVRQSWIDRLRH--ELSSIvgktngtGDAIEALDTVglrekanqdaASLSGGEAQRVAFARALAYE 167
Cdd:PLN03140 975 IYSAFLRLPKEVSKEEKMMFVDEVMElvELDNL-------KDAIVGLPGV----------TGLSTEQRKRLTIAVELVAN 1037
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490326802 168 PDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATH 207
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-210 |
5.49e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 31 VGIIGPSGVGKSTLLRLLALfdapdhgsiryenedvwqvseqerlEYRRSVGMVFQEASLFDASVRRNAEYGLRVRQSWI 110
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISG-------------------------ELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 111 DRLRH--------ELSSIVGKTNGTGDAiealdtvglrekANQDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDp 182
Cdd:PLN03073 593 LYMMRcfpgvpeqKLRAHLGSFGVTGNL------------ALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD- 659
|
170 180 190
....*....|....*....|....*....|...
gi 490326802 183 rntaviEDAVlEAKNRGI-----GVVIATHDMH 210
Cdd:PLN03073 660 ------LDAV-EALIQGLvlfqgGVLMVSHDEH 685
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-181 |
6.51e-07 |
|
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: 50.29 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 16 PVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENedvwqvseqeRLEYRRsvgmvfQEASLFDASV 95
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RISFSP------QTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 96 RRNAEYGLRVrqswiDRLRHelSSIVGKTNgtgdaIEAlDTVGLREKAN----QDAASLSGGEAQRVAFARALAYEPDIL 171
Cdd:TIGR01271 504 KDNIIFGLSY-----DEYRY--TSVIKACQ-----LEE-DIALFPEKDKtvlgEGGITLSGGQRARISLARAVYKDADLY 570
|
170
....*....|
gi 490326802 172 LLDEPTSDLD 181
Cdd:TIGR01271 571 LLDSPFTHLD 580
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
144-217 |
6.80e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.09 E-value: 6.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490326802 144 NQDAASLSGGEAQRVAFARALAYEPD--ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHD---MHQAERIAD 217
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNldvLSSADWIID 160
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
131-210 |
8.26e-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: 48.76 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 131 IEALDTVGLRE-KANQDAASLSGGEAQRVAFARALAYE---PDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAT 206
Cdd:cd03271 150 LQTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIE 229
|
....
gi 490326802 207 HDMH 210
Cdd:cd03271 230 HNLD 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-181 |
8.26e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 8 VHHAYGAE-PVFDGVSLSVTPGEVVGIIGPSGVGKSTL-----------------------LRLLALFDAPDHGsIRYEN 63
Cdd:NF040905 265 VYHPLHPErKVVDDVSLNVRRGEIVGIAGLMGAGRTELamsvfgrsygrnisgtvfkdgkeVDVSTVSDAIDAG-LAYVT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 64 EDvwqvseqerleyRRSVGMVFQEaslfdaSVRRN---AEYGLRVRQSWIDRLRhelssivgktngtgdaiEALDTVGLR 140
Cdd:NF040905 344 ED------------RKGYGLNLID------DIKRNitlANLGKVSRRGVIDENE-----------------EIKVAEEYR 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490326802 141 EKAN-------QDAASLSGGEAQRVAFARALAYEPDILLLDEPTSDLD 181
Cdd:NF040905 389 KKMNiktpsvfQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-207 |
8.27e-07 |
|
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: 49.75 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 22 SLSVTPGEVVGIIGPSGVGKSTLLRLLA-LFdaPDHGSIRYenedvwqVSEQERLEYrrsvgmVFQEASLFDASVRrnae 100
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGeLW--PVYGGRLT-------KPAKGKLFY------VPQRPYMTLGTLR---- 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 101 yglrvrqswiDRLRHELSSIVGKTNGTGDA--IEALDTVGL-----RE---KANQDAAS-LSGGEAQRVAFARALAYEPD 169
Cdd:TIGR00954 533 ----------DQIIYPDSSEDMKRRGLSDKdlEQILDNVQLthileREggwSAVQDWMDvLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*....
