|
Name |
Accession |
Description |
Interval |
E-value |
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-251 |
1.87e-121 |
|
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: 345.81 E-value: 1.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL-- 83
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 GVGLVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEq 163
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 164 hqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSE 243
Cdd:COG1127 162 ------ILLYDEPTAGLDPITSAVIDELIREL--RDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
....*...
gi 499173792 244 HPLLKQFF 251
Cdd:COG1127 234 DPWVRQFL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-250 |
3.98e-112 |
|
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: 322.14 E-value: 3.98e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALG--VG 86
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSEHPL 246
Cdd:cd03261 157 ---LLLYDEPTAGLDPIASGVIDDLIRSL--KKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
....
gi 499173792 247 LKQF 250
Cdd:cd03261 232 VRQF 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
2.37e-69 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 214.18 E-value: 2.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPvQPIIEFRGVSQSF----GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsi 76
Cdd:COG1116 1 MSAA-APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 eegeKALGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARA 156
Cdd:COG1116 78 ----PGPDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 157 IVINPEqhqqyknILLYDEPTAGLDPVasTRIE--SLIRHLLSQDHVCCcyLIVTH 210
Cdd:COG1116 153 LANDPE-------VLLMDEPFGALDAL--TRERlqDELLRLWQETGKTV--LFVTH 197
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-245 |
2.64e-69 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 217.27 E-value: 2.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRqrsie 77
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppEKR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 78 egekalGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAI 157
Cdd:COG3842 78 ------NVGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 158 VINPEqhqqyknILLYDEPTAGLDpvASTRIE--SLIRHLLSQDHVCCcyLIVTHQFS---TIdntTDRIIFLYDGKIQW 232
Cdd:COG3842 151 APEPR-------VLLLDEPLSALD--AKLREEmrEELRRLQRELGITF--IYVTHDQEealAL---ADRIAVMNDGRIEQ 216
|
250
....*....|...
gi 499173792 233 DGSTADAYksEHP 245
Cdd:COG3842 217 VGTPEEIY--ERP 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-238 |
3.24e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 210.69 E-value: 3.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsieEGEKALG-VGL 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR---DPAEVRRrIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVGFT--LYrdsDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhq 165
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFarLY---GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE--- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 166 qyknILLYDEPTAGLDPVASTRIESLIRHLLSQDH-VcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:COG1131 152 ----LLILDEPTSGLDPEARRELWELLRELAAEGKtV----LLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-245 |
5.21e-68 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 213.85 E-value: 5.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG-------HRRQRsieegek 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlPPRER------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 82 alGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINP 161
Cdd:COG1118 76 --RVGFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 162 EqhqqyknILLYDEPTAGLDpvASTR--IESLIRHLLSQDHVCCcyLIVTH------QFStidnttDRIIFLYDGKIQWD 233
Cdd:COG1118 153 E-------VLLLDEPFGALD--AKVRkeLRRWLRRLHDELGGTT--VFVTHdqeealELA------DRVVVMNQGRIEQV 215
|
250
....*....|..
gi 499173792 234 GSTADAYksEHP 245
Cdd:COG1118 216 GTPDEVY--DRP 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-246 |
2.78e-64 |
|
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: 208.99 E-value: 2.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSF-----GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGE 80
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 KALG--VGLVFQ--QSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGL-PGIGDRFPAELSGGMRKRVSLAR 155
Cdd:COG1123 338 RELRrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 156 AIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGS 235
Cdd:COG1123 418 ALALEPK-------LLILDEPTSALDVSVQAQILNLLRDL--QRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
250
....*....|..
gi 499173792 236 TADAYKS-EHPL 246
Cdd:COG1123 489 TEEVFANpQHPY 500
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-249 |
1.53e-63 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 198.33 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH---------RRQRsiee 78
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlreLRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekalgVGLVFQQSA--LFDSlTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARA 156
Cdd:COG1122 77 ------VGLVFQNPDdqLFAP-TVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 157 IVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGST 236
Cdd:COG1122 149 LAMEPE-------VLVLDEPTAGLDPRGRRELLELLKRLNKEGK---TVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
250
....*....|...
gi 499173792 237 ADAYkSEHPLLKQ 249
Cdd:COG1122 219 REVF-SDYELLEE 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-234 |
1.58e-63 |
|
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: 197.74 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRqrsieege 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvppERR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 kalGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVIN 160
Cdd:cd03259 73 ---NIGMVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 161 PEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCCYliVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03259 149 PS-------LLLLDEPLSALDAKLREELREELKELQRELGITTIY--VTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-210 |
7.57e-63 |
|
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: 196.15 E-value: 7.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG----RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKAlg 84
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqh 164
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499173792 165 qqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTH 210
Cdd:cd03293 152 -----VLLLDEPFSALDALTREQLQEELLDIWRETGKTV--LLVTH 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-230 |
6.42e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 194.11 E-value: 6.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFG----RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------- 70
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 --RRQRsieegekalgVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMR 148
Cdd:COG1136 82 rlRRRH----------IGFVFQFFNLLPELTALENVALPL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 149 KRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQfSTIDNTTDRIIFLYDG 228
Cdd:COG1136 151 QRVAIARALVNRPK-------LILADEPTGNLDSKTGEEVLELLRELNRELGTTI--VMVTHD-PELAARADRVIRLRDG 220
|
..
gi 499173792 229 KI 230
Cdd:COG1136 221 RI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-230 |
7.67e-61 |
|
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: 191.16 E-value: 7.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG----RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH-------------R 71
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 72 RQRsieegekalgVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRV 151
Cdd:cd03255 81 RRH----------IGFVFQSFNLLPDLTALENVELPL-LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 152 SLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvcCCYLIVTHQFStIDNTTDRIIFLYDGKI 230
Cdd:cd03255 150 AIARALANDPK-------IILADEPTGNLDSETGKEVMELLRELNKEAG--TTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-245 |
6.25e-60 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 192.98 E-value: 6.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR------RQRsieegeka 82
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppKDR-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 lGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPE 162
Cdd:COG3839 76 -NIAMVFQSYALYPHMTVYENIAFPL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 163 qhqqyknILLYDEPTAGLDPV--ASTRIEslIRHLLSQDHVCCCYliVTHqfstiDNT---T--DRIIFLYDGKIQWDGS 235
Cdd:COG3839 154 -------VFLLDEPLSNLDAKlrVEMRAE--IKRLHRRLGTTTIY--VTH-----DQVeamTlaDRIAVMNDGRIQQVGT 217
|
250
....*....|
gi 499173792 236 TADAYksEHP 245
Cdd:COG3839 218 PEELY--DRP 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-245 |
1.44e-59 |
|
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: 188.70 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEgekaLGVGL 87
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDaTDVPVQE----RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVGFTL-YRDSDLRP--REIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqh 164
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLrVKPRSERPpeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 165 qqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYksEH 244
Cdd:cd03296 157 -----VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTT--VFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY--DH 227
|
.
gi 499173792 245 P 245
Cdd:cd03296 228 P 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-238 |
2.49e-59 |
|
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: 188.14 E-value: 2.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVglV 88
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSALFDSLTVAENVGFtLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPeqhqqyK 168
Cdd:COG4555 80 PDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP------K 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 169 NILLyDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:COG4555 153 VLLL-DEPTNGLDVMARRLLREILRALKKEGK---TVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-252 |
3.24e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 185.20 E-value: 3.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHrrqrSIEEGEKAL---- 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE----DLTDSKKDInklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 -GVGLVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPE 162
Cdd:COG1126 77 rKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 163 qhqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKS 242
Cdd:COG1126 157 -------VMLFDEPTSALDPELVGEVLDVMRD-LAKEGMTM--VVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
250
....*....|.
gi 499173792 243 -EHPLLKQFFS 252
Cdd:COG1126 227 pQHERTRAFLS 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-234 |
8.74e-58 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 183.33 E-value: 8.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKV-ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH-------------RRQ 73
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 74 rsieegekalgVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSL 153
Cdd:COG2884 81 -----------IGVVFQDFRLLPDRTVYENVALPL-RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 154 ARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWD 233
Cdd:COG2884 149 ARALVNRPE-------LLLADEPTGNLDPETSWEIMELLEE-INRRGTTV--LIATHDLELVDRMPKRVLELEDGRLVRD 218
|
.
gi 499173792 234 G 234
Cdd:COG2884 219 E 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-245 |
1.26e-56 |
|
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: 180.90 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQrsieege 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlppHKRP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 kalgVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVIN 160
Cdd:cd03300 74 ----VNTVFQNYALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 161 PEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAY 240
Cdd:cd03300 149 PK-------VLLLDEPLGALDLKLRKDMQLELKRL--QKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
....*
gi 499173792 241 ksEHP 245
Cdd:cd03300 220 --EEP 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-230 |
2.18e-56 |
|
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: 180.01 E-value: 2.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRK----VILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL 83
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 G--VGLVFQ--QSALFDSLTVAENVGFTLYRDSDLRPRE-IRAIVEENLELVGLP-GIGDRFPAELSGGMRKRVSLARAI 157
Cdd:cd03257 81 RkeIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 158 VINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03257 161 ALNPK-------LLIADEPTSALDVSVQAQILDLLKKL--QEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-238 |
2.99e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.25 E-value: 2.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------RRQRS 75
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtalrgralRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 76 ieegekalGVGLVFQQSALFDSLTVAENV--GfTLYRDSDLR------PREIRAIVEENLELVGLPGIGDRFPAELSGGM 147
Cdd:COG3638 81 --------RIGMIFQQFNLVPRLSVLTNVlaG-RLGRTSTWRsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 148 RKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYD 227
Cdd:COG3638 152 QQRVAIARALVQEPK-------LILADEPVASLDPKTARQVMDLLRRIAREDGITV--VVNLHQVDLARRYADRIIGLRD 222
|
250
....*....|.
gi 499173792 228 GKIQWDGSTAD 238
Cdd:COG3638 223 GRVVFDGPPAE 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-229 |
6.21e-56 |
|
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: 178.43 E-value: 6.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 10 EFRGVSQSFGR--KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhRRQRSIEEGEKALGVGL 87
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG-KDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSAL-FDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:cd03225 155 ---ILLLDEPTAGLDPAGRRELLELLKKLKAEGK---TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-256 |
4.72e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 180.27 E-value: 4.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRK----VILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------RRQ 73
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalserelRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 74 RSieegekalGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSL 153
Cdd:COG1135 81 RR--------KIGMIFQHFNLLSSRTVAENVALPL-EIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 154 ARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHL-----LSqdhvcccYLIVTHQFSTIDNTTDRIIFLYDG 228
Cdd:COG1135 152 ARALANNPK-------VLLCDEATSALDPETTRSILDLLKDInrelgLT-------IVLITHEMDVVRRICDRVAVLENG 217
|
250 260
....*....|....*....|....*....
gi 499173792 229 KIQWDGSTADAY-KSEHPLLKQFFSGSID 256
Cdd:COG1135 218 RIVEQGPVLDVFaNPQSELTRRFLPTVLN 246
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-236 |
8.79e-55 |
|
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: 175.83 E-value: 8.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLL-----TPDSGEVIVHGH-RRQRSIEEGEKA 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 LGVGLVFQQSALFDsLTVAENVGFTLyRDSDLRPR-EIRAIVEENLELVGLPG-IGDRFPA-ELSGGMRKRVSLARAIVI 159
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGIKLKeELDERVEEALRKAALWDeVKDRLHAlGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGST 236
Cdd:cd03260 159 EPE-------VLLLDEPTSALDPISTAKIEELIAELKKEYTI----VIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-256 |
5.61e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.51 E-value: 5.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsieegeKALGV 85
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLVFQQSAlFDS---LTVAENVGFTLYRDSDLRPR---EIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVI 159
Cdd:COG1121 78 GYVPQRAE-VDWdfpITVRDVVLMGRYGRRGLFRRpsrADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDH-VcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWdGSTAD 238
Cdd:COG1121 157 DPD-------LLLLDEPFAGVDAATEEALYELLRELRREGKtI----LVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE 224
|
250
....*....|....*...
gi 499173792 239 AYKSEHplLKQFFSGSID 256
Cdd:COG1121 225 VLTPEN--LSRAYGGPVA 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-230 |
8.67e-54 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 173.10 E-value: 8.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRrqrsIEEGEKAL----- 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK----LTDDKKNInelrq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 GVGLVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEq 163
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 164 hqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHvcCCYLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03262 156 ------VMLFDEPTSALDPELVGEVLDVMKD-LAEEG--MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-238 |
1.23e-53 |
|
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: 173.15 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFG----RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrQRSIEEGEKAL 83
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG---TDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 -----GVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIV 158
Cdd:cd03258 78 rkarrRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 159 INPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:cd03258 157 NNPK-------VLLCDEATSALDPETTQSILALLRDI--NRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-230 |
2.10e-53 |
|
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: 170.66 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRrqrSIEEGEKALG-VGL 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD---IKKEPEEVKRrIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVgftlyrdsdlrpreiraiveenlelvglpgigdrfpaELSGGMRKRVSLARAIVINPEqhqqy 167
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPE----- 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 168 knILLYDEPTAGLDPVASTRIESLIRHLLSQD-HVcccyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03230 116 --LLILDEPTSGLDPESRREFWELLRELKKEGkTI----LLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-230 |
7.75e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 7.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG----------HRRQrsiee 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppeWRRQ----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekalgVGLVFQQSALFDSlTVAENVGFTlYRDSDLRPREIRAivEENLELVGLP-GIGDRFPAELSGGMRKRVSLARAI 157
Cdd:COG4619 76 ------VAYVPQEPALWGG-TVRDNLPFP-FQLRERKFDRERA--LELLERLGLPpDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 158 VINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:COG4619 146 LLQPD-------VLLLDEPTSALDPENTRRVEELLREYLAEEGRAV--LWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-246 |
2.43e-52 |
|
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: 177.40 E-value: 2.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD---SGEVIVHGhRRQRSIEEGE 80
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDG-RDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 KALGVGLVFQQ-SALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVI 159
Cdd:COG1123 81 RGRRIGMVFQDpMTQLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADA 239
Cdd:COG1123 160 DPD-------LLIADEPTTALDVTTQAEILDLLRELQRERGTTV--LLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
....*..
gi 499173792 240 YKSEHPL 246
Cdd:COG1123 231 LAAPQAL 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-238 |
5.28e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 169.17 E-value: 5.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 28 DLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRSIeegekalgvglVFQQSALFDSLT 99
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppAERPVSM-----------LFQENNLFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 100 VAENVGFTLyrDSDLRP-REIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVinpeqhqQYKNILLYDEPTA 178
Cdd:COG3840 88 VAQNIGLGL--RPGLKLtAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV-------RKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 179 GLDPvaSTRIESLirHLLSQdhVCCCY----LIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:COG3840 159 ALDP--ALRQEML--DLVDE--LCRERgltvLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-230 |
5.99e-52 |
|
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: 168.77 E-value: 5.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPIIEFRGVSQSF----GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSI 76
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEGEKAL---GVGLVFQQSALFDSLTVAENVGFTLYRDSDlrpREIRAIVEENLELVGLpgiGDR---FPAELSGGMRKR 150
Cdd:COG4181 81 EDARARLrarHVGFVFQSFQLLPTLTALENVMLPLELAGR---RDARARARALLERVGL---GHRldhYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 151 VSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVccCYLIVTHqfstiDNT----TDRIIFLY 226
Cdd:COG4181 155 VALARAFATEPA-------ILFADEPTGNLDAATGEQIIDLLFELNRERGT--TLVLVTH-----DPAlaarCDRVLRLR 220
|
....
gi 499173792 227 DGKI 230
Cdd:COG4181 221 AGRL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-238 |
1.13e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 168.35 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG-HRRQRSIEEGEKALGVG 86
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK---- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:PRK09493 157 ---LMLFDEPTSALDPELRHEVLKVMQDLAEEGMT---MVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-256 |
2.08e-51 |
|
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: 168.06 E-value: 2.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG----RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG----HRRQRSIeege 80
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtRRRRKAF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 kALGVGLVFQQ--SALFDSLTVAENVGFTLYrdsDLRPREIRAIVEENLELVGLP-GIGDRFPAELSGGMRKRVSLARAI 157
Cdd:COG1124 78 -RRRVQMVFQDpyASLHPRHTVDRILAEPLR---IHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 158 VINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVccCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTA 237
Cdd:COG1124 154 ILEPE-------LLLLDEPTSALDVSVQAEILNLLKDLREERGL--TYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250 260
....*....|....*....|
gi 499173792 238 DAYKS-EHPLLKQFFSGSID 256
Cdd:COG1124 225 DLLAGpKHPYTRELLAASLA 244
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-211 |
1.32e-50 |
|
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: 164.57 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALgvG 86
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFDSLTVAENVGFTlyrdSDLRPREIRAI-VEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhq 165
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFW----AALYGLRADREaIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP--- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499173792 166 qyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQ 211
Cdd:COG4133 152 ----LWLLDEPFTALDAAGVALLAELIAAHLARG---GAVLLTTHQ 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-229 |
1.21e-49 |
|
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: 161.20 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALG-VGL 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVGFTLyrdsdlrpreiraiveenlelvglpgigdrfpaelSGGMRKRVSLARAIVINPEqhqqy 167
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL-----------------------------------SGGQQQRVALARALAMDPD----- 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 168 knILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:cd03229 121 --VLLLDEPTSALDPITRREVRALLKSLQAQLGITV--VLVTHDLDEAARLADRVVVLRDGK 178
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-245 |
1.44e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 167.05 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQ--PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR------R 72
Cdd:PRK09452 5 NKQPSSlsPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvpaE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 73 QRSieegekalgVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVS 152
Cdd:PRK09452 85 NRH---------VNTVFQSYALFPHMTVFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 153 LARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQW 232
Cdd:PRK09452 155 IARAVVNKPK-------VLLLDESLSALDYKLRKQMQNELKAL--QRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 225
|
250
....*....|...
gi 499173792 233 DGSTADAYksEHP 245
Cdd:PRK09452 226 DGTPREIY--EEP 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-238 |
3.21e-49 |
|
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: 161.84 E-value: 3.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRsieege 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppHEIAR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 kaLGVGLVFQQSALFDSLTVAENV----------GFTLYRDSDLRpREIRAIVEENLELVGLPGIGDRFPAELSGGMRKR 150
Cdd:cd03219 75 --LGIGRTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREE-REARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 151 VSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03219 152 LEIARALATDPK-------LLLLDEPAAGLNPEETEELAELIRELRERGI---TVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
....*...
gi 499173792 231 QWDGSTAD 238
Cdd:cd03219 222 IAEGTPDE 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-238 |
1.15e-48 |
|
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: 160.81 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGR-KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL--GV 85
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLVFQQSALFDSLTVAENV--GFtLYRDSDLR------PREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAI 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsGR-LGRRSTWRslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 158 VINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTA 237
Cdd:cd03256 160 MQQPK-------LILADEPVASLDPASSRQVMDLLKRINREEGITV--IVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
.
gi 499173792 238 D 238
Cdd:cd03256 231 E 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-259 |
2.05e-48 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 161.09 E-value: 2.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-----RQRSIEEGEKa 82
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsRSRLYTVRKR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 lgVGLVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPE 162
Cdd:PRK11831 86 --MSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 163 qhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKS 242
Cdd:PRK11831 164 -------LIMFDEPFVGQDPITMGVLVKLISELNSALGVTC--VVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
250
....*....|....*..
gi 499173792 243 EHPLLKQFFSGSIDGPI 259
Cdd:PRK11831 235 PDPRVRQFLDGIADGPV 251
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-230 |
3.63e-48 |
|
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: 159.82 E-value: 3.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRsie 77
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglppHRIAR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 78 egekaLGVGLVFQQSALFDSLTVAENV-----------------GFTLYRDSDlrpREIRAIVEENLELVGLPGIGDRFP 140
Cdd:COG0411 79 -----LGIARTFQNPRLFPELTVLENVlvaaharlgrgllaallRLPRARREE---REARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 141 AELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTD 220
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPK-------LLLLDEPAAGLNPEETEELAELIRRLRDERGITI--LLIEHDMDLVMGLAD 221
|
250
....*....|
gi 499173792 221 RIIFLYDGKI 230
Cdd:COG0411 222 RIVVLDFGRV 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-238 |
1.42e-47 |
|
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: 158.28 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhRRQRSIEEGEKALGVGL 87
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENV--GFTLYRDSDLRPREI-RAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqh 164
Cdd:COG1120 80 VPQEPPAPFGLTVRELValGRYPHLGLFGRPSAEdREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 165 qqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTH------QFStidnttDRIIFLYDGKIQWDGSTAD 238
Cdd:COG1120 158 -----LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTV--VMVLHdlnlaaRYA------DRLVLLKDGRIVAQGPPEE 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-241 |
1.47e-46 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 158.73 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEkalgVGL 87
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDvTHRSIQQRD----ICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqy 167
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK----- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 168 knILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCCYliVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYK 241
Cdd:PRK11432 157 --VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLY--VTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-230 |
3.69e-46 |
|
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: 153.33 E-value: 3.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVI-LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG----HRRQRSIEEGEKAL 83
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 GVglVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEq 163
Cdd:cd03292 81 GV--VFQDFRLLPDRNVYENVAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 164 hqqyknILLYDEPTAGLDPVASTRIESLIRhllSQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03292 157 ------ILIADEPTGNLDPDTTWEIMNLLK---KINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-234 |
4.55e-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: 153.22 E-value: 4.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKI---YPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKAL-------GVGLVFQQSA 93
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG----TVLFDSRKKInlppqqrKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 94 LFDSLTVAENVGFTLYRdsdLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLY 173
Cdd:cd03297 86 LFPHLNVRENLAFGLKR---KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE-------LLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 174 DEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPV--IFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-235 |
5.08e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 157.17 E-value: 5.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG------HRRQRSieegeka 82
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlHARDRK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 lgVGLVFQQSALFDSLTVAENVGF---TLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVI 159
Cdd:PRK10851 76 --VGFVFQHYALFRHMTVFDNIAFgltVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDpvASTRIEslIRHLLSQDH--VCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGS 235
Cdd:PRK10851 154 EPQ-------ILLLDEPFGALD--AQVRKE--LRRWLRQLHeeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-233 |
8.57e-46 |
|
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: 152.30 E-value: 8.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 10 EFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKAlgVGLVF 89
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKR--IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 90 QQ-SALFDS-LTVAENVGFTLYRDSDLRP---REIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqh 164
Cdd:cd03235 75 QRrSIDRDFpISVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD-- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 165 qqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWD 233
Cdd:cd03235 153 -----LLLLDEPFAGVDPKTQEDIYELLRELRREG---MTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-178 |
4.25e-45 |
|
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: 148.56 E-value: 4.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAlGVGLVFQQSALFDSLTVAEN 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 104 VGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDR----FPAELSGGMRKRVSLARAIVINPeqhqqykNILLYDEPTA 178
Cdd:pfam00005 80 LRLGL-LLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKP-------KLLLLDEPTA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-251 |
4.68e-45 |
|
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: 151.68 E-value: 4.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhRRQRSIEEGEKALGVGL 87
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG-EDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVGFTLYRDSDLRPReIRAIVEENLELVGLP--GIGDRFPAELSGGMRKRVSLARAIVINPEqhq 165
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEK-IRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPP--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 166 qyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSEHP 245
Cdd:cd03295 156 ----LLLMDEPFGALDPITRDQLQEEFKRL--QQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
....*..