gi 490326802 170 ILLLDEPTSDLDPRntavIEDAVLE-AKNRGIGVVIATH 207
Cdd:TIGR00954 603 FAILDECTSAVSVD----VEGYMYRlCREFGITLFSVSH 637
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
144-219 |
1.30e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.02 E-value: 1.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 144 NQDAASLSGGEAQRVAFARALAYEPD--ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDmHQAERIADRV 219
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-188 |
1.48e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 17 VFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLAlfdapdhgsiryENEDVWQVSEQERL--------EYRRSVGMVFQE- 87
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA------------ERVTTGVITGGDRLvngrpldsSFQRSIGYVQQQd 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 ASLFDASVRRNAEYGLRVRQSwidrlrhelsSIVGKTNGTGDAIEALDTVGLREKAnqDAASLSGGEA------QRVAFA 161
Cdd:TIGR00956 846 LHLPTSTVRESLRFSAYLRQP----------KSVSKSEKMEYVEEVIKLLEMESYA--DAVVGVPGEGlnveqrKRLTIG 913
|
170 180
....*....|....*....|....*...
gi 490326802 162 RALAYEPDILL-LDEPTSDLDPRNTAVI 188
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSI 941
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-219 |
2.52e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 131 IEALDTVGLRE-KANQDAASLSGGEAQRVAfaraLAYE-------PDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGV 202
Cdd:PRK00635 790 IHALCSLGLDYlPLGRPLSSLSGGEIQRLK----LAYEllapskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTV 865
|
90
....*....|....*..
gi 490326802 203 VIATHDMHQAeRIADRV 219
Cdd:PRK00635 866 VIIEHNMHVV-KVADYV 881
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
150-216 |
2.62e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 2.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 150 LSGGEAQRVAFARALA---YEPDIL-LLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIA 216
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELAD 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
149-181 |
2.72e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.72e-06
10 20 30
....*....|....*....|....*....|...
gi 490326802 149 SLSGGEAQRVAFARALAYEPDILLLDEPTSDLD 181
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-253 |
2.83e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 144 NQDAASLSGGEAQRVAFARALAYEPD--ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDmHQAERIADRV-- 219
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIid 549
|
90 100 110
....*....|....*....|....*....|....*...
gi 490326802 220 ----AVLLGNGIIEVGDTKTvFDNPTDERTRKFIEGEL 253
Cdd:PRK00635 550 igpgAGIFGGEVLFNGSPRE-FLAKSDSLTAKYLRQEL 586
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-217 |
3.62e-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: 47.70 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 131 IEALDTVGLRE-KANQDAASLSGGEAQRVAFARAL---AYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIAT 206
Cdd:TIGR00630 810 LQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIE 889
|
90
....*....|....
gi 490326802 207 HDMH---QAERIAD 217
Cdd:TIGR00630 890 HNLDvikTADYIID 903
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-222 |
4.42e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.77 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 14 AEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRYENedvwqvseqeRLEYRRsvgmvfQEASLFDA 93
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RISFSS------QFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 94 SVRRNAEYGLRVrqswiDRLRHElsSIVGKTNgtgdaIEAlDTVGLREKAN----QDAASLSGGEAQRVAFARALAYEPD 169
Cdd:cd03291 113 TIKENIIFGVSY-----DEYRYK--SVVKACQ-----LEE-DITKFPEKDNtvlgEGGITLSGGQRARISLARAVYKDAD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490326802 170 ILLLDEPTSDLDPRNTAVIEDA----VLEAKNRgigvVIATHDMHQAeRIADRVAVL 222
Cdd:cd03291 180 LYLLDSPFGYLDVFTEKEIFEScvckLMANKTR----ILVTSKMEHL-KKADKILIL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
148-222 |
4.49e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 4.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490326802 148 ASLSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVL 222
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-208 |
6.91e-06 |
|
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: 45.68 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 33 IIGPSGVGKSTLLR--LLALF-DAPDHGSIRYENEDVwqVSEQERleyRRSVGMVFQEASLFDASVRRN---AEYGLRVR 106
Cdd:cd03240 27 IVGQNGAGKTTIIEalKYALTgELPPNSKGGAHDPKL--IREGEV---RAQVKLAFENANGKKYTITRSlaiLENVIFCH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 107 QSWIDRLrhelssivgktngtgdaieALDTVGlrekanqdaaSLSGGE------AQRVAFARALAYEPDILLLDEPTSDL 180
Cdd:cd03240 102 QGESNWP-------------------LLDMRG----------RCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNL 152
|
170 180 190
....*....|....*....|....*....|..