gi 499173792 246 -LLKQFF 251
Cdd:cd03295 230 dFVAEFV 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-231 |
5.14e-45 |
|
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: 150.48 E-value: 5.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhRRQRSIEEGEKalGVGLV 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-RDVTDLPPKDR--DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyk 168
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK------ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499173792 169 nILLYDEPTAGLDpvASTRIESL--IRHLLSQDHVCCCYliVTHQFSTIDNTTDRIIFLYDGKIQ 231
Cdd:cd03301 151 -VFLMDEPLSNLD--AKLRVQMRaeLKRLQQRLGTTTIY--VTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-234 |
3.20e-44 |
|
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: 148.50 E-value: 3.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGeAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGvgLV 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG--YL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSALFDSLTVAENVGFtLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyk 168
Cdd:cd03264 78 PQEFGVYPNFTVREFLDY-IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS------ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 169 nILLYDEPTAGLDPVASTRIESLIRHlLSQDHVcccYLIVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03264 151 -ILIVDEPTAGLDPEERIRFRNLLSE-LGEDRI---VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-234 |
4.25e-44 |
|
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: 148.13 E-value: 4.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKalgVGLV 88
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR---IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSALFDSLTVAENVgftlyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyk 168
Cdd:cd03268 78 IEAPGFYPNLTARENL-----RLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD------ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 169 nILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03268 147 -LLILDEPTNGLDPDGIKELRELILSLRDQG---ITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-241 |
5.11e-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: 149.91 E-value: 5.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGR-----KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL 83
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 --GVGLVFQQSA--LFdSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLP-GIGDRFPAELSGGMRKRVSLARAIV 158
Cdd:TIGR04521 81 rkKVGLVFQFPEhqLF-EETVYKDIAFGP-KNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 159 INPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:TIGR04521 159 MEPE-------VLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTV--ILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
...
gi 499173792 239 AYK 241
Cdd:TIGR04521 230 VFS 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-237 |
1.60e-43 |
|
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: 146.88 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG--RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVg 86
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 lVFQQSALFDSLTVAENVgfTLY-RDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPeqhq 165
Cdd:cd03263 80 -CPQFDALFDELTVREHL--RFYaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP---- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 166 qykNILLYDEPTAGLDPVASTRIESLIRHLLSQdhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTA 237
Cdd:cd03263 153 ---SVLLLDEPTSGLDPASRRAIWDLILEVRKG----RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-196 |
3.25e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 147.32 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFG----RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQrsieeGEKA 82
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-----GPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 lGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPE 162
Cdd:COG4525 77 -DRGVVFQKDALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190
....*....|....*....|....*....|....
gi 499173792 163 qhqqyknILLYDEPTAGLDpvASTRiESLIRHLL 196
Cdd:COG4525 155 -------FLLMDEPFGALD--ALTR-EQMQELLL 178
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-256 |
5.03e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 149.18 E-value: 5.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF---GRKVI-LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH-----------RRQ 73
Cdd:PRK11153 2 IELKNISKVFpqgGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 74 RSIeegekalgvGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSL 153
Cdd:PRK11153 82 RQI---------GMIFQHFNLLSSRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 154 ARAIVINPeqhqqykNILLYDEPTAGLDPvASTR-IESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQW 232
Cdd:PRK11153 152 ARALASNP-------KVLLCDEATSALDP-ATTRsILELLKDINRELGLTI--VLITHEMDVVKRICDRVAVIDAGRLVE 221
|
250 260
....*....|....*....|....*
gi 499173792 233 DGSTADAY-KSEHPLLKQFFSGSID 256
Cdd:PRK11153 222 QGTVSEVFsHPKHPLTREFIQSTLH 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-234 |
2.32e-42 |
|
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: 143.79 E-value: 2.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 26 DVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSiEEGEKAlgVGLVFQQSALFDSLTVAENVG 105
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-PPADRP--VSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 106 FTLYRDSDLRPrEIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVinpeqhqQYKNILLYDEPTAGLDPVAS 185
Cdd:cd03298 93 LGLSPGLKLTA-EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLV-------RDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499173792 186 TRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03298 165 AEMLDLVLDLHAETKMTV--LMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-250 |
2.35e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.39 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL----- 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIrllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 GVGLVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEq 163
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 164 hqqyknILLYDEPTAGLDPVASTRIESLIRHL----LSQdhvcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGstaDA 239
Cdd:COG4161 162 ------VLLFDEPTAALDPEITAQVVEIIRELsqtgITQ-------VIVTHEVEFARKVASQVVYMEKGRIIEQG---DA 225
|
250
....*....|.
gi 499173792 240 YKSEHPLLKQF 250
Cdd:COG4161 226 SHFTQPQTEAF 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-234 |
5.05e-42 |
|
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: 142.89 E-value: 5.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSF----GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL 83
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 GVglVFQQSALFDSLTVAENVGF--TLYrdsDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINP 161
Cdd:cd03266 81 GF--VSDSTGLYDRLTARENLEYfaGLY---GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 162 EqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03266 156 P-------VLLLDEPTTGLDVMATRALREFIRQLRALG---KCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-240 |
5.41e-42 |
|
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: 143.59 E-value: 5.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGR-KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsieEGEKAL--- 83
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK---LRGKKLrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 --GVGLVFQQSALFDSLTVAENV--GFtLYRDSDLR------PREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSL 153
Cdd:TIGR02315 78 rrRIGMIFQHYNLIERLTVLENVlhGR-LGYKPTWRsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 154 ARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWD 233
Cdd:TIGR02315 157 ARALAQQPD-------LILADEPIASLDPKTSKQVMDYLKRINKEDGITV--IINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
....*..
gi 499173792 234 GSTADAY 240
Cdd:TIGR02315 228 GAPSELD 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-250 |
9.98e-42 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 142.85 E-value: 9.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL----- 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIrelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 GVGLVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEq 163
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 164 hqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVccCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGsTADAYksE 243
Cdd:PRK11124 162 ------VLLFDEPTAALDPEITAQIVSIIRE-LAETGI--TQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCF--T 229
|
....*..
gi 499173792 244 HPLLKQF 250
Cdd:PRK11124 230 QPQTEAF 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-243 |
1.02e-41 |
|
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: 142.68 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRsieege 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmHKRAR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 kaLGVGLVFQQSALFDSLTVAENVGFTLYRDSDLRpREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVIN 160
Cdd:cd03218 75 --LGIGYLPQEASIFRKLTVEENILAVLEIRGLSK-KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 161 PEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAY 240
Cdd:cd03218 152 PK-------FLLLDEPFAGVDPIAVQDIQKIIKILKDRG---IGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
...
gi 499173792 241 KSE 243
Cdd:cd03218 222 ANE 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-229 |
8.72e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 8.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 10 EFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAlGVGLVF 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 90 QqsalfdsltvaenvgftlyrdsdlrpreiraiveenlelvglpgigdrfpaeLSGGMRKRVSLARAIVINPEqhqqykn 169
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPD------- 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 170 ILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEG---RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
1.26e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.56 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPV---QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGL--LTPD---SGEVIVHGH-- 70
Cdd:COG1117 1 MTAPAstlEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 ----------RRQrsieegekalgVGLVFQQSALFdSLTVAENVGFTLyRDSDLRPR-EIRAIVEENLELVGLPG-IGDR 138
Cdd:COG1117 81 ydpdvdvvelRRR-----------VGMVFQKPNPF-PKSIYDNVAYGL-RLHGIKSKsELDEIVEESLRKAALWDeVKDR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 139 F--PA-ELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHvccCYLIVTH---QF 212
Cdd:COG1117 148 LkkSAlGLSGGQQQRLCIARALAVEPE-------VLLMDEPTSALDPISTAKIEELILE-LKKDY---TIVIVTHnmqQA 216
|
250
....*....|....*...
gi 499173792 213 STIdntTDRIIFLYDGKI 230
Cdd:COG1117 217 ARV---SDYTAFFYLGEL 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-238 |
2.47e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.87 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEKALGVgl 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlAAWSPWELARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSAL-FDsLTVAENVGFTLYRdSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEQHQQ 166
Cdd:COG4559 80 LPQHSSLaFP-FTVEEVVALGRAP-HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 167 YKNILLYDEPTAGLDPVASTRIESLIRHLLSQD-HVCCcyliVTH------QFStidnttDRIIFLYDGKIQWDGSTAD 238
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGgGVVA----VLHdlnlaaQYA------DRILLLHQGRLVAQGTPEE 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-230 |
2.67e-40 |
|
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: 140.09 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 14 VSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH-------------RRQRsieege 80
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelRRKK------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 kalgVGLVFQQSALFDSLTVAENVGFTL-YRDSDLRPREIRAivEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVI 159
Cdd:cd03294 104 ----ISMVFQSFALLPHRTVLENVAFGLeVQGVPRAEREERA--AEALELVGLEGWEHKYPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPvastriesLIR-----HLLS-QDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03294 178 DPD-------ILLMDEAFSALDP--------LIRremqdELLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-229 |
3.63e-40 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 136.74 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG--RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRrQRSIEEGEKALGVG 86
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFDSlTVAENVgftlyrdsdlrpreiraiveenlelvglpgigdrfpaeLSGGMRKRVSLARAIVINPEqhqq 166
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDPP---- 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVCccyLIVTHQFSTIDNtTDRIIFLYDGK 229
Cdd:cd03228 117 ---ILILDEATSALDPETEALILEALRA-LAKGKTV---IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-251 |
6.25e-40 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 138.29 E-value: 6.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSG-EVIVHGHRRQR-SIEEGEKAL 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGeDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 gvGLVfqQSALFDSLTVAENV------GFT----LYRDSDlrpREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSL 153
Cdd:COG1119 81 --GLV--SPALQLRFPRDETVldvvlsGFFdsigLYREPT---DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 154 ARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLI-VTHQFSTIDNTTDRIIFLYDGKIQW 232
Cdd:COG1119 154 ARALVKDPE-------LLILDEPTAGLDLGARELLLALLDKLAAEGAPT---LVlVTHHVEEIPPGITHVLLLKDGRVVA 223
|
250
....*....|....*....
gi 499173792 233 DGSTADAYKSEHplLKQFF 251
Cdd:COG1119 224 AGPKEEVLTSEN--LSEAF 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-235 |
7.23e-40 |
|
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: 146.13 E-value: 7.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 3 EPVQPIIEFRGVSQSFGR--KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH---------- 70
Cdd:COG2274 468 PRLKGDIELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpasl 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 RRQrsieegekalgVGLVFQQSALFdSLTVAENVGFTlyrDSDLRPREIRAIveenLELVG-------LPG-----IGDR 138
Cdd:COG2274 548 RRQ-----------IGVVLQDVFLF-SGTIRENITLG---DPDATDEEIIEA----ARLAGlhdfieaLPMgydtvVGEG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 139 FpAELSGGMRKRVSLARAIVINPeqhqqykNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNt 218
Cdd:COG2274 609 G-SNLSGGQRQRLAIARALLRNP-------RILILDEATSALDAETEAIILENLRRLLKGRTV----IIIAHRLSTIRL- 675
|
250
....*....|....*..
gi 499173792 219 TDRIIFLYDGKIQWDGS 235
Cdd:COG2274 676 ADRIIVLDKGRIVEDGT 692
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-238 |
8.26e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 137.79 E-value: 8.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 28 DLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--HRR----QRSieegekalgVGLVFQQSALFDSLTVA 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdHTTtppsRRP---------VSMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 102 ENVGFTLyrDSDLR-PREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVinpeqHQQykNILLYDEPTAGL 180
Cdd:PRK10771 90 QNIGLGL--NPGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV-----REQ--PILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 181 DPvaSTRIESLirHLLSQdhVC----CCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:PRK10771 161 DP--ALRQEML--TLVSQ--VCqerqLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-245 |
1.15e-39 |
|
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: 139.80 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKV----ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTP---DSGEVIVHGH-------RRQ 73
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdllklseKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 74 RSIEEGEkalgVGLVFQ--QSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPG---IGDRFPAELSGGMR 148
Cdd:COG0444 81 RKIRGRE----IQMIFQdpMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 149 KRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDG 228
Cdd:COG0444 157 QRVMIARALALEPK-------LLIADEPTTALDVTIQAQILNLLKDL--QRELGLAILFITHDLGVVAEIADRVAVMYAG 227
|
250
....*....|....*...
gi 499173792 229 KIQWDGSTADAYKS-EHP 245
Cdd:COG0444 228 RIVEEGPVEELFENpRHP 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-243 |
1.49e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 137.08 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRsiee 78
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlpmHKRAR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekaLGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIV 158
Cdd:COG1137 78 ----LGIGYLPQEASIFRKLTVEDNILAVL-ELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 159 INPeqhqqyKNILLyDEPTAGLDPVASTRIESLIRHLLSQD-HVcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTA 237
Cdd:COG1137 153 TNP------KFILL-DEPFAGVDPIAVADIQKIIRHLKERGiGV----LITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
....*.
gi 499173792 238 DAYKSE 243
Cdd:COG1137 222 EILNNP 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-236 |
3.01e-39 |
|
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: 138.29 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 18 FGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVglVFQQSALFDS 97
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGI--VPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTVAENVGF--TLYrdsDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDE 175
Cdd:TIGR01188 81 LTGRENLEMmgRLY---GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPD-------VLFLDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 176 PTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGST 236
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKEEGVTI---LLTTHYMEEADKLCDRIAIIDHGRIIAEGTP 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-239 |
3.37e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 136.83 E-value: 3.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH-RRQRSIEEGEKALGV 85
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 glVFQQSALFDSLTVAENVGFTLYRDSdLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEQHQ 165
Cdd:PRK13548 81 --LPQHSSLSFPFTVEEVVAMGRAPHG-LSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 166 QYKnILLYDEPTAGLDPVASTRIESLIRHLLSQD--HVCCcyliVTH------QFStidnttDRIIFLYDGKIQWDGSTA 237
Cdd:PRK13548 158 PPR-WLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIV----VLHdlnlaaRYA------DRIVLLHQGRLVADGTPA 226
|
..
gi 499173792 238 DA 239
Cdd:PRK13548 227 EV 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-233 |
7.81e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 135.96 E-value: 7.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 12 RGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEgekalgVGLVFQQ 91
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------TRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 92 SALFDSLTVAENVGFTLyrDSDLRPREIRAiveenLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPeqhqqykNIL 171
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGL--KGQWRDAALQA-----LAAVGLADRANEWPAALSGGQKQRVALARALIHRP-------GLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 172 LYDEPTAGLDpvASTRIE--SLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWD 233
Cdd:PRK11247 156 LLDEPLGALD--ALTRIEmqDLIESLWQQHGFTV--LLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-260 |
1.15e-38 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 137.24 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 39 VIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRqrsieegekalGVGLVFQQSALFDSLTVAENVGFTLYR 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvppHLR-----------HINMVFQSYALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 111 DSDLRpREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIES 190
Cdd:TIGR01187 70 RKVPR-AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPK-------ILLLDEPLSALDKKLRDQMQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 191 LIRHLLSQDHVCCCYliVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYksEHPllKQFFSGSIDGPIS 260
Cdd:TIGR01187 142 ELKTIQEQLGITFVF--VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIY--EEP--ANLFVARFIGEIN 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-245 |
2.00e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 138.04 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR------RQRSIEege 80
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlshvppYQRPIN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 kalgvgLVFQQSALFDSLTVAENVGFTLYRDSdLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVIN 160
Cdd:PRK11607 95 ------MMFQSYALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 161 PEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAY 240
Cdd:PRK11607 168 PK-------LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTC--VMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
....*
gi 499173792 241 ksEHP 245
Cdd:PRK11607 239 --EHP 241
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-238 |
2.58e-38 |
|
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: 140.67 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQPIIEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHrrqrSIEE-GE 80
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV----DLRDlDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 KAL--GVGLVFQQSALFDSlTVAENVgftLYRDSDLRPREIRAIveenLELVGLPGIGDRFP-----------AELSGGM 147
Cdd:COG4987 405 DDLrrRIAVVPQRPHLFDT-TLRENL---RLARPDATDEELWAA----LERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 148 RKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIFLYD 227
Cdd:COG4987 477 RRRLALARALLRDAP-------ILLLDEPTEGLDAATEQALLADLLEALAGRTV----LLITHRLAGLER-MDRILVLED 544
|
250
....*....|.
gi 499173792 228 GKIQWDGSTAD 238
Cdd:COG4987 545 GRIVEQGTHEE 555
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-236 |
4.88e-38 |
|
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: 132.88 E-value: 4.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH---RRQRSIEEgekalGV 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdvvREPREVRR-----RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLVFQQSALFDSLTVAENVgFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhq 165
Cdd:cd03265 76 GIVFQDLSVDDELTGWENL-YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE--- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 166 qyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGST 236
Cdd:cd03265 152 ----VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTI--LLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-234 |
6.15e-38 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 139.04 E-value: 6.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 11 FRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRqrsieegekalgVGLVFQ 90
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR------------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 91 QSALFDSLTVAENV--GFTLYRDSDLRPREIRAIVEENLE---------------------------LVGLpGIGDRFP- 140
Cdd:COG0488 69 EPPLDDDLTVLDTVldGDAELRALEAELEELEAKLAEPDEdlerlaelqeefealggweaearaeeiLSGL-GFPEEDLd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 141 ---AELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDpvastrIES---LIRHLLSQDHvccCYLIVTH--QF 212
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPD-------LLLLDEPTNHLD------LESiewLEEFLKNYPG---TVLVVSHdrYF 211
|
250 260
....*....|....*....|...
gi 499173792 213 stIDNTTDRIIFLYDGKIQ-WDG 234
Cdd:COG0488 212 --LDRVATRILELDRGKLTlYPG 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-230 |
7.03e-38 |
|
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: 132.00 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 13 GVSQSFGRKV-ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKALGVGLVFQ- 90
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRKSIGYVMQd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 91 -QSALFDSlTVAENVGFTLyRDSDLRPREIRAIveenLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqykn 169
Cdd:cd03226 80 vDYQLFTD-SVREELLLGL-KELDAGNEQAETV----LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD------- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 170 ILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAV---IVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-210 |
2.14e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 130.68 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD---SGEVIVHGHR------RQRsieegekalGVGLVF 89
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRltalpaEQR---------RIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 90 QQSALFDSLTVAENVGFTLyrDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqykn 169
Cdd:COG4136 83 QDDLLFPHLSVGENLAFAL--PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR------- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499173792 170 ILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTH 210
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPA--LLVTH 192
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-254 |
3.12e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 131.85 E-value: 3.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG-------HRRQ 73
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpDRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 74 RSIEEGEKAL-----GVGLVFQQSALFDSLTVAENV--------GftlyrdsdlRPR-EIRAIVEENLELVGLPGIGDRF 139
Cdd:COG4598 81 ELVPADRRQLqrirtRLGMVFQSFNLWSHMTVLENVieapvhvlG---------RPKaEAIERAEALLAKVGLADKRDAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 140 PAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccYLIVTHQFSTIDNTT 219
Cdd:COG4598 152 PAHLSGGQQQRAAIARALAMEPE-------VMLFDEPTSALDPELVGEVLKVMRDLAEEGRT---MLVVTHEMGFARDVS 221
|
250 260 270
....*....|....*....|....*....|....*...
gi 499173792 220 DRIIFLYDGKIQWDGSTADAY---KSEHplLKQFFSGS 254
Cdd:COG4598 222 SHVVFLHQGRIEEQGPPAEVFgnpKSER--LRQFLSSS 257
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-230 |
4.95e-37 |
|
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: 129.71 E-value: 4.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHrrQRSIEEGEKalgVGLV 88
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK--PLDIAARNR---IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSALFDSLTVAENVGFtLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyk 168
Cdd:cd03269 76 PEERGLYPKMKVIDQLVY-LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE------ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 169 nILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03269 149 -LLILDEPFSGLDPVNVELLKDVIRELARAGKTV---ILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-230 |
8.15e-37 |
|
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: 130.15 E-value: 8.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEE--GEKAlGVGLVFQQSALFDSLTVA 101
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNlpPEKR-DISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 102 ENVGFTLYRDSDLRPrEIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLD 181
Cdd:cd03299 90 KNIAYGLKKRKVDKK-EIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK-------ILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499173792 182 PvastRIESLIRHLLS--QDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03299 162 V----RTKEKLREELKkiRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-241 |
8.77e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 131.32 E-value: 8.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG---HRRQRSIEEGEKAlgVGLVFQ--QSALF 95
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdiTDKKVKLSDIRKK--VGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 96 DSlTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLP--GIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLY 173
Cdd:PRK13637 98 EE-TIEKDIAFGP-INLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPK-------ILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 174 DEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYK 241
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKEL--HKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-229 |
9.46e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 132.65 E-value: 9.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH---RRQRSIEegekaLGV 85
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpARARLAR-----ARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLVFQQSALFDSLTVAENVgFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhq 165
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ--- 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 166 qyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:PRK13536 193 ----LLILDEPTTGLDPHARHLIWERLRSLLARGKTI---LLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-252 |
1.20e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 129.87 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS-----GEVIVHGHR----RQRSIEEG 79
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTARslsqQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 80 EKAlgVGLVFQQSALFDSLTVAENV--GFTLYRDSdlrPR-EIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARA 156
Cdd:PRK11264 84 RQH--VGFVFQNFNLFPHRTVLENIieGPVIVKGE---PKeEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 157 IVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGST 236
Cdd:PRK11264 159 LAMRPE-------VILFDEPTSALDPELVGEVLNTIRQLAQEKRT---MVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
250
....*....|....*..
gi 499173792 237 ADAYKS-EHPLLKQFFS 252
Cdd:PRK11264 229 KALFADpQQPRTRQFLE 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-238 |
1.20e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.15 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQ-RSIEEGEKAlG 84
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAA-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQQSALFDSLTVAENV--GFTLYRDSDLRPREIRAIVEENLELVGL---PgigDRFPAELSGGMRKRVSLARAIVI 159
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIflGREPRRGGLIDWRAMRRRARELLARLGLdidP---DTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:COG1129 158 DAR-------VLILDEPTASLTEREVERLFRIIRRLKAQG-VAI--IYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-238 |
1.47e-36 |
|
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: 132.53 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 26 DVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------------HRRQrsieegekalgVGLVFQQ 91
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflppHRRR-----------IGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 92 SALFDSLTVAENVGFTLYR-DSDLRPREIRAIVeenlELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknI 170
Cdd:COG4148 86 ARLFPHLSVRGNLLYGRKRaPRAERRISFDEVV----ELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPR-------L 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 171 LLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:COG4148 155 LLMDEPLAALDLARKAEILPYLERL--RDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-230 |
1.55e-36 |
|
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: 135.66 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRqRSIEEGEKALGVGL 87
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL-SDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFdSLTVAENVgfTLYRdSDLRPREIRAIVEE-NL-ELV-GLPG-----IGDRfPAELSGGMRKRVSLARAIVI 159
Cdd:COG4988 416 VPQNPYLF-AGTIRENL--RLGR-PDASDEELEAALEAaGLdEFVaALPDgldtpLGEG-GRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVCccyLIVTHQFSTIDNtTDRIIFLYDGKI 230
Cdd:COG4988 491 DAP-------LLLLDEPTAHLDAETEAEILQALRR-LAKGRTV---ILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-195 |
1.64e-36 |
|
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: 128.71 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVGLV 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSALFDSLTVAENVGFTLYRdsdLRPREIRAIVEENLELvglpgigdrFPA----------ELSGGMRKRVSLARAIV 158
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYA---RRRAKRKARLERVYEL---------FPRlkerrkqlagTLSGGEQQMLAIARALM 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 499173792 159 INPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHL 195
Cdd:cd03224 149 SRPK-------LLLLDEPSEGLAPKIVEEIFEAIREL 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-234 |
2.59e-36 |
|
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: 127.17 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 10 EFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIeegekalgvglvf 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG----KDL------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 90 qqsalfdsltvaenvgftlyrdSDLRPREI---RAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:cd03214 64 ----------------------ASLSPKELarkIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP---- 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVCCCyLIVTH------QFStidnttDRIIFLYDGKIQWDG 234
Cdd:cd03214 118 ---ILLLDEPTSHLDIAHQIELLELLRR-LARERGKTV-VMVLHdlnlaaRYA------DRVILLKDGRIVAQG 180
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-245 |
3.66e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 130.62 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSF-------GRKVI----LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQR 74
Cdd:COG4608 5 EPLLEVRDLKKHFpvrgglfGRTVGvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 75 SIEEGEKAL--GVGLVFQ--QSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGL-PGIGDRFPAELSGGMRK 149
Cdd:COG4608 85 LSGRELRPLrrRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 150 RVSLARAIVINPEqhqqyknILLYDEPTAGLDpVAstrIESLIRHLLS--QDHVCCCYLIVTHQFSTIDNTTDRIIFLYD 227
Cdd:COG4608 165 RIGIARALALNPK-------LIVCDEPVSALD-VS---IQAQVLNLLEdlQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250
....*....|....*....
gi 499173792 228 GKIQWDGSTADAYKS-EHP 245
Cdd:COG4608 234 GKIVEIAPRDELYARpLHP 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-241 |
3.69e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 128.66 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEpvqpIIEFRGVSQSF----------------------GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLL 58
Cdd:COG1134 1 MSS----MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 59 TPDSGEVIVHGhrRQRSIeegekaLGVGLVFQQsalfdSLTVAENVGF--TLYrdsDLRPREIRAIVEENLELVglpGIG 136
Cdd:COG1134 77 EPTSGRVEVNG--RVSAL------LELGAGFHP-----ELTGRENIYLngRLL---GLSRKEIDEKFDEIVEFA---ELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 137 DRFPAEL---SGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPV----ASTRIESLIRHllsqdhvCCCYLIVT 209
Cdd:COG1134 138 DFIDQPVktySSGMRARLAFAVATAVDPD-------ILLVDEVLAVGDAAfqkkCLARIRELRES-------GRTVIFVS 203
|
250 260 270
....*....|....*....|....*....|..
gi 499173792 210 HQFSTIDNTTDRIIFLYDGKIQWDGSTADAYK 241
Cdd:COG1134 204 HSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-230 |
3.84e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 134.91 E-value: 3.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 3 EPVQPIIEFRGVSqsF---GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH--------- 70
Cdd:COG1132 334 PPVRGEIEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltles 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 -RRQrsieegekalgVGLVFQQSALFdSLTVAENVGFTlyrdsdlRPREIRAIVEENLELVG-------LPG-----IGD 137
Cdd:COG1132 412 lRRQ-----------IGVVPQDTFLF-SGTIRENIRYG-------RPDATDEEVEEAAKAAQahefieaLPDgydtvVGE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 138 RFpAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLsQDHVCccyLIVTHQFSTIDN 217
Cdd:COG1132 473 RG-VNLSGGQRQRIAIARALLKDPP-------ILILDEATSALDTETEALIQEALERLM-KGRTT---IVIAHRLSTIRN 540
|
250
....*....|...
gi 499173792 218 tTDRIIFLYDGKI 230
Cdd:COG1132 541 -ADRILVLDDGRI 552
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-198 |
8.61e-36 |
|
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: 126.00 E-value: 8.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKAL-----GVGLVFQ--Q 91
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG----EPLDYSRKGLlerrqRVGLVFQdpD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 92 SALFdSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknIL 171
Cdd:TIGR01166 79 DQLF-AADVDQDVAFGP-LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPD-------VL 149
|
170 180
....*....|....*....|....*..
gi 499173792 172 LYDEPTAGLDPVASTRIESLIRHLLSQ 198
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAE 176
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-258 |
9.81e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 127.84 E-value: 9.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 11 FRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVhGHRRQRSIEEGEKalGVGLVFQ 90
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPPAER--GVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 91 QSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPeqhqqykNI 170
Cdd:PRK11000 83 SYALYPHLSVAENMSFGL-KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP-------SV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 171 LLYDEPTAGLDpvASTRIEslIRHLLSQDH--VCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYkseHPLLK 248
Cdd:PRK11000 155 FLLDEPLSNLD--AALRVQ--MRIEISRLHkrLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY---HYPAN 227
|
250
....*....|
gi 499173792 249 QFFSGSIDGP 258
Cdd:PRK11000 228 RFVAGFIGSP 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-243 |
3.02e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 125.30 E-value: 3.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRsiee 78
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarHARQR---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekalgVGLVFQQSALFDSLTVAENVgFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIV 158
Cdd:PRK13537 82 ------VGVVPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 159 INPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:PRK13537 155 NDPD-------VLVLDEPTTGLDPQARHLMWERLRSLLARGKTI---LLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
....*
gi 499173792 239 AYKSE 243
Cdd:PRK13537 225 LIESE 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-242 |
8.08e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 123.68 E-value: 8.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSI--------EEg 79
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylpEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 80 ekalgvglvfqqSALFDSLTVAENVGFtLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVI 159
Cdd:COG4152 80 ------------RGLYPKMKVGEQLVY-LARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADA 239
Cdd:COG4152 147 DPE-------LLILDEPFSGLDPVNVELLKDVIRELAAKG---TTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
...
gi 499173792 240 YKS 242
Cdd:COG4152 217 RRQ 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-245 |
1.07e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 122.87 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 13 GVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL--GVGLVFQ 90
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 91 QS--ALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGL-PGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqy 167
Cdd:PRK10419 97 DSisAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPK----- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 168 knILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSEHP 245
Cdd:PRK10419 172 --LLILDEAVSNLDLVLQAGVIRLLKKL--QQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSP 245
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-243 |
3.03e-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: 120.80 E-value: 3.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKV--ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------RRQrsi 76
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 eegekalgVGLVFQQSALFDSlTVAENVGFTlyrdsdlRPREIRAIVEENLELV-------GLPG-----IGDRfPAELS 144
Cdd:cd03251 78 --------IGLVSQDVFLFND-TVAENIAYG-------RPGATREEVEEAARAAnahefimELPEgydtvIGER-GVKLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 145 GGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIF 224
Cdd:cd03251 141 GGQRQRIAIARALLKDPP-------ILILDEATSALDTESERLVQAALERLMKNRTT----FVIAHRLSTIEN-ADRIVV 208
|
250
....*....|....*....
gi 499173792 225 LYDGKIQWDGSTADAYKSE 243
Cdd:cd03251 209 LEDGKIVERGTHEELLAQG 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-255 |
3.23e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.17 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGL--LTPD---SGEVIVHGhRRQRSIEEGE 80
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDG-QDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 KALGVGLVFQQSALFDSLTVAENV--GFTLYRDSDLRpREIRAIVEENLELVGL-PGIGDRFPA---ELSGGMRKRVSLA 154
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENValGLKLNRLVKSK-KELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 155 RAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:PRK14247 159 RALAFQPE-------VLLADEPTANLDPENTAKIESLFLELKKDMTI----VLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
250 260
....*....|....*....|..
gi 499173792 235 STADAY-KSEHPLLKQFFSGSI 255
Cdd:PRK14247 228 PTREVFtNPRHELTEKYVTGRL 249
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-211 |
3.96e-33 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 119.59 E-value: 3.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHrrqrSIEEGEKALGVGLVFQQSALFDSL 98
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG----DIDDPDVAEACHYLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 99 TVAENVGF--TLYRDSDLRpreiraiVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVInpeqhqqYKNILLYDEP 176
Cdd:PRK13539 89 TVAENLEFwaAFLGGEELD-------IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS-------NRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|....*
gi 499173792 177 TAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQ 211
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIV---IAATHI 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-243 |
5.38e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.73 E-value: 5.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKV-----ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEV--IVHGHRRQRSIEEGEK 81
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 82 ALG---------------------VGLVFQ--QSALFDSlTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLP-GIGD 137
Cdd:PRK13651 83 VLEklviqktrfkkikkikeirrrVGVVFQfaEYQLFEQ-TIEKDIIFGP-VSMGVSKEEAKKRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 138 RFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDN 217
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPD-------FLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTI---ILVTHDLDNVLE 230
|
250 260
....*....|....*....|....*.
gi 499173792 218 TTDRIIFLYDGKIQWDGSTADAYKSE 243
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDILSDN 256
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-234 |
6.41e-33 |
|
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: 119.62 E-value: 6.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHrRQRSIEEGEKALGVG 86
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT-DIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFdSLTVAENVGFTLYRDSDLRpreiraiVEENLELVGLPGIGDRFP-----------AELSGGMRKRVSLAR 155
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLADDER-------ILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 156 AIVINPeqhqqykNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFStIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03245 154 ALLNDP-------PILLLDEPTSAMDMNSEERLKERLRQLLGDKTL----IIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-232 |
7.38e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.18 E-value: 7.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIvHGHRrqrsieegekaLGVG 86
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGET-----------VKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFD-SLTVAENVgftlyRD--SDLRPREIRAIveenLELVGLPG------IGDrfpaeLSGGMRKRVSLARAI 157
Cdd:COG0488 382 YFDQHQEELDpDKTVLDEL-----RDgaPGGTEQEVRGY----LGRFLFSGddafkpVGV-----LSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 158 VINPeqhqqykNILLYDEPTAGLDPVAstrIESLIRHLLSqdhvcccY----LIVTH--QFstIDNTTDRIIFLYDGKIQ 231
Cdd:COG0488 448 LSPP-------NVLLLDEPTNHLDIET---LEALEEALDD-------FpgtvLLVSHdrYF--LDRVATRILEFEDGGVR 508
|
.
gi 499173792 232 W 232
Cdd:COG0488 509 E 509
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-234 |
9.27e-33 |
|
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: 118.42 E-value: 9.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 15 SQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTP--DSGEVIVHGhrRQRSIEEGEKAlgVGLVFQQS 92
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLING--RPLDKRSFRKI--IGYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 93 ALFDSLTVAENVGFTLyrdsdlrprEIRAIveenlelvglpgigdrfpaelSGGMRKRVSLARAIVINPeqhqqykNILL 172
Cdd:cd03213 92 ILHPTLTVRETLMFAA---------KLRGL---------------------SGGERKRVSIALELVSNP-------SLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 173 YDEPTAGLDPVASTRIESLIRHLLSQDHVCCCyliVTHQFST-IDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADTGRTIIC---SIHQPSSeIFELFDKLLLLSQGRVIYFG 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-233 |
1.54e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.42 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGR-----KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQR 74
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 75 SIeegekalgvGLVFQqsalfD-------SLTVAENVGFTLYRDS--DLRP---REIRAIVEENLELVGLpGIGDRFPAE 142
Cdd:COG1101 81 YI---------GRVFQ-----DpmmgtapSMTIEENLALAYRRGKrrGLRRgltKKRRELFRELLATLGL-GLENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 143 ---LSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTT 219
Cdd:COG1101 146 vglLSGGQRQALSLLMATLTKPK-------LLLLDEHTAALDPKTAALVLELTEKIVEENNLTT--LMVTHNMEQALDYG 216
|
250
....*....|....
gi 499173792 220 DRIIFLYDGKIQWD 233
Cdd:COG1101 217 NRLIMMHEGRIILD 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-225 |
1.94e-32 |
|
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: 123.94 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKAL-- 83
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG----VPLADADADSwr 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 -GVGLVFQQSALFDSlTVAENVGFTlyrdsdlRPREIRAIVEENLELVG-------LPG-----IGDRfPAELSGGMRKR 150
Cdd:TIGR02857 396 dQIAWVPQHPFLFAG-TIAENIRLA-------RPDASDAEIREALERAGldefvaaLPQgldtpIGEG-GAGLSGGQAQR 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499173792 151 VSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIFL 225
Cdd:TIGR02857 467 LALARAFLRDAP-------LLLLDEPTAHLDAETEAEVLEALRALAQGRTV----LLVTHRLALAAL-ADRIVVL 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-243 |
2.42e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.60 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrRQRSIEEGEKA--L 83
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG--KPVRIRSPRDAiaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 GVGLVFQQSALFDSLTVAENVgfTLYRDSD----LRPREIRAIVEENLELVGL---PgigDRFPAELSGGMRKRVSLARA 156
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENI--VLGLEPTkggrLDRKAARARIRELSERYGLdvdP---DAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 157 IVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDH-VcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGS 235
Cdd:COG3845 156 LYRGAR-------ILILDEPTAVLTPQEADELFEILRRLAAEGKsI----IFITHKLREVMAIADRVTVLRRGKVVGTVD 224
|
....*...
gi 499173792 236 TADAYKSE 243
Cdd:COG3845 225 TAETSEEE 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
9-235 |
3.01e-32 |
|
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: 117.89 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGekalgVGLV 88
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHK-----IGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSALFDSLTVAEN--VGFTLYRDSDLRpreiraiVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:TIGR03740 76 IESPPLYENLTARENlkVHTTLLGLPDSR-------IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK---- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGS 235
Cdd:TIGR03740 145 ---LLILDEPTNGLDPIGIQELRELIRSFPEQG---ITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-238 |
3.75e-32 |
|
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: 117.78 E-value: 3.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRsiee 78
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglppHRIAR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekaLGVGLVFQQSALFDSLTVAEN--VGFTLYRDsdlrPREIRAIVEENLELvglpgigdrFP--AE--------LSGG 146
Cdd:COG0410 78 ----LGIGYVPEGRRIFPSLTVEENllLGAYARRD----RAEVRADLERVYEL---------FPrlKErrrqragtLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 147 MRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDH-VcccyLIVTHQFSTIDNTTDRIIFL 225
Cdd:COG0410 141 EQQMLAIGRALMSRPK-------LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVtI----LLVEQNARFALEIADRAYVL 209
|
250
....*....|...
gi 499173792 226 YDGKIQWDGSTAD 238
Cdd:COG0410 210 ERGRIVLEGTAAE 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-248 |
4.61e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.55 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGR--KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQR-SIEEGEKA 82
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKeNLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 lgVGLVFQ----QsalFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIV 158
Cdd:PRK13632 85 --IGIIFQnpdnQ---FIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 159 INPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLI-VTHQFSTIDNtTDRIIFLYDGKIQWDGSTA 237
Cdd:PRK13632 159 LNPE-------IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKT---LIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPK 227
|
250
....*....|.
gi 499173792 238 DAYKSEHPLLK 248
Cdd:PRK13632 228 EILNNKEILEK 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-255 |
5.34e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 118.15 E-value: 5.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPIIEFRgvsQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhRRQRSIEEGE 80
Cdd:PRK10619 1 MSENKLNVIDLH---KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG-QTINLVRDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 KALGVG-------------LVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIG-DRFPAELSGG 146
Cdd:PRK10619 77 GQLKVAdknqlrllrtrltMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 147 MRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccYLIVTHQFSTIDNTTDRIIFLY 226
Cdd:PRK10619 157 QQQRVSIARALAMEPE-------VLLFDEPTSALDPELVGEVLRIMQQLAEEGKT---MVVVTHEMGFARHVSSHVIFLH 226
|
250 260 270
....*....|....*....|....*....|
gi 499173792 227 DGKIQWDGSTADAYKS-EHPLLKQFFSGSI 255
Cdd:PRK10619 227 QGKIEEEGAPEQLFGNpQSPRLQQFLKGSL 256
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-255 |
7.23e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 117.64 E-value: 7.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGL--LTPDS---GEVIVHGHR-RQRSIEEGEKA 82
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNiYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 LGVGLVFQQSALFDSLTVAENVGFTLYRDSDLRPR-EIRAIVEENLELVGL-PGIGDR---FPAELSGGMRKRVSLARAI 157
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKkELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 158 VINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTA 237
Cdd:PRK14267 165 AMKPK-------ILLMDEPTANIDPVGTAKIEELLFELKKEYTI----VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
250
....*....|....*....
gi 499173792 238 DAYKS-EHPLLKQFFSGSI 255
Cdd:PRK14267 234 KVFENpEHELTEKYVTGAL 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-235 |
8.77e-32 |
|
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: 116.82 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG--RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------RRQrsi 76
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 eegekalgVGLVFQQSALFdSLTVAENVGFTlyrdsdlRPREIRAIVEENLELVG-------LPG-----IGDRfPAELS 144
Cdd:cd03252 78 --------VGVVLQENVLF-NRSIRDNIALA-------DPGMSMERVIEAAKLAGahdfiseLPEgydtiVGEQ-GAGLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 145 GGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIF 224
Cdd:cd03252 141 GGQRQRIAIARALIHNPR-------ILIFDEATSALDYESEHAIMRNMHDICAGRTV----IIIAHRLSTVKN-ADRIIV 208
|
250
....*....|.
gi 499173792 225 LYDGKIQWDGS 235
Cdd:cd03252 209 MEKGRIVEQGS 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-230 |
9.99e-32 |
|
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: 114.45 E-value: 9.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQ-RSIEEGeKALGVGL 87
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDA-RRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQqsalfdsltvaenvgftlyrdsdlrpreiraiveenlelvglpgigdrfpaeLSGGMRKRVSLARAIVINPEqhqqy 167
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNAR----- 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 168 knILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03216 103 --LLILDEPTAALTPAEVERLFKVIRRLRAQGVAV---IFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-231 |
2.92e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 115.26 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQPIIEFRGVSQSFGRK----VILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEG 79
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 80 EKAL---GVGLVFQQSALFDSLTVAENVGF-TLYRDSDLRPREIRAIveENLELVGLPGIGDRFPAELSGGMRKRVSLAR 155
Cdd:PRK10584 82 RAKLrakHVGFVFQSFMLIPTLNALENVELpALLRGESSRQSRNGAK--ALLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 156 AIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVCCCYLiVTHQfSTIDNTTDRIIFLYDGKIQ 231
Cdd:PRK10584 160 AFNGRPD-------VLFADEPTGNLDRQTGDKIADLLFS-LNREHGTTLIL-VTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-245 |
3.67e-31 |
|
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: 120.56 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 18 FGRKV----ILDDVDLKIYPGEAVGVIGPSGTGKST----ILRivaglLTPDSGEVIVHGHRRQRSIEEGEKAL--GVGL 87
Cdd:COG4172 292 FRRTVghvkAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLR-----LIPSEGEIRFDGQDLDGLSRRALRPLrrRMQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQ--SALFDSLTVAENV--GFTLYRDsDLRPREIRAIVEENLELVGL-PGIGDRFPAELSGGMRKRVSLARAIVINPE 162
Cdd:COG4172 367 VFQDpfGSLSPRMTVGQIIaeGLRVHGP-GLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 163 qhqqyknILLYDEPTAGLDpvASTR--IESLIRHL-----LSqdhvcccYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGS 235
Cdd:COG4172 446 -------LLVLDEPTSALD--VSVQaqILDLLRDLqrehgLA-------YLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
250
....*....|.
gi 499173792 236 TADAYKS-EHP 245
Cdd:COG4172 510 TEQVFDApQHP 520
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-234 |
4.32e-31 |
|
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: 114.94 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrRQRSIeegekaLGVGLVFQqsalfDSL 98
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVSSL------LGLGGGFN-----PEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 99 TVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTA 178
Cdd:cd03220 100 TGRENIYLNG-RLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPD-------ILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 179 GLDpvASTRIESL--IRHLLSQDHVcccYLIVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03220 172 VGD--AAFQEKCQrrLRELLKQGKT---VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-251 |
7.59e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.80 E-value: 7.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH--RRQRSiEEGEKALGvg 86
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvATTPS-RELAKRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 lVFQQSALFDS-LTVAENVGFTLYRDSDLRP-REIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVinpeqh 164
Cdd:COG4604 79 -ILRQENHINSrLTVRELVAFGRFPYSKGRLtAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 165 QQYKNILLyDEPTAGLDPVASTRIESLIRHlLSQDH---VcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYK 241
Cdd:COG4604 152 QDTDYVLL-DEPLNNLDMKHSVQMMKLLRR-LADELgktV----VIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
250
....*....|
gi 499173792 242 SEhpLLKQFF 251
Cdd:COG4604 226 PE--VLSDIY 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-243 |
1.01e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 117.64 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEE-GEKALG- 84
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG----DDVEAlSARAASr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 -VGLVFQQSAL---FDSLTVAEnVGFTLYRDSDLRPREI-RAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVi 159
Cdd:PRK09536 78 rVASVPQDTSLsfeFDVRQVVE-MGRTPHRSRFDTWTETdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 160 npeqhqQYKNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADA 239
Cdd:PRK09536 156 ------QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTA---VAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
....