gi 490326802 181 DPRNTAV----IEDAVLEAKNRGIGVViaTHD 208
Cdd:cd03240 153 DEENIEEslaeIIEERKSQKNFQLIVI--THD 182
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
68-221 |
9.37e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 68 QVSEQ-ERLEYRRSVGMVFQEASL--------FDASVRRNAEYGLRVRqswidrLRHELSSivgkTNGTGDAIEALDTVG 138
Cdd:TIGR00618 870 KIIQLsDKLNGINQIKIQFDGDALikflheitLYANVRLANQSEGRFH------GRYADSH----VNARKYQGLALLVAD 939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 139 LREKANQDAASLSGGEAQRVAFARALAYEP----------DILLLDE--PTSDLDPRNTAV-IEDAvLEAKNRGIGVVIA 205
Cdd:TIGR00618 940 AYTGSVRPSATLSGGETFLASLSLALALADllstsggtvlDSLFIDEgfGSLDEDSLDRAIgILDA-IREGSKMIGIISH 1018
|
170
....*....|....*.
gi 490326802 206 THDMhqAERIADRVAV 221
Cdd:TIGR00618 1019 VPEF--RERIPHRILV 1032
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-208 |
1.06e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 30 VVGIIGPSGVGKSTLLR--LLALFDAPDHGS------IRYENEDVWqVS-----EQERLEYRRSVGMvFQEASLFDASVR 96
Cdd:COG0419 25 LNLIVGPNGAGKSTILEaiRYALYGKARSRSklrsdlINVGSEEAS-VElefehGGKRYRIERRQGE-FAEFLEAKPSER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 97 RNA---EYGLRVRQSWIDRLRhELSSIVGKTNGTGDAIEALDTVGLREKAN-QDAASLSGGEAQRVAFARALAyepdiLL 172
Cdd:COG0419 103 KEAlkrLLGLEIYEELKERLK-ELEEALESALEELAELQKLKQEILAQLSGlDPIETLSGGERLRLALADLLS-----LI 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 490326802 173 LDepTSDLDPRNTAVIEDAVLEAKnrgigvvIATHD 208
Cdd:COG0419 177 LD--FGSLDEERLERLLDALEELA-------IITHV 203
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
10-221 |
1.10e-05 |
|
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: 44.95 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 10 HAYGAEPVFDGVSLSVTPgeVVGIIGPSGVGKSTLLR--LLALFdapdhgsiryenedvwqvSEQERLEYRRSVGMVFQE 87
Cdd:cd03279 12 GPFREEQVIDFTGLDNNG--LFLICGPTGAGKSTILDaiTYALY------------------GKTPRYGRQENLRSVFAP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 88 AslfDASVRRNAEYGLRVRQSWIDRLRHElssivgktngtgDAIEALDTVGLRE-KANQ----DAASLSGGEAQRVAFAR 162
Cdd:cd03279 72 G---EDTAEVSFTFQLGGKKYRVERSRGL------------DYDQFTRIVLLPQgEFDRflarPVSTLSGGETFLASLSL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 163 ALA----------YEPDILLLDEPTSDLDPRNTAVIEDAV--LEAKNRGIGVViaTHDMHQAERIADRVAV 221
Cdd:cd03279 137 ALAlsevlqnrggARLEALFIDEGFGTLDPEALEAVATALelIRTENRMVGVI--SHVEELKERIPQRLEV 205
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-255 |
1.52e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.38 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 18 FDGVSLSVTPGEVVgIIGPSGVGKSTLLRLLALFDAPDhGSIRYENEDVWQVSEQE------RLEYRRSVGMVFQEasLF 91
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPS-SSRKFDEEDFYLGDDPDlpeieiELTFGSLLSRLLRL--LL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 92 DASVRRNAEYGLRVRQSWIDRLRHELSSIVGK---------------TNGTGDAIEALDTVGLREKANQDAASLSGGEAQ 156
Cdd:COG3593 90 KEEDKEELEEALEELNEELKEALKALNELLSEylkelldgldlelelSLDELEDLLKSLSLRIEDGKELPLDRLGSGFQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 157 RV--AFARALA-----YEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERI-ADRVAVLLGNGii 228
Cdd:COG3593 170 LIllALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRDS-- 247
|
250 260
....*....|....*....|....*..