gi 499173792 240 YKSE 243
Cdd:PRK09536 227 LTAD 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-187 |
1.64e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.03 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 13 GVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRrqrsiEEGEKAlGVGLVFQQS 92
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGA-ERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 93 ALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILL 172
Cdd:PRK11248 80 GLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ-------LLL 151
|
170
....*....|....*
gi 499173792 173 YDEPTAGLDpvASTR 187
Cdd:PRK11248 152 LDEPFGALD--AFTR 164
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-238 |
2.06e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 118.23 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVG 86
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLEL-----VGLPGIGDRFPAE-LSGGMRKrvslARaivin 160
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLdldssAGSLEVADRQIVEiLRGLMRD----SR----- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 161 peqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:PRK15439 161 ---------ILILDEPTASLTPAETERLFSRIRELLAQGV---GIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-230 |
2.12e-30 |
|
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: 113.09 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKV-ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhRRQRSIEEGEKALGVGL 87
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG-IDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFdSLTVAENVGFTlyrdsdlRPREIRAIVEENLELVGLPGIGDRFP-----------AELSGGMRKRVSLARA 156
Cdd:cd03254 82 VLQDTFLF-SGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 157 IVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIFLYDGKI 230
Cdd:cd03254 154 MLRDPK-------ILILDEATSNIDTETEKLIQEALEKLMKGRTS----IIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-230 |
3.58e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.63 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGR-KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKAL--- 83
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG----EPIKYDKKSLlev 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 --GVGLVFQQS--ALFdSLTVAENVGFTLYrDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVI 159
Cdd:PRK13639 77 rkTVGIVFQNPddQLF-APTVEEDVAFGPL-NLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:PRK13639 155 KPE-------IIVLDEPTSGLDPMGASQIMKLLYDLNKEG---ITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-211 |
7.70e-30 |
|
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: 110.91 E-value: 7.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--HRRQRSiEEGEKALGVG 86
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtpLAEQRD-EPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 lvfQQSALFDSLTVAENVGFtLYRDSDLRPREIraivEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:TIGR01189 80 ---HLPGLKPELSALENLHF-WAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRP---- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIR-HLLSQDHVcccyLIVTHQ 211
Cdd:TIGR01189 148 ---LWILDEPTTALDKAGVALLAGLLRaHLARGGIV----LLTTHQ 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-255 |
1.54e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 111.68 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH-----RRQRSIEEGEKALGVGLVFQQSALF 95
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 96 DSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGL-PGIGDRF--PA-ELSGGMRKRVSLARAIVINPEqhqqyknIL 171
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLnsPAsQLSGGQQQRLTIARALALKPK-------VL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 172 LYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKS-EHPLLKQF 250
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAI----VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSpKNELTEKY 251
|
....*
gi 499173792 251 FSGSI 255
Cdd:PRK14246 252 VIGRI 256
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-253 |
2.04e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.36 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSF----GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrQRSIEEGEKA 82
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG---QDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 LGV------GLVFQQSALFDSLTVAENVGF-TLYRDSDLRPREIRAIveenlELVGLPGIGDRF---PAELSGGMRKRVS 152
Cdd:PRK10535 80 LAQlrrehfGFIFQRYHLLSHLTAAQNVEVpAVYAGLERKQRLLRAQ-----ELLQRLGLEDRVeyqPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 153 LARAIvINPEQhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQfSTIDNTTDRIIFLYDGKIQW 232
Cdd:PRK10535 155 IARAL-MNGGQ------VILADEPTGALDSHSGEEVMAILHQLRDRGHTV---IIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
250 260 270
....*....|....*....|....*....|
gi 499173792 233 DG---STADAYKSEHPLL------KQFFSG 253
Cdd:PRK10535 224 NPpaqEKVNVAGGTEPVVntasgwRQFVSG 253
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-238 |
2.69e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.49 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsiEEGEKALGVGLVF-QQSALFDSLTVAE 102
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK--RRKEFARRIGVVFgQRSQLWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 103 NvgFTLYRD-SDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLD 181
Cdd:COG4586 116 S--FRLLKAiYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPK-------ILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 182 PVASTRIESLIRHlLSQDHvCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:COG4586 187 VVSKEAIREFLKE-YNRER-GTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE 241
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
3.40e-29 |
|
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: 115.15 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 2 SEPVQPIIEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQrSIEEGE 80
Cdd:TIGR02868 328 VGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 KALGVGLVFQQSALFDSlTVAENVGFTlyrdsdlRPREIRAIVEENLELVGLPGIGDRFP-----------AELSGGMRK 149
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDT-TVRENLRLA-------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQ 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 150 RVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQ 211
Cdd:TIGR02868 479 RLALARALLADAP-------ILLLDEPTEHLDAETADELLEDLLAALSGRTV----VLITHH 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-230 |
3.51e-29 |
|
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: 108.46 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG--RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVhGHRRQRSIEEGEKALGVG 86
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFDSlTVAENVgftlyrdsdlrpreiraiveenlelvglpgigdrfpaeLSGGMRKRVSLARAIVINPEqhqq 166
Cdd:cd03246 80 YLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPR---- 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccYLIVTHQFSTIdNTTDRIIFLYDGKI 230
Cdd:cd03246 117 ---ILVLDEPNSHLDVEGERALNQAIAALKAAGAT---RIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-240 |
4.91e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.25 E-value: 4.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIV--AGLLTPD---SGEVIVHGH----RRQRSI 76
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEGEKalgVGLVFQQSALFdSLTVAENVGFTLyRDSDLRPREI-RAIVEENLELVGL-PGIGDRFPAE---LSGGMRKRV 151
Cdd:PRK14239 83 DLRKE---IGMVFQQPNPF-PMSIYENVVYGL-RLKGIKDKQVlDEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 152 SLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIrHLLSQDHVcccYLIVTHQFSTIDNTTDRIIFLYDGKIQ 231
Cdd:PRK14239 158 CIARVLATSPK-------IILLDEPTSALDPISAGKIEETL-LGLKDDYT---MLLVTRSMQQASRISDRTGFFLDGDLI 226
|
....*....
gi 499173792 232 WDGSTADAY 240
Cdd:PRK14239 227 EYNDTKQMF 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-236 |
9.42e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 109.72 E-value: 9.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 5 VQPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS---GEVIVHGHRRQRsieEGEK 81
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQR---EGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 82 ALGV-------GLVFQQSALFDSLTVAENV-----GFTLYRDSDLR--PREIRAIVEENLELVGLPGIGDRFPAELSGGM 147
Cdd:PRK09984 78 ARDIrksrantGYIFQQFNLVNRLSVLENVligalGSTPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 148 RKRVSLARAIVinpeqhQQYKnILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVT-HQFSTIDNTTDRIIFLY 226
Cdd:PRK09984 158 QQRVAIARALM------QQAK-VILADEPIASLDPESARIVMDTLRDINQNDGIT---VVVTlHQVDYALRYCERIVALR 227
|
250
....*....|
gi 499173792 227 DGKIQWDGST 236
Cdd:PRK09984 228 QGHVFYDGSS 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-245 |
1.14e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 111.47 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKV-ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEvIVHGHRRQRSIEEGEKalGVGL 87
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIGGRVVNELEPADR--DIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqy 167
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGL-KIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 168 knILLYDEPTAGLDPV--ASTRIEslIRHLLSQDHVCCCYliVTHqfstiDNT-----TDRIIFLYDGKIQWDGSTADAY 240
Cdd:PRK11650 155 --VFLFDEPLSNLDAKlrVQMRLE--IQRLHRRLKTTSLY--VTH-----DQVeamtlADRVVVMNGGVAEQIGTPVEVY 223
|
....*
gi 499173792 241 ksEHP 245
Cdd:PRK11650 224 --EKP 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-248 |
1.36e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 109.72 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------RRQrsieegekalgVGLVFQ--- 90
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwdvRRQ-----------VGMVFQnpd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 91 -QsalFDSLTVAENVGFTLYRDSDLRPREIRAiVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqykn 169
Cdd:PRK13635 92 nQ---FVGATVQDDVAFGLENIGVPREEMVER-VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 170 ILLYDEPTAGLDPVAstRIESL--IRHLLSQDHVCCcyLIVTHQfstIDN--TTDRIIFLYDGKIQWDGSTADAYKSEHP 245
Cdd:PRK13635 161 IIILDEATSMLDPRG--RREVLetVRQLKEQKGITV--LSITHD---LDEaaQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
...
gi 499173792 246 LLK 248
Cdd:PRK13635 234 LQE 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-234 |
1.40e-28 |
|
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: 108.57 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR--RQRSieegEKALGVGLVF-QQSALFDS 97
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRK----KFLRRIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTVAEnvGFTLYRD-SDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEP 176
Cdd:cd03267 110 LPVID--SFYLLAAiYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE-------ILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 177 TAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTV--LLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-230 |
1.65e-28 |
|
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: 108.47 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG-RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEKALGVg 86
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDiREVTLDSLRRAIGV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 lVFQQSALFDSlTVAENVGftlYRDSDLRPREIR-----AIVEEnlELVGLPG-----IGDRfPAELSGGMRKRVSLARA 156
Cdd:cd03253 80 -VPQDTVLFND-TIGYNIR---YGRPDATDEEVIeaakaAQIHD--KIMRFPDgydtiVGER-GLKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 157 IVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIFLYDGKI 230
Cdd:cd03253 152 ILKNPP-------ILLLDEATSALDTHTEREIQAALRDVSKGRTT----IVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
9-241 |
2.19e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.06 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF-------GRKviLDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG-----HRRQRSI 76
Cdd:PRK13649 3 INLQNVSYTYqagtpfeGRA--LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitsTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEGEKAlgVGLVFQ--QSALFDSlTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLP-GIGDRFPAELSGGMRKRVSL 153
Cdd:PRK13649 81 KQIRKK--VGLVFQfpESQLFEE-TVLKDVAFGP-QNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 154 ARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsqDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWD 233
Cdd:PRK13649 157 AGILAMEPK-------ILVLDEPTAGLDPKGRKELMTLFKKL---HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
....*...
gi 499173792 234 GSTADAYK 241
Cdd:PRK13649 227 GKPKDIFQ 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-229 |
3.79e-28 |
|
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: 104.84 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHghrrqrsieegeKALGVGlV 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKIG-Y 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQsalfdsltvaenvgftlyrdsdlrpreiraiveenlelvglpgigdrfpaeLSGGMRKRVSLARAIVINPeqhqqyk 168
Cdd:cd03221 68 FEQ---------------------------------------------------LSGGEKMRLALAKLLLENP------- 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 169 NILLYDEPTAGLDPVAstrIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:cd03221 90 NLLLLDEPTNHLDLES---IEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-241 |
5.61e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 108.28 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS-----GEVIVHGHRRQRSIEEGEKALGVGLVFQQSALFDSl 98
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEgkvtvGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 99 TVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPG-IGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPT 177
Cdd:PRK13643 101 TVLKDVAFGP-QNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPE-------VLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 178 AGLDPVAstRIEsLIRHLLSQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYK 241
Cdd:PRK13643 173 AGLDPKA--RIE-MMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-234 |
7.82e-28 |
|
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: 105.09 E-value: 7.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG--RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVg 86
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 lVFQQSALFDSlTVAENVGftlyrdsdlrpreiraiveenlelvglpgigdrfpAELSGGMRKRVSLARAIVinpeqhqQ 166
Cdd:cd03247 80 -LNQRPYLFDT-TLRNNLG-----------------------------------RRFSGGERQRLALARILL-------Q 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 167 YKNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIFLYDGKIQWDG 234
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL----IWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-249 |
8.69e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 8.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQPIIEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGE---VIVHGhrrqrsIEE 78
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDG------ITL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 GEKAL-----GVGLVFQQ-SALFDSLTVAENVGFTLYRDSDLRPREIRaIVEENLELVGLPGIGDRFPAELSGGMRKRVS 152
Cdd:PRK13640 75 TAKTVwdireKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIK-IVRDVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 153 LARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQfstID--NTTDRIIFLYDGKI 230
Cdd:PRK13640 154 IAGILAVEPK-------IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTV--ISITHD---IDeaNMADQVLVLDDGKL 221
|
250
....*....|....*....
gi 499173792 231 QWDGSTADAYKSEHpLLKQ 249
Cdd:PRK13640 222 LAQGSPVEIFSKVE-MLKE 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-231 |
1.09e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 106.05 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 23 ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL---GVGLVFQQSALFDSLT 99
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 100 VAENVGFTLYRdSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPeqhqqykNILLYDEPTAG 179
Cdd:PRK11629 104 ALENVAMPLLI-GKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP-------RLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499173792 180 LDPVASTRIESLIRHLLSQDHVccCYLIVTHQFStIDNTTDRIIFLYDGKIQ 231
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGT--AFLVVTHDLQ-LAKRMSRQLEMRDGRLT 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-230 |
2.97e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.39 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQR----SIEEGEK 81
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLrdlyALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 82 ALGV----GLVFQQSA--LFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPG--IGDRfPAELSGGMRKRVSL 153
Cdd:PRK11701 84 RRLLrtewGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAarIDDL-PTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 154 ARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:PRK11701 163 ARNLVTHPR-------LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAV--VIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-235 |
3.62e-27 |
|
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: 104.93 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRK---VILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------RRQrs 75
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlRSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 76 ieegekalgVGLVFQQSALFDSlTVAENVGFTLYRDSDlrPREIRAIVEENLE--LVGLPG-----IGDRfPAELSGGMR 148
Cdd:cd03249 79 ---------IGLVSQEPVLFDG-TIAENIRYGKPDATD--EEVEEAAKKANIHdfIMSLPDgydtlVGER-GSQLSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 149 KRVSLARAIVINPEqhqqyknILLYDEPTAGLDpvasTRIESLIRHLLSQDHVCCCYLIVTHQFSTIDNtTDRIIFLYDG 228
Cdd:cd03249 146 QRIAIARALLRNPK-------ILLLDEATSALD----AESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNG 213
|
....*..
gi 499173792 229 KIQWDGS 235
Cdd:cd03249 214 QVVEQGT 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-230 |
4.85e-27 |
|
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: 109.12 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQ---SFGRKVI--LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVH------GHRRQR 74
Cdd:TIGR03269 277 EPIIKVRNVSKryiSVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 75 SIEEGEKALGVGLVFQQSALFDSLTVAEN----VGFTLyrdsdlrPREI---RAIVeeNLELVGLP-----GIGDRFPAE 142
Cdd:TIGR03269 357 PDGRGRAKRYIGILHQEYDLYPHRTVLDNlteaIGLEL-------PDELarmKAVI--TLKMVGFDeekaeEILDKYPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 143 LSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHllSQDHVCCCYLIVTHQFSTIDNTTDRI 222
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPR-------IVILDEPTGTMDPITKVDVTHSILK--AREEMEQTFIIVSHDMDFVLDVCDRA 498
|
....*...
gi 499173792 223 IFLYDGKI 230
Cdd:TIGR03269 499 ALMRDGKI 506
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-231 |
6.70e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.20 E-value: 6.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGR---KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrQRSIEEG--EKA 82
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENvwDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 LGVGLVFQQ-SALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINP 161
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 162 eqhqqykNILLYDEPTAGLDPvaSTRIEsLIRHLLS-QDHVCCCYLIVTHQFSTIdNTTDRIIFLYDGKIQ 231
Cdd:PRK13650 160 -------KIIILDEATSMLDP--EGRLE-LIKTIKGiRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVE 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-235 |
1.38e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.72 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQS------FGRKVILDdVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEV-----IVHGHRRQRSIE 77
Cdd:PRK13634 3 ITFQKVEHRyqyktpFERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 78 EGEKAlgVGLVFQ--QSALFDSlTVAENVGFTlyrdsdlrP-------REIRAIVEENLELVGLP-GIGDRFPAELSGGM 147
Cdd:PRK13634 82 PLRKK--VGIVFQfpEHQLFEE-TVEKDICFG--------PmnfgvseEDAKQKAREMIELVGLPeELLARSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 148 RKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYD 227
Cdd:PRK13634 151 MRRVAIAGVLAMEPE-------VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTT--VLVTHSMEDAARYADQIVVMHK 221
|
....*...
gi 499173792 228 GKIQWDGS 235
Cdd:PRK13634 222 GTVFLQGT 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-241 |
1.38e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.40 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 20 RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrRQRSIEEG-----EKAlgvGLVFQQSal 94
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENlwdirNKA---GMVFQNP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 95 fDSLTVA----ENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknI 170
Cdd:PRK13633 95 -DNQIVAtiveEDVAFGP-ENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE-------C 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 171 LLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNtTDRIIFLYDGKIQWDGSTADAYK 241
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITI--ILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-229 |
1.81e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.53 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsiEEGEKALGV 85
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG--LPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLV--FQQSALFDSLTVAENV----------GFT--LYRDSDLRPREIRAI--VEENLELVGLPGIGDRFPAELSGGMRK 149
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLlvaqhqqlktGLFsgLLKTPAFRRAESEALdrAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 150 RVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:PRK11300 161 RLEIARCMVTQPE-------ILMLDEPAAGLNPKETKELDELIAELRNEHNVTV--LLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-234 |
1.90e-26 |
|
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: 102.73 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 23 ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD---SGEVIVHGhrRQRSIEEGEKAlgVGLVFQQSALFDSLT 99
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG--QPRKPDQFQKC--VAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 100 VAENVGFTL-----YRDSDLRPREIRAIVeeNLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYD 174
Cdd:cd03234 98 VRETLTYTAilrlpRKSSDAIRKKRVEDV--LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPK-------VLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 175 EPTAGLDPVASTRIESLIRHLLSQDhvccCYLIVT-HQ-FSTIDNTTDRIIFLYDGKIQWDG 234
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRN----RIVILTiHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-230 |
2.04e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 102.65 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH--RRQRSIEEGEKALG 84
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdiTRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQQSALFDSLTVAENVGFTLYRdSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqh 164
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLII-AGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 165 qqyknILLYDEPTAGLDPVAStriESLIRHLLSQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:PRK10908 158 -----VLLADEPTGNLDDALS---EGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-225 |
2.19e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.48 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------RRQrsi 76
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyRQQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 eegekalgVGLVFQQSALFDSlTVAENVGFtlyrdsdlrPREIRAIVEE------NLELVGLP-GIGDRFPAELSGGMRK 149
Cdd:PRK10247 83 --------VSYCAQTPTLFGD-TVYDNLIF---------PWQIRNQQPDpaifldDLERFALPdTILTKNIAELSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 150 RVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIdNTTDRIIFL 225
Cdd:PRK10247 145 RISLIRNLQFMPK-------VLLLDEITSALDESNKHNVNEIIHRYVREQNIAV--LWVTHDKDEI-NHADKVITL 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-253 |
4.45e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.87 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKiYPGEAV-GVIGPSGTGKSTILRI-------VAGLLTpdSGEVIVHGHR--RQRSI 76
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMG-FPARAVtSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGGRSifNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEGEKAlgVGLVFQQSALFdSLTVAENVgFTLYRDSDLRPR-EIRAIVEENLELVGL-PGIGDRF---PAELSGGMRKRV 151
Cdd:PRK14271 97 LEFRRR--VGMLFQRPNPF-PMSIMDNV-LAGVRAHKLVPRkEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 152 SLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNTTDRIIFLYDGKIQ 231
Cdd:PRK14271 173 CLARTLAVNPE-------VLLLDEPTSALDPTTTEKIEEFIRSLADRLTV----IIVTHNLAQAARISDRAALFFDGRLV 241
|
250 260
....*....|....*....|...
gi 499173792 232 WDGSTADAYKS-EHPLLKQFFSG 253
Cdd:PRK14271 242 EEGPTEQLFSSpKHAETARYVAG 264
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-238 |
6.25e-26 |
|
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: 105.99 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH-RRQRSIEEgekaLG--VGLVFQQSALF 95
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdLSQWDREE----LGrhIGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 96 DSlTVAENVGftlyRDSDLRPREI-----RAIVEENleLVGLPG-----IGDRfPAELSGGMRKRVSLARAIVINPEqhq 165
Cdd:COG4618 419 DG-TIAENIA----RFGDADPEKVvaaakLAGVHEM--ILRLPDgydtrIGEG-GARLSGGQRQRIGLARALYGDPR--- 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 166 qyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIdNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:COG4618 488 ----LVVLDEPNSNLDDEGEAALAAAIRALKARGATV---VVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-244 |
1.37e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 100.74 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVIlDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRSieegekalGVGLVFQ 90
Cdd:PRK10895 15 GRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplHARARR--------GIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 91 QSALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPeqhqqyKNI 170
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP------KFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 171 LLyDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSEH 244
Cdd:PRK10895 160 LL-DEPFAGVDPISVIDIKRIIEHLRDSG---LGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-193 |
3.53e-25 |
|
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: 98.72 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG---HRRQRSIEEGEKALGv 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgplDFQRDSIARGLLYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 glvfQQSALFDSLTVAENVGFtlyrdsdLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhq 165
Cdd:cd03231 80 ----HAPGIKTTLSVLENLRF-------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRP--- 145
|
170 180
....*....|....*....|....*...
gi 499173792 166 qyknILLYDEPTAGLDPVASTRIESLIR 193
Cdd:cd03231 146 ----LWILDEPTTALDKAGVARFAEAMA 169
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-243 |
6.64e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEKAlgV 85
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPiTKENIREVRKF--V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLVFQQS--ALFdSLTVAENVGFTLYrDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEq 163
Cdd:PRK13652 81 GLVFQNPddQIF-SPTVEQDIAFGPI-NLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 164 hqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCCYliVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSE 243
Cdd:PRK13652 158 ------VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIF--STHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-226 |
1.78e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.19 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVaGLLTPDSGEVIVHGHRR--QRSIEEGEKALG 84
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEffNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 -----VGLVFQQSALFdSLTVAENVGFTLyRDSDLRPR-EIRAIVEENLELVGL-PGIGDRF---PAELSGGMRKRVSLA 154
Cdd:PRK14258 85 rlrrqVSMVHPKPNLF-PMSVYDNVAYGV-KIVGWRPKlEIDDIVESALKDADLwDEIKHKIhksALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 155 RAIVINPeqhqqykNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVccCYLIVTHQFSTIDNTTDRIIFLY 226
Cdd:PRK14258 163 RALAVKP-------KVLLMDEPCFGLDPIASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-252 |
2.18e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 101.66 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD---SGEVIVHGHRRQRSieegEKALGVGLVFQQSALF 95
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK----EMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 96 DSLTVAENVGFT--LYRDSDLRPREIRAIVEENLELVGLP-------GIGDRFPAeLSGGMRKRVSLARAIVINPEqhqq 166
Cdd:TIGR00955 112 PTLTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPP---- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCCyliVTHQ-FSTIDNTTDRIIFLYDGKIQWDGSTADAYKsehp 245
Cdd:TIGR00955 187 ---LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIIC---TIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVP---- 256
|
....*..
gi 499173792 246 llkqFFS 252
Cdd:TIGR00955 257 ----FFS 259
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-229 |
4.38e-24 |
|
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: 95.61 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKV-----ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqrsieegekal 83
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 GVGLVFQQSALFdSLTVAENVGFTLYRDSDLRPREIRAI-VEENLELvgLPG-----IGDRfPAELSGGMRKRVSLARAI 157
Cdd:cd03250 67 SIAYVSQEPWIQ-NGTIRENILFGKPFDEERYEKVIKACaLEPDLEI--LPDgdlteIGEK-GINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499173792 158 vinpeqhqqYKN--ILLYDEPTAGLDP-VASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNtTDRIIFLYDGK 229
Cdd:cd03250 143 ---------YSDadIYLLDDPLSAVDAhVGRHIFENCILGLLLNNKTR---ILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
9-252 |
9.66e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 9.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG-----RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHrrQRSIEEGEKAL 83
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY--HITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 G-----VGLVFQ--QSALFDSlTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLP-GIGDRFPAELSGGMRKRVSLAR 155
Cdd:PRK13641 81 KklrkkVSLVFQfpEAQLFEN-TVLKDVEFGP-KNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 156 AIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGS 235
Cdd:PRK13641 159 VMAYEPE-------ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTV---ILVTHNMDDVAEYADDVLVLEHGKLIKHAS 228
|
250
....*....|....*..
gi 499173792 236 TADAYKSEHPLLKQFFS 252
Cdd:PRK13641 229 PKEIFSDKEWLKKHYLD 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-240 |
1.33e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.46 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKAL-----GVGLVFQQ--SALFd 96
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG----KPIDYSRKGLmklreSVGMVFQDpdNQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 97 SLTVAENVGFTLYrDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEP 176
Cdd:PRK13636 97 SASVYQDVSFGAV-NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK-------VLVLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 177 TAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAY 240
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEM--QKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-184 |
3.30e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.27 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR--------RQRsiee 78
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdagdiatRRR---- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekalgVGLVFQQSALFDSLTVAENVgfTLY-RDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAI 157
Cdd:NF033858 341 ------VGYMSQAFSLYGELTVRQNL--ELHaRLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAV 412
|
170 180
....*....|....*....|....*..
gi 499173792 158 VINPEqhqqyknILLYDEPTAGLDPVA 184
Cdd:NF033858 413 IHKPE-------LLILDEPTSGVDPVA 432
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-230 |
4.05e-23 |
|
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: 93.69 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 5 VQPIIEFRGVSQSFGRK---VILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG-------HRRQR 74
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyeHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 75 SIeegekalgVGLVFQQSALFdSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLP-----GIGDRfPAELSGGMRK 149
Cdd:cd03248 88 SK--------VSLVGQEPVLF-ARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELAsgydtEVGEK-GSQLSGGQKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 150 RVSLARAIVINPEqhqqyknILLYDEPTAGLDpvasTRIESLIRHLLSQDHVCCCYLIVTHQFSTIDNtTDRIIFLYDGK 229
Cdd:cd03248 158 RVAIARALIRNPQ-------VLILDEATSALD----AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
.
gi 499173792 230 I 230
Cdd:cd03248 226 I 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-245 |
4.18e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.80 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKAL--GVGLVFQQSalFDSLTVA 101
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQNP--YGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 102 ENVGFTLYR----DSDLRPREIRAIVEENLELVGL-PGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEP 176
Cdd:PRK11308 109 KKVGQILEEplliNTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPD-------VVVADEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 177 TAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAY-KSEHP 245
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDL--QQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFnNPRHP 249
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-234 |
4.20e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPIIEFRGVSQSFGR---KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrQRSIE 77
Cdd:TIGR00958 471 APLNLEGLIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG---VPLVQ 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 78 EGEKAL--GVGLVFQQSALFdSLTVAENVGFTLYRDSDlrpREIRAIVEENLE---LVGLPGIGDRFPAE----LSGGMR 148
Cdd:TIGR00958 548 YDHHYLhrQVALVGQEPVLF-SGSVRENIAYGLTDTPD---EEIMAAAKAANAhdfIMEFPNGYDTEVGEkgsqLSGGQK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 149 KRVSLARAIVINPEqhqqyknILLYDEPTAGLDpvasTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNtTDRIIFLYDG 228
Cdd:TIGR00958 624 QRIAIARALVRKPR-------VLILDEATSALD----AECEQLLQESRSRASRTV--LLIAHRLSTVER-ADQILVLKKG 689
|
....*.
gi 499173792 229 KIQWDG 234
Cdd:TIGR00958 690 SVVEMG 695
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
7-247 |
4.66e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.82 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVS---QSfGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEKA 82
Cdd:PRK13648 6 SIIVFKNVSfqyQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAiTDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 lgVGLVFQQ-SALFDSLTVAENVGFTLyrDSDLRP-REIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVIN 160
Cdd:PRK13648 85 --IGIVFQNpDNQFVGSIVKYDVAFGL--ENHAVPyDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 161 PEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFS-TIDntTDRIIFLYDGKIQWDGSTADA 239
Cdd:PRK13648 161 PS-------VIILDEATSMLDPDARQNLLDLVRKVKSEHNITI--ISITHDLSeAME--ADHVIVMNKGTVYKEGTPTEI 229
|
....*...
gi 499173792 240 YKSEHPLL 247
Cdd:PRK13648 230 FDHAEELT 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-248 |
5.38e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 14 VSQSFGRKV-----ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIV------HGHRRQRSIEEGEKA 82
Cdd:PRK13645 12 VSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 LGVGLVFQQSALFDSlTVAENVGF-TLYRDSDlrPREIRAIVEENLELVGLP-GIGDRFPAELSGGMRKRVSLARAIVIN 160
Cdd:PRK13645 92 IGLVFQFPEYQLFQE-TIEKDIAFgPVNLGEN--KQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 161 peqhqqyKNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAY 240
Cdd:PRK13645 169 -------GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRI--IMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
....*...
gi 499173792 241 KSEHPLLK 248
Cdd:PRK13645 240 SNQELLTK 247
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-253 |
8.87e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILD---------DVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsI 76
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK-I 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEGE----KALGVGLVFQQSALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVS 152
Cdd:PRK10070 96 SDAElrevRRKKIAMVFQSFALMPHMTVLDNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 153 LARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCCYliVTHQFSTIDNTTDRIIFLYDGKIQW 232
Cdd:PRK10070 175 LARALAINPD-------ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVF--ISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
250 260
....*....|....*....|..
gi 499173792 233 DGSTADAYKS-EHPLLKQFFSG 253
Cdd:PRK10070 246 VGTPDEILNNpANDYVRTFFRG 267
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-225 |
1.01e-22 |
|
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: 92.88 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSF-----GRKVI--LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIV-HGHR------ 71
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGwvdlaq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 72 ---------RQRSIeegekalgvGLVFQ-------QSALfDslTVAENVgftlyRDSDLRPREIRAIVEENLELVGLPgi 135
Cdd:COG4778 82 aspreilalRRRTI---------GYVSQflrviprVSAL-D--VVAEPL-----LERGVDREEARARARELLARLNLP-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 136 gDR----FPAELSGGMRKRVSLARAIVINPeqhqqykNILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQ 211
Cdd:COG4778 143 -ERlwdlPPATFSGGEQQRVNIARGFIADP-------PLLLLDEPTASLDAANRAVVVELIEEAKARG---TAIIGIFHD 211
|
250
....*....|....
gi 499173792 212 FSTIDNTTDRIIFL 225
Cdd:COG4778 212 EEVREAVADRVVDV 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-230 |
1.08e-22 |
|
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: 96.81 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSqsFG---RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH--R--RQRSIeegEK 81
Cdd:COG5265 358 VRFENVS--FGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdiRdvTQASL---RA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 82 ALGVglVFQQSALFDSlTVAENVGFTlyrdsdlRPREIRAIVEENLEL-------VGLPG-----IGDRfPAELSGGMRK 149
Cdd:COG5265 433 AIGI--VPQDTVLFND-TIAYNIAYG-------RPDASEEEVEAAARAaqihdfiESLPDgydtrVGER-GLKLSGGEKQ 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 150 RVSLARAIVINPEqhqqyknILLYDEPTAGLDpvasTRIESLIRHLL---SQDHVCccyLIVTHQFSTIDNtTDRIIFLY 226
Cdd:COG5265 502 RVAIARTLLKNPP-------ILIFDEATSALD----SRTERAIQAALrevARGRTT---LVIAHRLSTIVD-ADEILVLE 566
|
....
gi 499173792 227 DGKI 230
Cdd:COG5265 567 AGRI 570
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-238 |
2.04e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.62 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 5 VQPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALG 84
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQQSALFDSLTVAEN--VGFTLYRDSDLRP----REIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIV 158
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENlyIGRHLTKKVCGVNiidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 159 INPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:PRK09700 162 LDAK-------VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT---AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-238 |
2.27e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 95.52 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFG----RKVILDDVDLKIYPGEAVGVIGPSGTGKS----TILRIVAGLLTPDSGEVIVHGH------- 70
Cdd:COG4172 4 MPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdllglse 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 RRQRSIEEGEkalgVGLVFQQ--SALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLP---GIGDRFPAELSG 145
Cdd:COG4172 84 RELRRIRGNR----IAMIFQEpmTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPdpeRRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 146 GMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDH---VcccyLIVTHQFSTIDNTTDRI 222
Cdd:COG4172 160 GQRQRVMIAMALANEPD-------LLIADEPTTALDVTVQAQILDLLKD-LQRELgmaL----LLITHDLGVVRRFADRV 227
|
250
....*....|....*.
gi 499173792 223 IFLYDGKIQWDGSTAD 238
Cdd:COG4172 228 AVMRQGEIVEQGPTAE 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-181 |
5.81e-22 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 94.62 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVhghrrqrsieeGEkALGVGL 87
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----------GE-TVKLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQ-SALFDSLTVAENV--GFTLYRdsdLRPREI--RAIV-------EENLELVGlpgigdrfpaELSGGMRKRVSLAR 155
Cdd:TIGR03719 390 VDQSrDALDPNKTVWEEIsgGLDIIK---LGKREIpsRAYVgrfnfkgSDQQKKVG----------QLSGGERNRVHLAK 456
|
170 180
....*....|....*....|....*.
gi 499173792 156 AIvinpeqhQQYKNILLYDEPTAGLD 181
Cdd:TIGR03719 457 TL-------KSGGNVLLLDEPTNDLD 475
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-198 |
6.85e-22 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 90.29 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQ---PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsie 77
Cdd:PRK13543 1 MIEPLHtapPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 78 eGEKALGVGLVFQQSALFDSLTVAENVGFTlyrdSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARaI 157
Cdd:PRK13543 78 -GDRSRFMAYLGHLPGLKADLSTLENLHFL----CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-L 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499173792 158 VINPEQhqqyknILLYDEPTAGLDPVASTRIESLIR-HLLSQ 198
Cdd:PRK13543 152 WLSPAP------LWLLDEPYANLDLEGITLVNRMISaHLRGG 187
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-230 |
8.34e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.26 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 5 VQPIIEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEKA 82
Cdd:PRK13657 331 VKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDiRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 LGVglVFQQSALFDSlTVAEN--VGFTLYRDSDLRPREIRAIVEENLE--LVGLPG-IGDRfPAELSGGMRKRVSLARAI 157
Cdd:PRK13657 411 IAV--VFQDAGLFNR-SIEDNirVGRPDATDEEMRAAAERAQAHDFIErkPDGYDTvVGER-GRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 158 VINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVCccyLIVTHQFSTIDNtTDRIIFLYDGKI 230
Cdd:PRK13657 487 LKDPP-------ILILDEATSALDVETEAKVKAALDE-LMKGRTT---FIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-230 |
1.14e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.51 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGL--LTPDSGEVIVHGHR-RQRSIEEGEKAlGVGLVFQQSA---- 93
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDiLELSPDERARA-GIFLAFQYPVeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 94 --LFDSLTVAENVGftlyRDSDLRPREIRAIVEENLELVGL-PGIGDRFPAE-LSGGMRKRVSLARAIVINPEqhqqykn 169
Cdd:COG0396 92 vsVSNFLRTALNAR----RGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPK------- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 170 ILLYDEPTAGLDpVASTRIES-LIRHLLSQDHvccCYLIVTHQFSTID-NTTDRIIFLYDGKI 230
Cdd:COG0396 161 LAILDETDSGLD-IDALRIVAeGVNKLRSPDR---GILIITHYQRILDyIKPDFVHVLVDGRI 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-239 |
1.36e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 93.79 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 15 SQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS--GEVIVHGHRRQRSIEEgekalGVGLVFQQS 92
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK-----RTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 93 ALFDSLTVAENVGF--------TLYRDSDLRPREiRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPeqh 164
Cdd:PLN03211 150 ILYPHLTVRETLVFcsllrlpkSLTKQEKILVAE-SVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINP--- 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 165 qqykNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccylIVT--HQFST-IDNTTDRIIFLYDGKIQWDGSTADA 239
Cdd:PLN03211 226 ----SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKT-----IVTsmHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDA 294
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1-238 |
1.76e-21 |
|
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: 93.23 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPIIEFRGVSQSF-GR--KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhRRQRSIE 77
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYpARpdQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDG-VDLRQLD 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 78 EGEKALGVGLVFQQSALFdSLTVAENVGFTlyrdsdlRPREIRAIVEENLE-------LVGLPGIGDRFPAE----LSGG 146
Cdd:TIGR02204 409 PAELRARMALVPQDPVLF-AASVMENIRYG-------RPDATDEEVEAAARaahahefISALPEGYDTYLGErgvtLSGG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 147 MRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIFLY 226
Cdd:TIGR02204 481 QRQRIAIARAILKDAP-------ILLLDEATSALDAESEQLVQQALETLMKGRTT----LIIAHRLATVLK-ADRIVVMD 548
|
250
....*....|..
gi 499173792 227 DGKIQWDGSTAD 238
Cdd:TIGR02204 549 QGRIVAQGTHAE 560
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-230 |
1.81e-21 |
|
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: 88.26 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSqsfgRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVG 86
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LV---FQQSALFDSLTVAENVGFTLYrdsdlrpreiraiveenlelvglpgigdrfpaeLSGGMRKRVSLARAIVINPEq 163
Cdd:cd03215 79 YVpedRKREGLVLDLSVAENIALSSL---------------------------------LSGGNQQKVVLARWLARDPR- 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 164 hqqyknILLYDEPTAGLDpVASTR-IESLIRHLLSQDH-VcccyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:cd03215 125 ------VLILDEPTRGVD-VGAKAeIYRLIRELADAGKaV----LLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-253 |
1.83e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.57 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrQRSIEEGEKAL--GVGLVFQQ--SALFdSLT 99
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG---REVNAENEKWVrsKVGLVFQDpdDQVF-SST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 100 VAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAG 179
Cdd:PRK13647 97 VWDDVAFGP-VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD-------VIVLDEPMAY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 180 LDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDG--------STADAYKSEHPLLKQFF 251
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGKTV---IVATHDVDLAAEWADQVIVLKEGRVLAEGdkslltdeDIVEQAGLRLPLVAQIF 245
|
..
gi 499173792 252 SG 253
Cdd:PRK13647 246 ED 247
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-235 |
1.99e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.43 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG-HRRQRSIEEGEKALgVGLVFQQ-SALFDSLTVA 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKL-VGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 102 ENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLD 181
Cdd:PRK13644 97 EDLAFGP-ENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE-------CLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499173792 182 PVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIdNTTDRIIFLYDGKIQWDGS 235
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTI---VYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-252 |
2.40e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 91.31 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 25 DDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH--RRQRSIEEGEKALGVGLVFQQ--SALFDSLTV 100
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdlLGMKDDEWRAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 101 AENVGFTL--YRdSDLRPREIRAIVEENLELVGL-PGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPT 177
Cdd:PRK15079 118 GEIIAEPLrtYH-PKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPK-------LIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 178 AGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKS-EHPLLKQFFS 252
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQL--QREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNpLHPYTKALMS 263
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-230 |
3.94e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.00 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSqsfgRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGeKALGV 85
Cdd:COG1129 255 VVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvRIRSPRDA-IRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLV---FQQSALFDSLTVAENVGFTLYRD-SD---LRPREIRAIVEENLELVGL--PGIgDRFPAELSGGMRKRVSLARA 156
Cdd:COG1129 330 AYVpedRKGEGLVLDLSIRENITLASLDRlSRgglLDRRRERALAEEYIKRLRIktPSP-EQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 157 IVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:COG1129 409 LATDPK-------VLILDEPTRGIDVGAKAEIYRLIRELAAEGKAV---IVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-182 |
8.99e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 91.34 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG-------HRRQrsieege 80
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarHRRA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 kalgvglVFQQSA---------LFDSLTVAENVGF--TLYrdsDLRPREIRAIVEENLELVGLPGIGDRfPA-ELSGGMR 148
Cdd:NF033858 74 -------VCPRIAympqglgknLYPTLSVFENLDFfgRLF---GQDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMK 142
|
170 180 190
....*....|....*....|....*....|....
gi 499173792 149 KRVSLARAIVINPEqhqqyknILLYDEPTAGLDP 182
Cdd:NF033858 143 QKLGLCCALIHDPD-------LLILDEPTTGVDP 169
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-230 |
9.48e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.81 E-value: 9.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGL--LTPDSGEVIVHGHR-RQRSIEEGEKaLGV 85
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDiTDLPPEERAR-LGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLVFQQSALFDSLTVAE-----NVGFtlyrdsdlrpreiraiveenlelvglpgigdrfpaelSGGMRKRVSLARAIVIN 160
Cdd:cd03217 80 FLAFQYPPEIPGVKNADflryvNEGF-------------------------------------SGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 161 PEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTID-NTTDRIIFLYDGKI 230
Cdd:cd03217 123 PD-------LAILDEPDSGLDIDALRLVAEVINKLREEG---KSVLIITHYQRLLDyIKPDRVHVLYDGRI 183
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-224 |
1.19e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGL--LTPD---SGEVIVHGHRRQRS-IEEGEK 81
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPdVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 82 ALGVGLVFQQSALFdSLTVAENVGFTL----YR-DSD-LRPREIRAI-----VEENLELVGLpgigdrfpaELSGGMRKR 150
Cdd:PRK14243 90 RRRIGMVFQKPNPF-PKSIYDNIAYGAringYKgDMDeLVERSLRQAalwdeVKDKLKQSGL---------SLSGGQQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 151 VSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNTTDRIIF 224
Cdd:PRK14243 160 LCIARAIAVQPE-------VILMDEPCSALDPISTLRIEELMHELKEQYTI----IIVTHNMQQAARVSDMTAF 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-229 |
1.73e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.97 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGV 85
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLVFQQSALFDSLTVAENV--GFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEq 163
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLylGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 164 hqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:PRK11288 161 ------VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVI---LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-252 |
2.34e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 15 SQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEE-GEKALGVGLVF--QQ 91
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD----KPISMlSSRQLARRLALlpQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 92 SALFDSLTVAENVGF------TLY-RDSDlrprEIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVinpeqh 164
Cdd:PRK11231 85 HLTPEGITVRELVAYgrspwlSLWgRLSA----EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 165 qQYKNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSEh 244
Cdd:PRK11231 155 -QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTV---VTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG- 229
|
....*...
gi 499173792 245 pLLKQFFS 252
Cdd:PRK11231 230 -LLRTVFD 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-234 |
2.82e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 89.61 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVivhghRRQRSIEegekalg 84
Cdd:TIGR03719 2 QYIYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-----RPQPGIK------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQQSALFDSLTVAENVG----------------FTLYRDSDlrpREIRAIVEENLELVGLPGIGD----------- 137
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEegvaeikdaldrfneiSAKYAEPD---ADFDKLAAEQAELQEIIDAADawdldsqleia 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 138 ----RFP------AELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDpvASTrIESLIRHLlsQDHVCCCyLI 207
Cdd:TIGR03719 147 mdalRCPpwdadvTKLSGGERRRVALCRLLLSKPD-------MLLLDEPTNHLD--AES-VAWLERHL--QEYPGTV-VA 213
|
250 260
....*....|....*....|....*...
gi 499173792 208 VTHQFSTIDNTTDRIIFLYDGK-IQWDG 234
Cdd:TIGR03719 214 VTHDRYFLDNVAGWILELDRGRgIPWEG 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-225 |
3.30e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.71 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVivhghrrqrsieEGEKALGVG 86
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFDSLTVaenvgfTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:PRK09544 71 YVPQKLYLDTTLPL------TVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ---- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvcCCYLIVTHQFSTIDNTTDRIIFL 225
Cdd:PRK09544 141 ---LLVLDEPTQGVDVNGQVALYDLIDQLRRELD--CAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-235 |
3.92e-20 |
|
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: 89.69 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 14 VSQSFGRKVIlDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALgvGLVFQQSA 93
Cdd:TIGR01257 937 IFEPSGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSL--GMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 94 LFDSLTVAENVGFTlyrdSDLRPR---EIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknI 170
Cdd:TIGR01257 1014 LFHHLTVAEHILFY----AQLKGRsweEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK-------V 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499173792 171 LLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGS 235
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI----IMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-260 |
4.02e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.77 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 5 VQPIIEFRGVSQSFGRKVIL---------DDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----- 70
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 ----RRQRsieegekalgVGLVFQQSAlfDSLTVAENVG----FTLYRDSDLRPREIRAIVEENLELVGL-PGIGDRFPA 141
Cdd:PRK15112 81 dysyRSQR----------IRMIFQDPS--TSLNPRQRISqildFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 142 ELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDR 221
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPK-------VIIADEALASLDMSMRSQLINLMLEL--QEKQGISYIYVTQHLGMMKHISDQ 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499173792 222 IIFLYDGKIQWDGSTADAYKSE-HPLLKQFFSGSIDGPIS 260
Cdd:PRK15112 220 VLVMHQGEVVERGSTADVLASPlHELTKRLIAGHFGEALT 259
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-181 |
5.00e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 89.02 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVhghrrqrsieeGEkALGVGL 87
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-----------GE-TVKLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQ-SALFDSLTVAENVgftlyrdSD------LRPREI--RAIV-------EENLELVGlpgigdrfpaELSGGMRKRV 151
Cdd:PRK11819 392 VDQSrDALDPNKTVWEEI-------SGgldiikVGNREIpsRAYVgrfnfkgGDQQKKVG----------VLSGGERNRL 454
|
170 180 190
....*....|....*....|....*....|
gi 499173792 152 SLARAIvinpeqhQQYKNILLYDEPTAGLD 181
Cdd:PRK11819 455 HLAKTL-------KQGGNVLLLDEPTNDLD 477
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-240 |
5.59e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 23 ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSiEEGEKAL--GVGLVFQ---QSALFDS 97
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS-KRGLLALrqQVATVFQdpeQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 ltVAENVGFTLyRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVInpeqHQQYkniLLYDEPT 177
Cdd:PRK13638 95 --IDSDIAFSL-RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL----QARY---LLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 178 AGLDPVASTRIESLIRHLLSQ-DHVcccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAY 240
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQgNHV----IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-230 |
1.11e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPIIEFRGVSQSF-----------GRKVILDDVDLKIYPGEAVGVIGPSGTGKST----ILRivaglLTPDSGEV 65
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLR-----LINSQGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 66 IVHGH------RRQ-----RSIEegekalgvgLVFQ--QSALFDSLTVAENV--GFTLYRdSDLRPREIRAIVEENLELV 130
Cdd:PRK15134 343 WFDGQplhnlnRRQllpvrHRIQ---------VVFQdpNSSLNPRLNVLQIIeeGLRVHQ-PTLSAAQREQQVIAVMEEV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 131 GL-PGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHlLSQDHVcCCYLIVT 209
Cdd:PRK15134 413 GLdPETRHRYPAEFSGGQRQRIAIARALILKPS-------LIILDEPTSSLDKTVQAQILALLKS-LQQKHQ-LAYLFIS 483
|
250 260
....*....|....*....|.