gi 490326802 229 EVGDTKTVFDNPTDErtRKFIEGELIY 255
Cdd:COG3593 248 GGTTSTKLIDLDDED--LRKLLRYLGV 272
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-181 |
4.84e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 1 MTLEAIDVHHAYGAEPVFDGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRyenedvwqvseqerleyrrs 80
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-------------------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 81 VGMVFqEASLFDasvRRNAEygLRVRQSWIDRL-------------RHELSSIvgktngtgdaieaLDTVGLREKANQDA 147
Cdd:PRK11147 378 CGTKL-EVAYFD---QHRAE--LDPEKTVMDNLaegkqevmvngrpRHVLGYL-------------QDFLFHPKRAMTPV 438
|
170 180 190
....*....|....*....|....*....|....
gi 490326802 148 ASLSGGEAQRVAFARALAYEPDILLLDEPTSDLD 181
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
33-227 |
6.33e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 43.42 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 33 IIGPSGVGKSTLLRLLALFDA-------PDHGSIRYENEdvWQVSEQERLEYR-RSVGMVFQEASLFDASVRRNAEYGLR 104
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLLLQsnfiylpAERSGPARLYP--SLVRELSDLGSRgEYTADFLAELENLEILDDKSKELLEQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 105 VrQSWIDRLrhelssIVGKTNgtgdaIEA---LDTVGLREKANQDAASLSG-GEAQR-----VAFARALAYEPDILLLDE 175
Cdd:COG4938 103 V-EEWLEKI------FPGKVE-----VDAssdLVRLVFRPSGNGKRIPLSNvGSGVSellpiLLALLSAAKPGSLLIIEE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490326802 176 PTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIadRVAVLLGNGI 227
Cdd:COG4938 171 PEAHLHPKAQSALAELLAELANSGVQVIIETHSDYILNGL--RNLIKEGKLL 220
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-177 |
1.22e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 1.22e-04
10 20 30
....*....|....*....|....*....|....*..
gi 490326802 145 QDAASLSGGEAQRVAFARALAyEPD----ILLLDEPT 177
Cdd:COG0178 822 QPATTLSGGEAQRVKLASELS-KRStgktLYILDEPT 857
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-54 |
1.39e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 1.39e-04
10 20 30
....*....|....*....|....*....|....*...
gi 490326802 18 FDGVSLSVTPGEVVGIIGPSGVGKSTLL-RLLALFDAP 54
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLdAIQTLLVPA 49
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-219 |
1.67e-04 |
|
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: 42.69 E-value: 1.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490326802 144 NQDAASLSGGEAQRVAFARALAYEPD--ILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDmHQAERIADRV 219
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYV 559
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
150-236 |
2.81e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 150 LSGGEAQRVAFARALAYEPDILLLDEPTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIE 229
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
....*..
gi 490326802 230 VGDTKTV 236
Cdd:PRK10938 216 TGEREEI 222
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-236 |
3.97e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 19 DGVSLSVTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIRyENEDVWQVSEQERLEYRRSvGMvfqeaslfdasvrRN 98
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-RNGEVSVIAISAGLSGQLT-GI-------------EN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 99 AEYG---LRVRQSWIDRLRHELssivgktngtgdaIEALDtvgLREKANQDAASLSGGEAQRVAFARALAYEPDILLLDE 175
Cdd:PRK13546 106 IEFKmlcMGFKRKEIKAMTPKI-------------IEFSE---LGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490326802 176 PTSDLDPRNTAVIEDAVLEAKNRGIGVVIATHDMHQAERIADRVAVLLGNGIIEVGDTKTV 236
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
110-208 |
4.88e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490326802 110 IDRLRHELSSIVGKTNGTGDAIEALDTVGLREKANQD-----AASLSGGEAQRVAFARALAY---EPDILLLDEPTSDLD 181
Cdd:pfam13304 192 LKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGggelpAFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLH 271
|
90 100
....*....|....*....|....*..
gi 490326802 182 PRNTAVIEDAVLEAKNRGIGVVIATHD 208
Cdd:pfam13304 272 PKLLRRLLELLKELSRNGAQLILTTHS 298
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
145-180 |
1.92e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 490326802 145 QDAASLSGGEAQRVAFARALA--------YepdilLLDEPTSDL 180
Cdd:PRK00349 826 QPATTLSGGEAQRVKLAKELSkrstgktlY-----ILDEPTTGL 864
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
25-60 |
8.72e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 36.84 E-value: 8.72e-03
10 20 30
....*....|....*....|....*....|....*.
gi 490326802 25 VTPGEVVGIIGPSGVGKSTLLRLLALFDAPDHGSIR 60
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-49 |
9.75e-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: 36.22 E-value: 9.75e-03
|
| |