gi 499173792 210 HQFSTIDNTTDRIIFLYDGKI 230
Cdd:PRK15134 484 HDLHVVRALCHQVIVLRQGEV 504
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-250 |
1.41e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.77 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 3 EPVQPIIEFRGVSQSF-GR-KVILDDVDLKIYPGEAVGVIGPSGTGKSTIlrivAGLLTP----DSGEVIVHGH------ 70
Cdd:PRK11176 336 ERAKGDIEFRNVTFTYpGKeVPALRNINFKIPAGKTVALVGRSGSGKSTI----ANLLTRfydiDEGEILLDGHdlrdyt 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 ----RRQrsieegekalgVGLVFQQSALFDSlTVAENVGftlYRDSDLRPRE--IRAI-----------VEENLELVglp 133
Cdd:PRK11176 412 laslRNQ-----------VALVSQNVHLFND-TIANNIA---YARTEQYSREqiEEAArmayamdfinkMDNGLDTV--- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 134 gIGDRfPAELSGGMRKRVSLARAIVIN-PeqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQF 212
Cdd:PRK11176 474 -IGEN-GVLLSGGQRQRIAIARALLRDsP--------ILILDEATSALDTESERAIQAALDELQKNRTS----LVIAHRL 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499173792 213 STIDNtTDRIIFLYDGKIQWDGSTAD------AYKSEHPLlkQF 250
Cdd:PRK11176 540 STIEK-ADEILVVEDGEIVERGTHAEllaqngVYAQLHKM--QF 580
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-211 |
1.84e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEgekalgvglvFQQSALF--- 95
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----------YHQDLLYlgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 96 -----DSLTVAENVGFTLYRDSDLRPREIRAIveenLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknI 170
Cdd:PRK13538 82 qpgikTELTALENLRFYQRLHGPGDDEALWEA----LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAP-------L 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499173792 171 LLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQ 211
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAEQGG---MVILTTHQ 188
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-245 |
2.94e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 85.18 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLT-PD--SGEVIVHGHRRQRSIEEGEKALGVG----LVFQQSalFD 96
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGrvMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDP--MT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 97 SLTVAENVGFTL------YRDSDLRPREIRAIveENLELVGLPGIGDR---FPAELSGGMRKRVSLARAIVINPEqhqqy 167
Cdd:PRK11022 101 SLNPCYTVGFQImeaikvHQGGNKKTRRQRAI--DLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPK----- 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 168 knILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKS-EHP 245
Cdd:PRK11022 174 --LLIADEPTTALDVTIQAQIIELLLEL--QQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRApRHP 248
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-230 |
3.83e-19 |
|
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: 82.93 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH----------RRQRSI 76
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiglhdlRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 eegekalgvglVFQQSALFDSlTVAENVG-FTLYRDSDLrpreIRAIVEENL-ELVGLPGIGDRFPAE-----LSGGMRK 149
Cdd:cd03244 83 -----------IPQDPVLFSG-TIRSNLDpFGEYSDEEL----WQALERVGLkEFVESLPGGLDTVVEeggenLSVGQRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 150 RVSLARAIVINPeqhqqykNILLYDEPTAGLDPVASTRIESLIRHLLSQdhvcCCYLIVTHQFSTIDNtTDRIIFLYDGK 229
Cdd:cd03244 147 LLCLARALLRKS-------KILVLDEATASVDPETDALIQKTIREAFKD----CTVLTIAHRLDTIID-SDRILVLDKGR 214
|
.
gi 499173792 230 I 230
Cdd:cd03244 215 V 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-243 |
4.68e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 26 DVDLKIyPGEAVGVI-GPSGTGKSTILRIVAGLLTPDSGEVIVHGhRRQRSIEEG-----EKAlGVGLVFQQSALFDSLT 99
Cdd:PRK11144 16 TVNLTL-PAQGITAIfGRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLFDAEKGiclppEKR-RIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 100 VAENVgftLYRDSDLRPREIRAIVEenleLVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAG 179
Cdd:PRK11144 93 VRGNL---RYGMAKSMVAQFDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPE-------LLLMDEPLAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 180 LD-PvastRIESLIRHL--LSQDhVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSE 243
Cdd:PRK11144 159 LDlP----RKRELLPYLerLARE-INIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-229 |
5.77e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 85.65 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS--GEVIVHGHRRQ-RSIEEGEKAlG 84
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKaSNIRDTERA-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQQSALFDSLTVAENV----------GFTLYRDSDLRPREIraiveenLELVGLPGIGDRFP-AELSGGMRKRVSL 153
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIflgneitlpgGRMAYNAMYLRAKNL-------LRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 154 ARAIvinpeqHQQYKnILLYDEPTAGLDPVASTRIESLIRHlLSQDHVCCCYliVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:TIGR02633 153 AKAL------NKQAR-LLILDEPSSSLTEKETEILLDIIRD-LKAHGVACVY--ISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-230 |
5.85e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 3 EPVQPIIEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILrivaGLLT----PDSGEVIVHGHRRQrsi 76
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTrawdPQQGEILLNGQPIA--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEGEKAL--GVGLVFQQSALFdSLTVAENVGFTLYRDSDLRPREIraiveenLELVGLP-------------GIGDRfpa 141
Cdd:PRK11160 406 DYSEAALrqAISVVSQRVHLF-SATLRDNLLLAAPNASDEALIEV-------LQQVGLEklleddkglnawlGEGGR--- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 142 ELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDR 221
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAP-------LLLLDEPTEGLDAETERQILELLAEHAQNKTV----LMITHRLTGLEQ-FDR 542
|
....*....
gi 499173792 222 IIFLYDGKI 230
Cdd:PRK11160 543 ICVMDNGQI 551
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-248 |
6.83e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrQRSIEEGEKAL--GVGLVFQQ-SALFDSLTV 100
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLrrKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 101 AENVGFTLYRDSDLRPREIRAiVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGL 180
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE-------IIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 181 DPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIdNTTDRIIFLYDGKIQWDGSTADAYKSEHPLLK 248
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTV--LSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-260 |
9.43e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.11 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 5 VQPIIEFRG--VSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEgEKA 82
Cdd:PRK10253 2 TESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK-EVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 LGVGLVFQQSALFDSLTVAENVGFTLYRDSDLRPR---EIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVi 159
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 160 npeqhqQYKNILLYDEPTAGLDpvASTRIESLirHLLSQDHVCCCYLI--VTHQFSTIDNTTDRIIFLYDGKIQWDGSTA 237
Cdd:PRK10253 160 ------QETAIMLLDEPTTWLD--ISHQIDLL--ELLSELNREKGYTLaaVLHDLNQACRYASHLIALREGKIVAQGAPK 229
|
250 260
....*....|....*....|....*.
gi 499173792 238 DAYKSEhpLLKQFFSGS---IDGPIS 260
Cdd:PRK10253 230 EIVTAE--LIERIYGLRcmiIDDPVA 253
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
9.90e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.75 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRK-----VILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEV----IVHGHR------- 71
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 72 ---RQRSIEEGEKALG-VGLVFQ--QSALFDSlTVAENVGFTlyrDSDLRPREIRAIVEENLELVGLpGIG----DRFPA 141
Cdd:PRK13631 101 tnpYSKKIKNFKELRRrVSMVFQfpEYQLFKD-TIEKDIMFG---PVALGVKKSEAKKLAKFYLNKM-GLDdsylERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 142 ELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDR 221
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPE-------ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTV---FVITHTMEHVLEVADE 245
|
250 260
....*....|....*....|...
gi 499173792 222 IIFLYDGKIQWDGSTADAYKSEH 244
Cdd:PRK13631 246 VIVMDKGKILKTGTPYEIFTDQH 268
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-244 |
1.32e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.57 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD--------SGEVIVHGhRRQRSIEEGEKALGVGLVFQQS 92
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNG-EPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 93 ALFDSLTVAENVGFTLY---RDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAI--VINPEQHQQY 167
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYphaRRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqLWPPHDAAQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 168 KNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSEH 244
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGV--LAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAH 247
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-228 |
1.61e-18 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 84.78 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTP---DSGEVIVHGHRRQRSIEEgekalGVGLVFQQSALF 95
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQR-----SIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 96 DSLTVAENVGFTLY--RDSDLRPREIRAIVEENLEL----------VGLPGIGdrfpaeLSGGMRKRVSLARAIVINPeq 163
Cdd:TIGR00956 849 PTSTVRESLRFSAYlrQPKSVSKSEKMEYVEEVIKLlemesyadavVGVPGEG------LNVEQRKRLTIGVELVAKP-- 920
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 164 hqqyKNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCCYLivtHQFS-TIDNTTDRIIFLYDG 228
Cdd:TIGR00956 921 ----KLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTI---HQPSaILFEEFDRLLLLQKG 979
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-235 |
7.29e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 7.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGL--LTPDSGEVIVHGHR--------RQRSIEE 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALcekcgyveRPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 GEKALG------------------------VGLVFQQS-ALFDSLTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLP 133
Cdd:TIGR03269 81 PCPVCGgtlepeevdfwnlsdklrrrirkrIAIMLQRTfALYGDDTVLDNVLEAL-EEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 134 GIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVccCYLIVTHQFS 213
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPF-------LFLADEPTGTLDPQTAKLVHNALEEAVKASGI--SMVLTSHWPE 230
|
250 260
....*....|....*....|..
gi 499173792 214 TIDNTTDRIIFLYDGKIQWDGS 235
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGT 252
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-225 |
1.30e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.78 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVS-QSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHghrrqrsieEGEKALgvgl 87
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP---------AGARVL---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 vF--QQSALfdsltvaeNVGfTLyRDSDLRPREIRAI----VEENLELVGLPGIGDRFPAE------LSGGMRKRVSLAR 155
Cdd:COG4178 430 -FlpQRPYL--------PLG-TL-REALLYPATAEAFsdaeLREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 156 AIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQdhvcCCYLIVTHQfSTIDNTTDRIIFL 225
Cdd:COG4178 499 LLLHKPD-------WLFLDEATSALDEENEAALYQLLREELPG----TTVISVGHR-STLAAFHDRVLEL 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-230 |
1.38e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 3 EPVQPIIEFRGVS-QSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH------RRQRs 75
Cdd:COG3845 252 EPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsPRER- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 76 IEEG-----EKALGVGLVfqqsalfDSLTVAENVGFTLYRDSD------LRPREIRAIVEENLEL--VGLPGIGDRFpAE 142
Cdd:COG3845 331 RRLGvayipEDRLGRGLV-------PDMSVAENLILGRYRRPPfsrggfLDRKAIRAFAEELIEEfdVRTPGPDTPA-RS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 143 LSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDpVAStrIESLIRHLLSQDHVCCCYLIVTHQFSTIDNTTDRI 222
Cdd:COG3845 403 LSGGNQQKVILARELSRDPK-------LLIAAQPTRGLD-VGA--IEFIHQRLLELRDAGAAVLLISEDLDEILALSDRI 472
|
....*...
gi 499173792 223 IFLYDGKI 230
Cdd:COG3845 473 AVMYEGRI 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-229 |
2.26e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPvqpIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLtPD---SGEVIVHGHRRQ-RSI 76
Cdd:PRK13549 1 MMEY---LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQaSNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEGEKAlGVGLVFQQSALFDSLTVAENV---------GFTLYRDSDLRPREIraiveenLELVGLpgigDRFPA----EL 143
Cdd:PRK13549 77 RDTERA-GIAIIHQELALVKELSVLENIflgneitpgGIMDYDAMYLRAQKL-------LAQLKL----DINPAtpvgNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 144 SGGMRKRVSLARAIvinpeqHQQYKnILLYDEPTAGLdpvastrIESLIRHLLS-----QDH-VCCCYliVTHQFSTIDN 217
Cdd:PRK13549 145 GLGQQQLVEIAKAL------NKQAR-LLILDEPTASL-------TESETAVLLDiirdlKAHgIACIY--ISHKLNEVKA 208
|
250
....*....|..
gi 499173792 218 TTDRIIFLYDGK 229
Cdd:PRK13549 209 ISDTICVIRDGR 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-234 |
7.35e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.39 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 12 RGVSQSFG-RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIvhghrrqrsIEEGEKalgVGLVFQ 90
Cdd:PRK11819 10 NRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR---------PAPGIK---VGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 91 QSALFDSLTVAENV--GFtlyrdsdlrpREIRAIVEE-----------------------------------NLEL---- 129
Cdd:PRK11819 78 EPQLDPEKTVRENVeeGV----------AEVKAALDRfneiyaayaepdadfdalaaeqgelqeiidaadawDLDSqlei 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 130 ----VGLPGiGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDpvASTrIESLIRHLlsQDhvcccY 205
Cdd:PRK11819 148 amdaLRCPP-WDAKVTKLSGGERRRVALCRLLLEKPD-------MLLLDEPTNHLD--AES-VAWLEQFL--HD-----Y 209
|
250 260 270
....*....|....*....|....*....|....
gi 499173792 206 ----LIVTHQFSTIDNTTDRIIFLYDGK-IQWDG 234
Cdd:PRK11819 210 pgtvVAVTHDRYFLDNVAGWILELDRGRgIPWEG 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-229 |
2.06e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSF-GRKViLDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALG 84
Cdd:PRK10762 2 QALLQLKGIDKAFpGVKA-LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQQSALFDSLTVAENV----GFT----------LYRDSDLRpreiraiveenLELVGLPGIGDRFPAELSGGMRKR 150
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgrEFVnrfgridwkkMYAEADKL-----------LARLNLRFSSDKLVGELSIGEQQM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 151 VSLARAIVINpeqhqqyKNILLYDEPTaglDPVASTRIESL---IRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYD 227
Cdd:PRK10762 150 VEIAKVLSFE-------SKVIIMDEPT---DALTDTETESLfrvIRELKSQG---RGIVYISHRLKEIFEICDDVTVFRD 216
|
..
gi 499173792 228 GK 229
Cdd:PRK10762 217 GQ 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-188 |
2.80e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.38 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 2 SEPVQPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLL--TPDSGEVIVhghrrqrsieeg 79
Cdd:COG2401 24 SERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 80 ekalgvglvfQQSALFDSLTVAENVgftlYRDSDlrpreiraiVEENLELVGLPGIGD-----RFPAELSGGMRKRVSLA 154
Cdd:COG2401 92 ----------PDNQFGREASLIDAI----GRKGD---------FKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLA 148
|
170 180 190
....*....|....*....|....*....|....
gi 499173792 155 RAIVINPeqhqqykNILLYDEPTAGLDPVASTRI 188
Cdd:COG2401 149 LLLAERP-------KLLVIDEFCSHLDRQTAKRV 175
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-249 |
3.41e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 3 EPVQPIIEFRGVSQSF---GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS-GEVIVHGHrrqrsiee 78
Cdd:PLN03130 609 EPGLPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekalgVGLVFQQSALFDSlTVAENVGFTLYRDSDLRPREIR-AIVEENLELvgLPG-----IGDRfPAELSGGMRKRVS 152
Cdd:PLN03130 681 ------VAYVPQVSWIFNA-TVRDNILFGSPFDPERYERAIDvTALQHDLDL--LPGgdlteIGER-GVNISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 153 LARAIVINpeqhqqyKNILLYDEPTAGLDP-VASTRIESLIRHLLSQDhvccCYLIVTHQFSTIDNtTDRIIFLYDGKIQ 231
Cdd:PLN03130 751 MARAVYSN-------SDVYIFDDPLSALDAhVGRQVFDKCIKDELRGK----TRVLVTNQLHFLSQ-VDRIILVHEGMIK 818
|
250
....*....|....*...
gi 499173792 232 WDGsTADAYKSEHPLLKQ 249
Cdd:PLN03130 819 EEG-TYEELSNNGPLFQK 835
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-248 |
3.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.97 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGR-----KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSG-----EVIVHGHRRQRSIEE 78
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvdDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 GEKAlgVGLVFQ--QSALFDSlTVAENVGFTLyRDSDLRPREIRAIVEENLELVGLP-GIGDRFPAELSGGMRKRVSLAR 155
Cdd:PRK13646 83 VRKR--IGMVFQfpESQLFED-TVEREIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 156 AIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGS 235
Cdd:PRK13646 159 ILAMNPD-------IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTI--ILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
250
....*....|...
gi 499173792 236 TADAYKSEHPLLK 248
Cdd:PRK13646 230 PKELFKDKKKLAD 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-230 |
4.23e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQPIIEFRGVSQSF----------GRKV-ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRR 72
Cdd:PRK10261 309 DGEPILQVRNLVTRFplrsgllnrvTREVhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 73 QRSIEEGEKAL--GVGLVFQQSalFDSLTVAENVGFT----LYRDSDLRPREIRAIVEENLELVGL-PGIGDRFPAELSG 145
Cdd:PRK10261 389 DTLSPGKLQALrrDIQFIFQDP--YASLDPRQTVGDSimepLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 146 GMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFL 225
Cdd:PRK10261 467 GQRQRICIARALALNPK-------VIIADEAVSALDVSIRGQIINLLLDL--QRDFGIAYLFISHDMAVVERISHRVAVM 537
|
....*
gi 499173792 226 YDGKI 230
Cdd:PRK10261 538 YLGQI 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-248 |
8.97e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 26 DVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG---HRRQRS-IEEGE---------KALGVGLVFQQ- 91
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllRRRSRQvIELSEqsaaqmrhvRGADMAMIFQEp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 92 -SALFDSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGLP---GIGDRFPAELSGGMRKRVSLARAIVINPEqhqqy 167
Cdd:PRK10261 114 mTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPeaqTILSRYPHQLSGGMRQRVMIAMALSCRPA----- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 168 knILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKS-EHPL 246
Cdd:PRK10261 189 --VLIADEPTTALDVTIQAQILQLIKVL--QKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHApQHPY 264
|
..
gi 499173792 247 LK 248
Cdd:PRK10261 265 TR 266
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-251 |
1.50e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.92 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 23 ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVA----GLLTPDSGEVIVHGHrrqrSIEEGEKALGVGLVF--QQSALFD 96
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGI----TPEEIKKHYRGDVVYnaETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 97 SLTVAENVGFT-LYRDSDLRP----REIRA--IVEENLELVGL-----PGIGDRFPAELSGGMRKRVSLARAIVINPeqh 164
Cdd:TIGR00956 152 HLTVGETLDFAaRCKTPQNRPdgvsREEYAkhIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGA--- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 165 qqykNILLYDEPTAGLDpvASTRIEsLIRHLLSQDHVC-CCYLIVTHQFS-TIDNTTDRIIFLYDGKIQWDGSTADAyks 242
Cdd:TIGR00956 229 ----KIQCWDNATRGLD--SATALE-FIRALKTSANILdTTPLVAIYQCSqDAYELFDKVIVLYEGYQIYFGPADKA--- 298
|
....*....
gi 499173792 243 ehpllKQFF 251
Cdd:TIGR00956 299 -----KQYF 302
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-230 |
1.93e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 26 DVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEgekALGVGLVF-----QQSALFDSLT 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEiNALSTAQ---RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 100 VAENVGFTLYRDSD--LRPREIRAIVEENLELVGLPGIGDRFPAE-LSGGMRKRVSLARAIVINPEqhqqyknILLYDEP 176
Cdd:PRK15439 358 LAWNVCALTHNRRGfwIKPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQ-------LLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499173792 177 TAGLDPVASTRIESLIRHlLSQDHVCCcyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRS-IAAQNVAV--LFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-240 |
4.39e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVhghrrqrsieegEKALGVGL 87
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY------------EQDLIVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQ------QSALFDslTVAENVG----------------FTLYRDSDL-RPREIRAIVE------------ENLELVGL 132
Cdd:PRK11147 71 LQQdpprnvEGTVYD--FVAEGIEeqaeylkryhdishlvETDPSEKNLnELAKLQEQLDhhnlwqlenrinEVLAQLGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 133 PGigDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDpvaSTRIESLIRHLLSQDHvccCYLIVTHQF 212
Cdd:PRK11147 149 DP--DAALSSLSGGWLRKAALGRALVSNPD-------VLLLDEPTNHLD---IETIEWLEGFLKTFQG---SIIFISHDR 213
|
250 260
....*....|....*....|....*....
gi 499173792 213 STIDNTTDRIIFLYDGKI-QWDGSTaDAY 240
Cdd:PRK11147 214 SFIRNMATRIVDLDRGKLvSYPGNY-DQY 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-242 |
5.53e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.63 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 3 EPVQPIIEFRGVSQSFGRKV---ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTP-DSGEVIVHGhrrqrsiee 78
Cdd:PLN03232 609 QPGAPAISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG--------- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekalGVGLVFQQSALFDSlTVAENVGFtlyrDSDLRP-REIRAI----VEENLELvgLPG-----IGDRfPAELSGGMR 148
Cdd:PLN03232 680 -----SVAYVPQVSWIFNA-TVRENILF----GSDFESeRYWRAIdvtaLQHDLDL--LPGrdlteIGER-GVNISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 149 KRVSLARAIVINpeqhqqyKNILLYDEPTAGLDP-VASTRIESLIRHLLSQDhvccCYLIVTHQFSTIDnTTDRIIFLYD 227
Cdd:PLN03232 747 QRVSMARAVYSN-------SDIYIFDDPLSALDAhVAHQVFDSCMKDELKGK----TRVLVTNQLHFLP-LMDRIILVSE 814
|
250
....*....|....*
gi 499173792 228 GKIQWDGSTADAYKS 242
Cdd:PLN03232 815 GMIKEEGTFAELSKS 829
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-198 |
5.69e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 31 IYPGEAVGVIGPSGTGKSTILRIVAGLLtPDSGEVIVHGhrrqRSIEE---GEKALGVG-LVFQQSALFdSLTVaenvgF 106
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAG----QPLEAwsaAELARHRAyLSQQQTPPF-AMPV-----F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 107 ---TLYRDSDLRPREIRAIVEENLELVGLpgiGDRFP---AELSGGMRKRVSLARAI-----VINPeqhqqYKNILLYDE 175
Cdd:PRK03695 88 qylTLHQPDKTRTEAVASALNEVAEALGL---DDKLGrsvNQLSGGEWQRVRLAAVVlqvwpDINP-----AGQLLLLDE 159
|
170 180
....*....|....*....|...
gi 499173792 176 PTAGLDPVASTRIESLIRHLLSQ 198
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQ 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-243 |
7.85e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 7.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPIIEFRGVSQSF---GRkVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIE 77
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFrvpGR-TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA----QPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 78 E-GEKALG--VGLVFQQSALFDSLTVAENVGFTLYRDSDLRPR---EIRAIVEENLELVGLPGIGDRFPAELSGGMRKRV 151
Cdd:PRK10575 77 SwSSKAFArkVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 152 SLARAIVinpeqhqQYKNILLYDEPTAGLDPVASTRIESLIrHLLSQDHvCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQ 231
Cdd:PRK10575 157 WIAMLVA-------QDSRCLLLDEPTSALDIAHQVDVLALV-HRLSQER-GLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
250
....*....|..
gi 499173792 232 WDGSTADAYKSE 243
Cdd:PRK10575 228 AQGTPAELMRGE 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-230 |
8.57e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.34 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLtPDSGEVIVHGHR-RQRSIEEGEKALG-VGlvfQQSALFDSl 98
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIElRELDPESWRKHLSwVG---QNPQLPHG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 99 TVAENVgftLYRDSDLRPREIRAIVEEN--LELV-GLPG-----IGDRfPAELSGGMRKRVSLARAIvINPEQhqqyknI 170
Cdd:PRK11174 438 TLRDNV---LLGNPDASDEQLQQALENAwvSEFLpLLPQgldtpIGDQ-AAGLSVGQAQRLALARAL-LQPCQ------L 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 171 LLYDEPTAGLDPVASTRIESLIRHlLSQDHVCccyLIVTHQFSTIDNtTDRIIFLYDGKI 230
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNA-ASRRQTT---LMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-228 |
1.40e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 69.96 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD--SGEVIVHGHRRQRSIEEgekalGVGLVFQQSALFD 96
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQR-----STGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 97 SLTVAENVGFTLYrdsdLRpreiraiveenlelvglpgigdrfpaELSGGMRKRVSLARAIVINPEqhqqyknILLYDEP 176
Cdd:cd03232 93 NLTVREALRFSAL----LR--------------------------GLSVEQRKRLTIGVELAAKPS-------ILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499173792 177 TAGLDPVASTRIESLIRHLLSQDHVCCCYLivtHQFS-TIDNTTDRIIFLYDG 228
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKLADSGQAILCTI---HQPSaSIFEKFDRLLLLKRG 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-259 |
1.65e-14 |
|
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: 73.12 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVGLVFqqSALFDSLTVAEN 103
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQF--DAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 104 vgftLYRDSDLR---PREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGL 180
Cdd:TIGR01257 2033 ----LYLYARLRgvpAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP-------LVLLDEPTTGM 2101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 181 DPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGST-------ADAY----KSEHP---L 246
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAV---VLTSHSMEECEALCTRLAIMVKGAFQCLGTIqhlkskfGDGYivtmKIKSPkddL 2178
|
250
....*....|....*....
gi 499173792 247 L------KQFFSGSIDGPI 259
Cdd:TIGR01257 2179 LpdlnpvEQFFQGNFPGSV 2197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-238 |
1.94e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 72.51 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVivhghrrqrSIEEGEKaLGvg 86
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---------GLAKGIK-LG-- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 lVFQQSALfDSLTVAENvgfTLYRDSDLRPREIRAIVEENLELVGLPG-----IGDRFpaelSGGMRKRVSLArAIVinp 161
Cdd:PRK10636 379 -YFAQHQL-EFLRADES---PLQHLARLAPQELEQKLRDYLGGFGFQGdkvteETRRF----SGGEKARLVLA-LIV--- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 162 eqhQQYKNILLYDEPTAGLDpvASTRiESLIRHLLSQDHVcccYLIVTHQFSTIDNTTDRIIFLYDGKIQ-WDGSTAD 238
Cdd:PRK10636 446 ---WQRPNLLLLDEPTNHLD--LDMR-QALTEALIDFEGA---LVVVSHDRHLLRSTTDDLYLVHDGKVEpFDGDLED 514
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-210 |
2.07e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.83 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGllTPD----SGEVIVHGhrrqRSI---EE 78
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKG----ESIldlEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 GEKA-LGVGLVFQQSALF------DSLTVAENVGFTLYRDSDLRPREIRAIVEENLELVGL-PGIGDRFPAE-LSGGMRK 149
Cdd:CHL00131 79 EERAhLGIFLAFQYPIEIpgvsnaDFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMdPSFLSRNVNEgFSGGEKK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 150 RVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTH 210
Cdd:CHL00131 159 RNEILQMALLDSE-------LAILDETDSGLDIDALKIIAEGINKLMTSEN---SIILITH 209
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-230 |
2.40e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQPIIEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQR-SIEEGE 80
Cdd:PLN03232 1230 PSRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 81 KALGvglVFQQSALFDSLTVAENVG-FTLYRDSDLRpreiraiveENLELVGLPGIGDRFPAEL-----------SGGMR 148
Cdd:PLN03232 1310 RVLS---IIPQSPVLFSGTVRFNIDpFSEHNDADLW---------EALERAHIKDVIDRNPFGLdaevseggenfSVGQR 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 149 KRVSLARAIVinpeqhqQYKNILLYDEPTAGLDpvasTRIESLIRHLLSQDHVCCCYLIVTHQFSTIDNtTDRIIFLYDG 228
Cdd:PLN03232 1378 QLLSLARALL-------RRSKILVLDEATASVD----VRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSG 1445
|
..
gi 499173792 229 KI 230
Cdd:PLN03232 1446 QV 1447
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-229 |
5.06e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.36 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 31 IYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR---RQRSIEEGEKalgvGLVfqqSALFDSLTvaENVGFT 107
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvsyKPQYIKADYE----GTV---RDLLSSIT--KDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 108 LYRDSDL-RPREIRAIVEENLElvglpgigdrfpaELSGGMRKRVSLARAIvinpeqhQQYKNILLYDEPTAGLDPVAST 186
Cdd:cd03237 93 PYFKTEIaKPLQIEQILDREVP-------------ELSGGELQRVAIAACL-------SKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499173792 187 RIESLIRHLLsqDHVCCCYLIVTHQFSTIDNTTDRIIfLYDGK 229
Cdd:cd03237 153 MASKVIRRFA--ENNEKTAFVVEHDIIMIDYLADRLI-VFEGE 192
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-230 |
5.54e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.53 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTiLRIVAGLLTPDSGE-----VIVHGHRR--- 72
Cdd:NF000106 6 ISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRrpwrf*TWCANRRalr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 73 -----QRSIEEGEKalgvglvfqqsalfDSLTVAENVgFTLYRDSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGM 147
Cdd:NF000106 85 rtig*HRPVR*GRR--------------ESFSGRENL-YMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 148 RKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCC---YLIVTHQFSTIDNTTDRIIF 224
Cdd:NF000106 150 RRRLDLAASMIGRPA-------VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLttqYMEEAEQLAHELTVIDRGRV 222
|
....*.
gi 499173792 225 LYDGKI 230
Cdd:NF000106 223 IADGKV 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-230 |
5.94e-14 |
|
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: 68.44 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 12 RGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD---SGEVIVHGHRRQrsiEEGEKALG-VGL 87
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYK---EFAEKYPGeIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVGFTLyrdsDLRpreiraiveenlelvglpgiGDRFPAELSGGMRKRVSLARAIVINPeqhqqy 167
Cdd:cd03233 88 VSEEDVHFPTLTVRETLDFAL----RCK--------------------GNEFVRGISGGERKRVSIAEALVSRA------ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 168 kNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFS-TIDNTTDRIIFLYDGKI 230
Cdd:cd03233 138 -SVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTT--FVSLYQASdEIYDLFDKVLVLYEGRQ 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-253 |
6.95e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALgvglvFQQSALFD---SLTV 100
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAY-----VPQSEEVDwsfPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 101 AENVGFTLYRDSDL--RPR-EIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVinpeqhQQYKNILLyDEPT 177
Cdd:PRK15056 98 EDVVMMGRYGHMGWlrRAKkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA------QQGQVILL-DEPF 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 178 AGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLyDGKIQWDGSTADAYKSEHplLKQFFSG 253
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEG---KTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAEN--LELAFSG 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-238 |
7.58e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVhghrrQRSIeegekalgvGLVFQQSALFDSlTV 100
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----ERSI---------AYVPQQAWIMNA-TV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 101 AENVgftLYRDSDLRPREIRAIVEENLE--LVGLPG-----IGDRfPAELSGGMRKRVSLARAIVINpeqhqqyKNILLY 173
Cdd:PTZ00243 738 RGNI---LFFDEEDAARLADAVRVSQLEadLAQLGGgleteIGEK-GVNLSGGQKARVSLARAVYAN-------RDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 174 DEPTAGLDPVASTRI--ESLIRHLLSQDHVcccylIVTHQFSTIDNtTDRIIFLYDGKIQWDGSTAD 238
Cdd:PTZ00243 807 DDPLSALDAHVGERVveECFLGALAGKTRV-----LATHQVHVVPR-ADYVVALGDGRVEFSGSSAD 867
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-229 |
1.31e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 1 MSEPVQPI----IEFRgvSQSFGRKVIlDDVDLKIYPGEAVGVIGPSGTGKS-TILRIVAGLLTPD----SGEVIVHGH- 70
Cdd:PRK15134 1 MTQPLLAIenlsVAFR--QQQTVRTVV-NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGEs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 ------RRQRSIEeGEKalgVGLVFQQSALfdSLTVAENVGFTLYRDSDL----RPREIRAIVEENLELVGLPGIGDR-- 138
Cdd:PRK15134 78 llhaseQTLRGVR-GNK---IAMIFQEPMV--SLNPLHTLEKQLYEVLSLhrgmRREAARGEILNCLDRVGIRQAAKRlt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 139 -FPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDN 217
Cdd:PRK15134 152 dYPHQLSGGERQRVMIAMALLTRPE-------LLIADEPTTALDVSVQAQILQLLREL--QQELNMGLLFITHNLSIVRK 222
|
250
....*....|..
gi 499173792 218 TTDRIIFLYDGK 229
Cdd:PRK15134 223 LADRVAVMQNGR 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-211 |
2.76e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.55 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDsGEVIVHG-HRRQRSIEEGEKALGVglVFQQSALFdS 97
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvSWNSVTLQTWRKAFGV--IPQKVFIF-S 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTVAENVG-FTLYRDsdlrpREIRAIVEEnlelVGLPGIGDRFPAE-----------LSGGMRKRVSLARAIVINPEqhq 165
Cdd:TIGR01271 1306 GTFRKNLDpYEQWSD-----EEIWKVAEE----VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAK--- 1373
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499173792 166 qyknILLYDEPTAGLDPVAStrieSLIRHLLSQDHVCCCYLIVTHQ 211
Cdd:TIGR01271 1374 ----ILLLDEPSAHLDPVTL----QIIRKTLKQSFSNCTVILSEHR 1411
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-230 |
5.11e-13 |
|
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: 65.90 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKV--ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG--------HRRQRSIee 78
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistiplEDLRSSL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 gekalgvGLVFQQSALFDSlTVAENVG-FTLYRDSDLrpREIRAIVEENLelvglpgigdrfpaELSGGMRKRVSLARAI 157
Cdd:cd03369 85 -------TIIPQDPTLFSG-TIRSNLDpFDEYSDEEI--YGALRVSEGGL--------------NLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 158 VINPeqhqqykNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNtTDRIIFLYDGKI 230
Cdd:cd03369 141 LKRP-------RVLVLDEATASIDYATDALIQKTIREEFTNSTI----LTIAHRLRTIID-YDKILVMDAGEV 201
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-238 |
6.85e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.05 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsIEEGEKALGVG 86
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK-IGLHDLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFdSLTVAENVG-FTLYRDSDlrpreiraiVEENLELVGLPGIGDRFPAE-----------LSGGMRKRVSLA 154
Cdd:TIGR00957 1364 IIPQDPVLF-SGSLRMNLDpFSQYSDEE---------VWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLA 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 155 RAIVinpeqhqQYKNILLYDEPTAGLDPVASTRIESLIRHLLSQdhvcCCYLIVTHQFSTIDNTTdRIIFLYDGKIQWDG 234
Cdd:TIGR00957 1434 RALL-------RKTKILVLDEATAAVDLETDNLIQSTIRTQFED----CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
....
gi 499173792 235 STAD 238
Cdd:TIGR00957 1502 APSN 1505
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-231 |
7.33e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKV--ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEKALGV 85
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiSKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 glVFQQSALFdSLTVAENVG-FTLYRDSDLRpreiraiveENLELVGLPGIGDRFP----AEL-------SGGMRKRVSL 153
Cdd:PLN03130 1318 --IPQAPVLF-SGTVRFNLDpFNEHNDADLW---------ESLERAHLKDVIRRNSlgldAEVseagenfSVGQRQLLSL 1385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 154 ARAIVinpeqhqQYKNILLYDEPTAGLDpvasTRIESLIRHLLSQDHVCCCYLIVTHQFSTIDNtTDRIIFLYDGKIQ 231
Cdd:PLN03130 1386 ARALL-------RRSKILVLDEATAAVD----VRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-254 |
8.90e-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: 66.42 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDsGEVIVHGHRRQR-SIEEGEKALGVglVFQQSALFdS 97
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSvPLQKWRKAFGV--IPQKVFIF-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTVAENVG-FTLYRDsdlrpREIRAIVEEnlelVGLPGIGDRFPAE-----------LSGGMRKRVSLARAIVINPEqhq 165
Cdd:cd03289 91 GTFRKNLDpYGKWSD-----EEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAK--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 166 qyknILLYDEPTAGLDPVAStrieSLIRHLLSQDHVCCCYLIVTHQFSTIDNtTDRIIFLYDGKIqWDGSTADAYKSEHP 245
Cdd:cd03289 159 ----ILLLDEPSAHLDPITY----QVIRKTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKV-RQYDSIQKLLNEKS 228
|
....*....
gi 499173792 246 LLKQFFSGS 254
Cdd:cd03289 229 HFKQAISPS 237
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-235 |
9.05e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.05 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqrsieegekalGVGLVFQQsALFDSLTVAEN 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQ-AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 104 VGFtlyrDSDLRPREIRAIVEE-----NLELvgLPGiGDRFP-----AELSGGMRKRVSLARAIVINpeqhqqyKNILLY 173
Cdd:TIGR00957 719 ILF----GKALNEKYYQQVLEAcallpDLEI--LPS-GDRTEigekgVNLSGGQKQRVSLARAVYSN-------ADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499173792 174 DEPTAGLDP-VASTRIESLI--RHLLSQDhvccCYLIVTHQFSTIDNtTDRIIFLYDGKIQWDGS 235
Cdd:TIGR00957 785 DDPLSAVDAhVGKHIFEHVIgpEGVLKNK----TRILVTHGISYLPQ-VDVIIVMSGGKISEMGS 844
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-235 |
1.31e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQP-IIEFRGVSQSF--GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGH---------- 70
Cdd:PTZ00243 1303 PVQAgSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigayglrel 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 71 RRQRSieegekalgvgLVFQQSALFDSlTVAENVGFTLyrdsDLRPREIRAIveenLELVGL--------PGIGDRF--- 139
Cdd:PTZ00243 1383 RRQFS-----------MIPQDPVLFDG-TVRQNVDPFL----EASSAEVWAA----LELVGLrervasesEGIDSRVleg 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 140 PAELSGGMRKRVSLARAIVinpeqhQQYKNILLYDEPTAGLDPVASTRIESLIRHLLSQdhvcccYLIVT--HQFSTIDN 217
Cdd:PTZ00243 1443 GSNYSVGQRQLMCMARALL------KKGSGFILMDEATANIDPALDRQIQATVMSAFSA------YTVITiaHRLHTVAQ 1510
|
250
....*....|....*...
gi 499173792 218 tTDRIIFLYDGKIQWDGS 235
Cdd:PTZ00243 1511 -YDKIIVMDHGAVAEMGS 1527
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-238 |
1.82e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.11 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRkVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD----SGEVIVHGHRRQRSIEEGEKalg 84
Cdd:PRK10418 5 IELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRGRK--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQ--QSALFDSLTVAENVGFTLYRDSDLRPreiRAIVEENLELVGLPG---IGDRFPAELSGGMRKRVSLARAIVI 159
Cdd:PRK10418 81 IATIMQnpRSAFNPLHTMHTHARETCLALGKPAD---DATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVccCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTAD 238
Cdd:PRK10418 158 EAP-------FIIADEPTTDLDVVAQARILDLLESIVQKRAL--GMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-245 |
1.89e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 25 DDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD---SGEVIVHGhRRQRSIEEGE----KALGVGLVFQQSalFDS 97
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNG-REILNLPEKElnklRAEQISMIFQDP--MTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTVAENVGFTLYRDSDLRPREIRA-IVEEN---LELVGLPGIGDR---FPAELSGGMRKRVSLARAIVINPEqhqqyknI 170
Cdd:PRK09473 110 LNPYMRVGEQLMEVLMLHKGMSKAeAFEESvrmLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPK-------L 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 171 LLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADA-YKSEHP 245
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNEL--KREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVfYQPSHP 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-181 |
1.92e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.25 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLtPDSGEVIVHGHR----------RQRSIeegekalgvgLVFQQSA 93
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlsdwsaaelaRHRAY----------LSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 94 LFdSLTVaenvgF---TLYRDSDLRPREIRAIVEenlELVGLPGIGDRFP---AELSGGMRKRVSLARAIV-INPEQHQQ 166
Cdd:COG4138 81 PF-AMPV-----FqylALHQPAGASSEAVEQLLA---QLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLLqVWPTINPE 151
|
170
....*....|....*
gi 499173792 167 YKnILLYDEPTAGLD 181
Cdd:COG4138 152 GQ-LLLLDEPMNSLD 165
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-215 |
1.96e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG-RK--VILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGV 85
Cdd:PTZ00265 383 IQFKNVRFHYDtRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 86 GLVFQQSALFdSLTVAENVGFTLYRDSDLRPRE-------------------IRAIVEENLELVG--------------- 131
Cdd:PTZ00265 463 GVVSQDPLLF-SNSIKNNIKYSLYSLKDLEALSnyynedgndsqenknkrnsCRAKCAGDLNDMSnttdsneliemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 132 --------------------LPGIGDRF-------PAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVA 184
Cdd:PTZ00265 542 qtikdsevvdvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPK-------ILILDEATSSLDNKS 614
|
250 260 270
....*....|....*....|....*....|.
gi 499173792 185 STRIESLIRHLLSQDHVCCcyLIVTHQFSTI 215
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRIT--IIIAHRLSTI 643
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-230 |
2.35e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGlltpD-----SGEVIVHGHRR------ 72
Cdd:PRK10938 256 ANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgySNDLTLFGRRRgsgeti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 73 ---QRSIeegekalgvGLVFQQ----------------SALFDSLTVAENVgftlyrdSDlrprEIRAIVEENLELVGLP 133
Cdd:PRK10938 332 wdiKKHI---------GYVSSSlhldyrvstsvrnvilSGFFDSIGIYQAV-------SD----RQQKLAQQWLDILGID 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 134 G-IGDRFPAELSGGMRKRVSLARAIVINPeqhqqykNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVccCYLIVTHQF 212
Cdd:PRK10938 392 KrTADAPFHSLSWGQQRLALIVRALVKHP-------TLLILDEPLQGLDPLNRQLVRRFVDVLISEGET--QLLFVSHHA 462
|
250
....*....|....*....
gi 499173792 213 STIDN-TTDRIIFLYDGKI 230
Cdd:PRK10938 463 EDAPAcITHRLEFVPDGDI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-230 |
3.48e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 10 EFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVhghrrqrsieeGEKaLGVGLVF 89
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----------GTK-LEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 90 QQSALFD-SLTVAENVGftlyrDS------DLRPREIRAIVEENLelvgLPGIGDRFPAE-LSGGMRKRVSLARaIVINP 161
Cdd:PRK11147 389 QHRAELDpEKTVMDNLA-----EGkqevmvNGRPRHVLGYLQDFL----FHPKRAMTPVKaLSGGERNRLLLAR-LFLKP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 162 eqhqqyKNILLYDEPTAGLDpvastrIES--LIRHLLS--QDHVcccyLIVTH--QFstIDNT-TDRIIFLYDGKI 230
Cdd:PRK11147 459 ------SNLLILDEPTNDLD------VETleLLEELLDsyQGTV----LLVSHdrQF--VDNTvTECWIFEGNGKI 516
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-226 |
3.77e-12 |
|
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: 64.31 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 33 PGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEvivhgHRRQRSIEEGEKAlgvglvFQQSALFDSLTVAENVGFTLYRDS 112
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-----FDDPPDWDEILDE------FRGSELQNYFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 113 ---DLRPREIRAIVEENLELV-------------GLPGIGDRFPAELSGGMRKRVSLARAIVinpeqhqQYKNILLYDEP 176
Cdd:cd03236 94 qyvDLIPKAVKGKVGELLKKKdergkldelvdqlELRHVLDRNIDQLSGGELQRVAIAAALA-------RDADFYFFDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499173792 177 TAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLY 226
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYV---LVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-198 |
1.89e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 20 RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEKALGVglVFQQSALFdSL 98
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPlTKLQLDSWRSRLAV--VSQTPFLF-SD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 99 TVAENVGFTlyrdsdlRPREIRAIVEENLELVG-------LPG-----IGDRfPAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:PRK10789 404 TVANNIALG-------RPDATQQEIEHVARLASvhddilrLPQgydteVGER-GVMLSGGQKQRISIARALLLNAE---- 471
|
170 180 190
....*....|....*....|....*....|..
gi 499173792 167 yknILLYDEPTAGLDpvasTRIESLIRHLLSQ 198
Cdd:PRK10789 472 ---ILILDDALSAVD----GRTEHQILHNLRQ 496
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-229 |
2.78e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 8 IIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS--GEVIVHGHRRQ-RSIEEGEkALG 84
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRfKDIRDSE-ALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQQSALFDSLTVAENV---------GFTLYRDSDLRPREIRAIV--EENLE-LVGLPGIGDRFPAELSGGMRKRVS 152
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIflgnerakrGVIDWNETNRRARELLAKVglDESPDtLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 153 LaraivinpeqhqqykniLLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGK 229
Cdd:NF040905 160 L-----------------LILDEPTAALNEEDSAALLDLLLELKAQGITS---IIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-223 |
2.98e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 31 IYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVivhghrrqrsieegekalgvglvfqqsalFDSLTVAenvgftlYR 110
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----------------------------DPELKIS-------YK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 111 ------DSDLRPRE-IRAIVEE------NLELV---GLPGIGDRFPAELSGGMRKRVSLARAIVinpeqhqQYKNILLYD 174
Cdd:PRK13409 406 pqyikpDYDGTVEDlLRSITDDlgssyyKSEIIkplQLERLLDKNVKDLSGGELQRVAIAACLS-------RDADLYLLD 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499173792 175 EPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRII 223
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEREATA--LVVDHDIYMIDYISDRLM 525
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-223 |
3.01e-11 |
|
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: 62.88 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 30 KIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVivhghrrqrsieegEKALGV------------GLVfqQSALFDS 97
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------------DEDLKIsykpqyispdydGTV--EEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTvaENVGFTLYRDSDLRPREIRAIVEENLElvglpgigdrfpaELSGGMRKRVSLARAIVinpeqhqQYKNILLYDEPT 177
Cdd:COG1245 426 NT--DDFGSSYYKTEIIKPLGLEKLLDKNVK-------------DLSGGELQRVAIAACLS-------RDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499173792 178 AGLDpvASTRIE--SLIRHLLSQDHVCCcyLIVTHQFSTIDNTTDRII 223
Cdd:COG1245 484 AHLD--VEQRLAvaKAIRRFAENRGKTA--MVVDHDIYLIDYISDRLM 527
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-230 |
3.16e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGR-KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEE-GEKAL--G 84
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG----RPLSSlSHSVLrqG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVfQQSALFDSLTVAENVgfTLYRDSDlrpreiRAIVEENLELVGLPGIGDRFPA-----------ELSGGMRKRVSL 153
Cdd:PRK10790 417 VAMV-QQDPVVLADTFLANV--TLGRDIS------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 154 ARAIVINPEqhqqyknILLYDEPTAGLDpvasTRIESLIRHLLSQDHVCCCYLIVTHQFSTIDNtTDRIIFLYDGKI 230
Cdd:PRK10790 488 ARVLVQTPQ-------ILILDEATANID----SGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-250 |
3.24e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHrrqrsieegekalgVGLVFQQSALFDSLTVAEN 103
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 104 VGFTLYRdSDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPV 183
Cdd:PRK13546 106 IEFKMLC-MGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPD-------ILVIDEALSVGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 184 ASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADAYKSEHPLLKQF 250
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTI---FFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDF 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-198 |
3.32e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqRSIEEGEKAL-- 83
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDITDWQTAKim 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 84 --GVGLVFQQSALFDSLTVAENV---GFTLYRDS---------DLRPReiraIVEENLELVGlpgigdrfpaELSGGMRK 149
Cdd:PRK11614 79 reAVAIVPEGRRVFSRMTVEENLamgGFFAERDQfqerikwvyELFPR----LHERRIQRAG----------TMSGGEQQ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499173792 150 RVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQ 198
Cdd:PRK11614 145 MLAIGRALMSQPR-------LLLLDEPSLGLAPIIIQQIFDTIEQLREQ 186
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-226 |
3.43e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 33 PGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEvivhgHRRQRSIEEGEKAlgvglvFQQSALFDSltvaenvgFTLYRDS 112
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD-----YEEEPSWDEVLKR------FRGTELQNY--------FKKLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 113 DLRP------------------REI------RAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINpeqhqqyK 168
Cdd:PRK13409 159 EIKVvhkpqyvdlipkvfkgkvRELlkkvdeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRD-------A 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 169 NILLYDEPTAGLDPVASTRIESLIRHLLSQDHVcccyLIVTHQFSTIDNTTDRIIFLY 226
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIRELAEGKYV----LVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-191 |
4.83e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVivhghrrqrsiEEGEKAlGVGLV 88
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENA-NIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSAL-FDS-LTVAENVG-FTLYRDSDLrprEIRAIVEENLelvglpgigdrFPAE--------LSGGMRKRVSLARAI 157
Cdd:PRK15064 388 AQDHAYdFENdLTLFDWMSqWRQEGDDEQ---AVRGTLGRLL-----------FSQDdikksvkvLSGGEKGRMLFGKLM 453
|
170 180 190
....*....|....*....|....*....|....
gi 499173792 158 VINPeqhqqykNILLYDEPTAGLDPVAstrIESL 191
Cdd:PRK15064 454 MQKP-------NVLVMDEPTNHMDMES---IESL 477
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-232 |
1.01e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 12 RGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrRQRSIEEGEKAL--GVGLVF 89
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG--KEIDFKSSKEALenGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 90 QQSALFDSLTVAENVGFTLYR------DSDLRPREIRAIVEEnLELvglpgigDRFP----AELSGGMRKRVSLARAIVI 159
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPtkgmfvDQDKMYRDTKAIFDE-LDI-------DIDPrakvATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 160 NPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGkiQW 232
Cdd:PRK10982 152 NAK-------IVIMDEPTSSLTEKEVNHLFTIIRKLKERG---CGIVYISHKMEEIFQLCDEITILRDG--QW 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-230 |
1.10e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 6 QPIIEFRGVSQSFGRKVilDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR-RQRSIEEGEKAlG 84
Cdd:PRK09700 263 ETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPLDAVKK-G 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 85 VGLVFQ---QSALFDSLTVAENVGFTLY-RDSDLR-------PREIRAIVEENLELVGLPGIG-DRFPAELSGGMRKRVS 152
Cdd:PRK09700 340 MAYITEsrrDNGFFPNFSIAQNMAISRSlKDGGYKgamglfhEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 153 LARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNTTDRIIFLYDGKI 230
Cdd:PRK09700 420 ISKWLCCCPE-------VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVI---LMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-232 |
2.17e-10 |
|
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: 57.93 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVS-QSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQrsieegekalgvgL 87
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDL-------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENVGFTLYRdsdlrpreiraiveenlelvglpgigdrfpaELSGGMRKRVSLARAIVINPeqhqqy 167
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDD-------------------------------VLSGGEQQRLAFARLLLHKP------ 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499173792 168 KNILLyDEPTAGLDPVASTRIESLIRHLLsqdhvcCCYLIVTHQfSTIDNTTDRIIFLyDGKIQW 232
Cdd:cd03223 111 KFVFL-DEATSALDEESEDRLYQLLKELG------ITVISVGHR-PSLWKFHDRVLDL-DGEGGW 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-235 |
5.68e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 23 ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEvIVHGHRRQRSieegekalgvglvfQQSALFDSLTVAE 102
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK-IKHSGRISFS--------------PQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 103 NVGFTLYRDSDLRPREIRAI-VEENLELvgLPGiGDRFP-----AELSGGMRKRVSLARAIvinpeqhqqYKNILLY--D 174
Cdd:TIGR01271 506 NIIFGLSYDEYRYTSVIKACqLEEDIAL--FPE-KDKTVlgeggITLSGGQRARISLARAV---------YKDADLYllD 573
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499173792 175 EPTAGLDPVASTRI-ESLIRHLLSQDhvccCYLIVTHQFSTIDNtTDRIIFLYDGKIQWDGS 235
Cdd:TIGR01271 574 SPFTHLDVVTEKEIfESCLCKLMSNK----TRILVTSKLEHLKK-ADKILLLHEGVCYFYGT 630
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-226 |
5.75e-10 |
|
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: 59.03 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 33 PGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEvivhgHRRQRSIEEGEKAlgvglvFQQSALFDSLT-VAENvgftlyrd 111
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGD-----YDEEPSWDEVLKR------FRGTELQDYFKkLANG-------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 112 sDLRP------------------REI------RAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINpeqhqqy 167
Cdd:COG1245 159 -EIKVahkpqyvdlipkvfkgtvRELlekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRD------- 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 168 KNILLYDEPTAGLDPVASTRIESLIRHLLSQDH-VcccyLIVTHQFSTIDNTTDRIIFLY 226
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKyV----LVVEHDLAILDYLADYVHILY 286
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-229 |
1.04e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.89 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 7 PIIEFRGVSQSF----GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGlLTPDSGEVIVHGHR------RQRSI 76
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRfddidlLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEGEKALG--VGLVFQ--QSALFDSltvaENVGFTLYRD-----------SDLRPREIRAIveenlELVGLPGIGDR--- 138
Cdd:PRK15093 81 RERRKLVGhnVSMIFQepQSCLDPS----ERVGRQLMQNipgwtykgrwwQRFGWRKRRAI-----ELLHRVGIKDHkda 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 139 ---FPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCcyLIVTHQFSTI 215
Cdd:PRK15093 152 mrsFPYELTEGECQKVMIAIALANQPR-------LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTI--LLISHDLQML 222
|
250
....*....|....
gi 499173792 216 DNTTDRIIFLYDGK 229
Cdd:PRK15093 223 SQWADKINVLYCGQ 236
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
9-182 |
1.10e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSFG-RKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALgVGL 87
Cdd:PRK10522 323 LELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 88 VFQQSALFDSLTVAENvgftlyRDSDlrpreiRAIVEENLELVGLpgiGDRFPAE--------LSGGMRKRVSLARAIVi 159
Cdd:PRK10522 402 VFTDFHLFDQLLGPEG------KPAN------PALVEKWLERLKM---AHKLELEdgrisnlkLSKGQKKRLALLLALA- 465
|
170 180
....*....|....*....|...
gi 499173792 160 npEQhqqyKNILLYDEPTAGLDP 182
Cdd:PRK10522 466 --EE----RDILLLDEWAADQDP 482
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-183 |
1.10e-09 |
|
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: 58.27 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 9 IEFRGVSQSF-----GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHR---------RQR 74
Cdd:COG4615 328 LELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPvtadnreayRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 75 -SIeegekalgvglVFQQSALFDSLtvaenvgftLYRDSDLRPREIRAIVEEnLELVGLPGI-GDRF-PAELSGGMRKRV 151
Cdd:COG4615 408 fSA-----------VFSDFHLFDRL---------LGLDGEADPARARELLER-LELDHKVSVeDGRFsTTDLSQGQRKRL 466
|
170 180 190
....*....|....*....|....*....|..
gi 499173792 152 SLARAIVinpEQhqqyKNILLYDEPTAGLDPV 183
Cdd:COG4615 467 ALLVALL---ED----RPILVFDEWAADQDPE 491
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-239 |
1.27e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQ-RSIEEGekaLGVGLVF-----QQSALFDS 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDG---LANGIVYisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTVAENVGFTLYRD-----SDLRPREIRAIVEENLEL--VGLPGIgDRFPAELSGGMRKRVSLARAIVINPeqhqqykNI 170
Cdd:PRK10762 345 MSVKENMSLTALRYfsragGSLKHADEQQAVSDFIRLfnIKTPSM-EQAIGLLSGGNQQKVAIARGLMTRP-------KV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499173792 171 LLYDEPTAGLDPVASTRIESLIRHL----LSqdhvcccYLIVTHQFSTIDNTTDRIIFLYDGKIQWDGSTADA 239
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFkaegLS-------IILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA 482
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-228 |
1.35e-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: 56.57 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALG---VGLVFQQSALFDSlTV 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 101 AENVGFtlyrDSDLRPREIRAIVEE-----NLELvgLP-----GIGDRfPAELSGGMRKRVSLARAIVinpeqhqQYKNI 170
Cdd:cd03290 96 EENITF----GSPFNKQRYKAVTDAcslqpDIDL--LPfgdqtEIGER-GINLSGGQRQRICVARALY-------QNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 171 LLYDEPTAGLDPVASTRI-ESLIRHLLSQDHVCCcyLIVTHQFSTIDNtTDRIIFLYDG 228
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTL--VLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-241 |
1.57e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQPIIEFRGVSQSF-GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRsieegeka 82
Cdd:PLN03073 504 PGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA-------- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 83 lgvglVFQQSALfDSLTVAENVGFTLYRDSDLRPRE-IRAiveeNLELVGLPGIGDRFPA-ELSGGMRKRVSLARAIVIN 160
Cdd:PLN03073 576 -----VFSQHHV-DGLDLSSNPLLYMMRCFPGVPEQkLRA----HLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKK 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 161 PeqhqqykNILLYDEPTAGLDPVAstrIESLIRHL-LSQDHVCccylIVTHQFSTIDNTTDRIIFLYDGKIQ-WDGSTAD 238
Cdd:PLN03073 646 P-------HILLLDEPSNHLDLDA---VEALIQGLvLFQGGVL----MVSHDEHLISGSVDELWVVSEGKVTpFHGTFHD 711
|
...
gi 499173792 239 aYK 241
Cdd:PLN03073 712 -YK 713
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-216 |
8.97e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.01 E-value: 8.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 12 RGVSQSfgRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD--SGEVIVHGH-RRQRSIeegekALGVGLV 88
Cdd:PLN03140 886 QGVTED--RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFpKKQETF-----ARISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 89 FQQSALFDSLTVAENVGFTLYrdsdLR-PREIRA-----IVEENLELV----------GLPGIgdrfpAELSGGMRKRVS 152
Cdd:PLN03140 959 EQNDIHSPQVTVRESLIYSAF----LRlPKEVSKeekmmFVDEVMELVeldnlkdaivGLPGV-----TGLSTEQRKRLT 1029
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499173792 153 LARAIVINPeqhqqykNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCCYLivtHQFStID 216
Cdd:PLN03140 1030 IAVELVANP-------SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTI---HQPS-ID 1082
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-228 |
1.48e-08 |
|
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: 54.09 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 23 ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEvIVHGHRRQRSieegekalgvglvfQQSALFDSLTVAE 102
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-IKHSGRISFS--------------SQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 103 NVGFTLYRDsDLRPR----------EIRAIVEENLELVGLPGIgdrfpaELSGGMRKRVSLARAIvinpeqhqqYKNILL 172
Cdd:cd03291 117 NIIFGVSYD-EYRYKsvvkacqleeDITKFPEKDNTVLGEGGI------TLSGGQRARISLARAV---------YKDADL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499173792 173 Y--DEPTAGLDPVASTRI-ESLIRHLLSQDhvccCYLIVTHQFSTIdNTTDRIIFLYDG 228
Cdd:cd03291 181 YllDSPFGYLDVFTEKEIfESCVCKLMANK----TRILVTSKMEHL-KKADKILILHEG 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-211 |
2.89e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALgvGLVFQQSALFDSLTV 100
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL--CFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 101 AENVGFTLYRDSDlrpreiRAIVEENLELVGLPGIGDrFPAE-LSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAG 179
Cdd:PRK13540 92 RENCLYDIHFSPG------AVGITELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAK-------LWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|..
gi 499173792 180 LDPVAstrIESLIRHLLSQDHVCCCYLIVTHQ 211
Cdd:PRK13540 158 LDELS---LLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-175 |
1.47e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGhrrqrsieegekalGVGLVFQQSALFDSLTVAEN 103
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------------SAALIAISSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499173792 104 V---GFTLyrdsDLRPREIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDE 175
Cdd:PRK13545 106 IelkGLMM----GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPD-------ILVIDE 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-233 |
2.07e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.36 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD-SGEVIVHGHrrQRSIEEGEKALGVGLVF-----QQSALFDS 97
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGK--PVDIRNPAQAIRAGIAMvpedrKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTVAENVGFTLYRDSDLRPR-----EIRAIVEENLELVGLPGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILL 172
Cdd:TIGR02633 354 LGVGKNITLSVLKSFCFKMRidaaaELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPR-------VLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 173 YDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWD 233
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEG---VAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-226 |
2.11e-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: 49.88 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 34 GEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVivhghrrqrsieegekalgvglvfqqsaLFDSLTVAenvgftlyrdsd 113
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------------------EWDGITPV------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 114 LRPREIraiveenlelvglpgigdrfpaELSGGMRKRVSLARAIVINpeqhqqyKNILLYDEPTAGLDPVASTRIESLIR 193
Cdd:cd03222 65 YKPQYI----------------------DLSGGELQRVAIAAALLRN-------ATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|...
gi 499173792 194 HLLsqDHVCCCYLIVTHQFSTIDNTTDRIIFLY 226
Cdd:cd03222 116 RLS--EEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-181 |
3.18e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 18 FGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVivhghrrqrSIEEGEKalgVGLVFQQSALFDS 97
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV---------SLDPNER---LGKLRQDQFAFEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 98 LTVAENV--GFT-LYRDSDLRPReIRAIVE---------ENLE------------------LVGLpGIGDRFP----AEL 143
Cdd:PRK15064 79 FTVLDTVimGHTeLWEVKQERDR-IYALPEmseedgmkvADLEvkfaemdgytaearagelLLGV-GIPEEQHyglmSEV 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 499173792 144 SGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLD 181
Cdd:PRK15064 157 APGWKLRVLLAQALFSNPD-------ILLLDEPTNNLD 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
19-211 |
9.32e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRivaglltpdsgevivhghrrqrsieegekALGVGLVFQQSALfdsl 98
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILD-----------------------------AIGLALGGAQSAT---- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 99 tvaenvgftlYRDSDLRPREIRAIVEenLELVG-LPGigdrfpaeLSGGMRKRVSLARAIvinpeQHQQYKNILLY--DE 175
Cdd:cd03227 53 ----------RRRSGVKAGCIVAAVS--AELIFtRLQ--------LSGGEKELSALALIL-----ALASLKPRPLYilDE 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 499173792 176 PTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQ 211
Cdd:cd03227 108 IDRGLDPRDGQALAEAILEHLVKG---AQVIVITHL 140
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-230 |
1.35e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 2 SEPVQPIIEFRGVSQSfgRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHG-----HRRQRSI 76
Cdd:PRK10982 244 NKPGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnHNANEAI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 77 EEG-----EKALGVGLVFQQSALFDSLTvaENV-----GFTLYRDSDLRPREIRAIVEENlelVGLPG----IGdrfpaE 142
Cdd:PRK10982 322 NHGfalvtEERRSTGIYAYLDIGFNSLI--SNIrnyknKVGLLDNSRMKSDTQWVIDSMR---VKTPGhrtqIG-----S 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 143 LSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQFSTIDNTTDRI 222
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPE-------ILMLDEPTRGIDVGAKFEIYQLIAELAKKDK---GIIIISSEMPELLGITDRI 461
|
....*...
gi 499173792 223 IFLYDGKI 230
Cdd:PRK10982 462 LVMSNGLV 469
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-230 |
1.53e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 21 KVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGL--LTPDSGEVIVHGHRRQRSIEEGEKALGVGLVFQ-------- 90
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQypveipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 91 --QSALFDSLTVAENvgftlYRDSDLRPR-EIRAIVEENLELVGLPG--IGDRFPAELSGGMRKRVSLARAIVINPEqhq 165
Cdd:PRK09580 94 snQFFLQTALNAVRS-----YRGQEPLDRfDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMAVLEPE--- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 166 qyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHvccCYLIVTHQFSTIDNTT-DRIIFLYDGKI 230
Cdd:PRK09580 166 ----LCILDESDSGLDIDALKIVADGVNSLRDGKR---SFIIVTHYQRILDYIKpDYVHVLYQGRI 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-67 |
5.52e-06 |
|
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: 45.06 E-value: 5.52e-06
10 20 30
....*....|....*....|....*....|....*
gi 499173792 33 PGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIV 67
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-181 |
6.36e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHghrrQRSIEEGEKALgVGLVFQQSALFDSLTVAEN 103
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYK----NCNINNIAKPY-CTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 104 VGF--TLYRDSDLRPREIraiveenlELVGLPGIGDRFPAELSGGMRKRVSLARAIVInpeqhqqYKNILLYDEPTAGLD 181
Cdd:PRK13541 91 LKFwsEIYNSAETLYAAI--------HYFKLHDLLDEKCYSLSSGMQKIVAIARLIAC-------QSDLWLLDEVETNLS 155
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-234 |
6.92e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 23 ILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPD---SGEVIVHGHR------RQRSIEEGEKALGVGLVFQQSA 93
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRlnefvpRKTSAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 94 LfDSLTVAENVGFTLYRDSDLRPREIRA------------------------IVEENLELVGL-----PGIGDRFPAELS 144
Cdd:PLN03140 260 L-DFSARCQGVGTRYDLLSELARREKDAgifpeaevdlfmkatamegvksslITDYTLKILGLdickdTIVGDEMIRGIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 145 GGMRKRVSLARAIViNPEQhqqyknILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCCCYLIVTHQFSTIDnTTDRIIF 224
Cdd:PLN03140 339 GGQKKRVTTGEMIV-GPTK------TLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFD-LFDDIIL 410
|
250
....*....|
gi 499173792 225 LYDGKIQWDG 234
Cdd:PLN03140 411 LSEGQIVYQG 420
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-181 |
9.10e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQRSIEEGEKALGVGLV---------F 89
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALeyvidgdreY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 90 QQsaLFDSLTVA--ENVGF---TLYRDSD-LRPREIRAIVEENLELVGLPGIGDRFP-AELSGGMRKRVSLARAIVINpe 162
Cdd:PRK10636 92 RQ--LEAQLHDAneRNDGHaiaTIHGKLDaIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICR-- 167
|
170
....*....|....*....
gi 499173792 163 qhqqyKNILLYDEPTAGLD 181
Cdd:PRK10636 168 -----SDLLLLDEPTNHLD 181
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-233 |
1.93e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 19 GRKVIlDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS-GEVIVHGhrRQRSIEEGEKALGVGLVF-----QQS 92
Cdd:PRK13549 274 HIKRV-DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDG--KPVKIRNPQQAIAQGIAMvpedrKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 93 ALFDSLTVAENVGFTLYRDSDLRPR-----EIRAIVEENLEL-VGLPGIGDRFpAELSGGMRKRVSLARAIVINPeqhqq 166
Cdd:PRK13549 351 GIVPVMGVGKNITLAALDRFTGGSRiddaaELKTILESIQRLkVKTASPELAI-ARLSGGNQQKAVLAKCLLLNP----- 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 167 ykNILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYDGKIQWD 233
Cdd:PRK13549 425 --KILILDEPTRGIDVGAKYEIYKLINQLVQQG---VAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-227 |
2.23e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 20 RKVILDDvdLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVIVHGHRRQR-SIEEGEKalgvgLVFQ--QSALFD 96
Cdd:PRK10938 17 KTLQLPS--LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlSFEQLQK-----LVSDewQRNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 97 SLTVAENvgftlyrDSDLRPREIraIVEEN------LELVGLPGIGD----RFpAELSGGMRKRVSLARAIVINPEqhqq 166
Cdd:PRK10938 90 MLSPGED-------DTGRTTAEI--IQDEVkdparcEQLAQQFGITAlldrRF-KYLSTGETRKTLLCQALMSEPD---- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499173792 167 yknILLYDEPTAGLDPVASTRIESLIRHLLSQDhvcCCYLIVTHQFSTIDNTTDRIIFLYD 227
Cdd:PRK10938 156 ---LLILDEPFDGLDVASRQQLAELLASLHQSG---ITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
87-224 |
4.21e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 87 LVFQQSALFDsLTVAENVGFTlyRDSDLRPREIR----AIVEENLElvGLPGIGDR----FPAELSGGMRKRVSLARAIV 158
Cdd:PTZ00265 1300 IVSQEPMLFN-MSIYENIKFG--KEDATREDVKRackfAAIDEFIE--SLPNKYDTnvgpYGKSLSGGQKQRIAIARALL 1374
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499173792 159 INPEqhqqyknILLYDEPTAGLDPVASTRIESLIRHLlsQDHVCCCYLIVTHQFSTIDNTTDRIIF 224
Cdd:PTZ00265 1375 REPK-------ILLLDEATSSLDSNSEKLIEKTIVDI--KDKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-62 |
8.03e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 8.03e-05
10 20 30
....*....|....*....|....*....|....*...
gi 499173792 25 DDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDS 62
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-234 |
3.55e-04 |
|
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: 40.38 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 24 LDDVDLKIYPGEAVGVIGPSGTGKSTILRivaglltpdsgevivhghrrqrsiEEGEKALGVGLVFQQSALFDSLTVAen 103
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------------EGLYASGKARLISFLPKFSRNKLIF-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 104 VGftlyrdsdlrprEIRAIVEENLELVGLpgigDRFPAELSGGMRKRVSLARAIVINPEqhqqyKNILLYDEPTAGLDPV 183
Cdd:cd03238 65 ID------------QLQFLIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPP-----GTLFILDEPSTGLHQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499173792 184 ASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDnTTDRIIFL------YDGKIQWDG 234
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTV---ILIEHNLDVLS-SADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-190 |
1.43e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 4 PVQPIIEFRGVSQSFGRKVILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVA-----GLltPDSGEVIvhgHRRQRSIEE 78
Cdd:PLN03073 173 PAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQIL---HVEQEVVGD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 79 GEKALG----------------VGLVFQQSALFDSLTVAENVGFTlyrDSDLRPREIRAIVEE---NLELV--------- 130
Cdd:PLN03073 248 DTTALQcvlntdiertqlleeeAQLVAQQRELEFETETGKGKGAN---KDGVDKDAVSQRLEEiykRLELIdaytaeara 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499173792 131 -----GL---PGIGDRFPAELSGGMRKRVSLARAIVINPEqhqqyknILLYDEPTAGLDPVASTRIES 190
Cdd:PLN03073 325 asilaGLsftPEMQVKATKTFSGGWRMRIALARALFIEPD-------LLLLDEPTNHLDLHAVLWLET 385
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
22-66 |
2.25e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 38.12 E-value: 2.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 499173792 22 VILDDVDLKIYPGEAVGVIGPSGTGKSTILRIVAGLLTPDSGEVI 66
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI 45
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-253 |
5.74e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499173792 141 AELSGGMRKRVSLARAIVINPEQhqqyKNILLYDEPTAGLDPVASTRIESLIRHLLSQDHVCccyLIVTHQFSTIDNtTD 220
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKH----PTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSV---IYIDHDPALLKQ-AD 1769
|
90 100 110
....*....|....*....|....*....|....*....
gi 499173792 221 RIIFL------YDGKIQWDGSTADAYKSEHPLLKQFFSG 253
Cdd:PRK00635 1770 YLIEMgpgsgkTGGKILFSGPPKDISASKDSLLKTYMCN 1808
|
|
| |
