|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-256 |
2.73e-138 |
|
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: 389.40 E-value: 2.73e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILP 83
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLECCI 243
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|...
gi 489326441 244 MRSPIDQKPMCLP 256
Cdd:COG1120 242 IEDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-255 |
2.10e-115 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 331.59 E-value: 2.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 3 KLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAIL 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLNrDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLECC 242
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|...
gi 489326441 243 IMRSPIDQKPMCL 255
Cdd:PRK11231 241 IHPEPVSGTPMCV 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-256 |
4.72e-105 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 305.08 E-value: 4.72e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSP 86
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAPEGLTVEELCYFGRHPHKKllSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:COG4604 85 HINSRLTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 167 TTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLECCIMRs 246
Cdd:COG4604 163 LNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVEE- 241
|
250
....*....|
gi 489326441 247 pIDQKPMCLP 256
Cdd:COG4604 242 -IDGKRICVY 250
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-258 |
1.20e-97 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 286.88 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 3 KLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAIL 82
Cdd:PRK10253 7 RLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLECC 242
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCM 246
|
250
....*....|....*.
gi 489326441 243 IMRSPIDQKPMCLPTG 258
Cdd:PRK10253 247 IIDDPVAGTPLVVPLG 262
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-222 |
7.31e-87 |
|
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: 256.21 E-value: 7.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 5 AADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQ 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 spqapegltveelcyfgrhphkkllskhtqedhdmvewALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLD 164
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 165 EPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAG 222
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-256 |
9.63e-82 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 246.18 E-value: 9.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILP 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYFGRHPHkkllSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQ------- 156
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRdHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREV 236
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
250 260
....*....|....*....|
gi 489326441 237 FGLECCIMRSPIDQKPMCLP 256
Cdd:COG4559 237 YGADLRVLAHPEGGCPQVLP 256
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-238 |
2.67e-80 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 241.92 E-value: 2.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPskevaKKLAILP 83
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEG--LTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRdHGRTVVMVLHDLNQAAQYADYLIsVLDGKIYNAGTPEDVFTQPFFREVFG 238
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVL-LLNRGLVAHGPPEEVLTPENLSRAYG 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-256 |
6.27e-76 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 231.20 E-value: 6.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILP 83
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYFGRHPHkkllSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQ------G 157
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 158 TDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVF 237
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
|
250
....*....|....*....
gi 489326441 238 GLECCIMRSPIDQKPMCLP 256
Cdd:PRK13548 239 GADVLVQPHPETGAPLVLP 257
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-256 |
2.29e-71 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 224.34 E-value: 2.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQA 88
Cdd:PRK09536 9 LSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 89 PEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTT 168
Cdd:PRK09536 89 SFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 169 YLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLECCIMRSPI 248
Cdd:PRK09536 169 SLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVGTDPA 247
|
....*...
gi 489326441 249 DQKPMCLP 256
Cdd:PRK09536 248 TGAPTVTP 255
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
7-253 |
4.72e-71 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 219.27 E-value: 4.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSP 86
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 167 TTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLECCIMRS 246
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPH 254
|
....*..
gi 489326441 247 PIDQKPM 253
Cdd:PRK10575 255 PAGAAPV 261
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-231 |
3.44e-65 |
|
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: 202.95 E-value: 3.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAIL 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQ----APeglTVEE-----LCYFGrhphkklLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMA 153
Cdd:COG1122 81 FQNPDdqlfAP---TVEEdvafgPENLG-------LPR--EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 154 LAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLIsVLD-GKIYNAGTPEDVFTQP 231
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVI-VLDdGRIVADGTPREVFSDY 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-222 |
1.28e-64 |
|
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: 200.84 E-value: 1.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPskevaKKLAILPQS 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEG--LTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:cd03235 77 RSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNRdHGRTVVMVLHDLNQAAQYADYLIsVLDGKIYNAG 222
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVL-LLNRTVVASG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-237 |
9.85e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 189.12 E-value: 9.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPsKEVAKKLAILP 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEE-LCYFGR-HPHKKllskhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:COG1131 80 QEPALYPDLTVREnLRFFARlYGLPR------KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDvFTQPFFREVF 237
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE-LKARLLEDVF 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-240 |
7.39e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.88 E-value: 7.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS-TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK---KL 79
Cdd:COG3638 3 LELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEE--LC-YFGRHP-HKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALA 155
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTnvLAgRLGRTStWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 156 QGTDLLLLDEPTTYLD--ISHQieVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVfTQPFF 233
Cdd:COG3638 163 QEPKLILADEPVASLDpkTARQ--VMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVL 239
|
....*..
gi 489326441 234 REVFGLE 240
Cdd:COG3638 240 REIYGGE 246
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-217 |
9.64e-57 |
|
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: 180.74 E-value: 9.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDS--TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQ 84
Cdd:cd03225 3 KNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SpqaPE----GLTVEELCYFGRhphkKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDL 160
Cdd:cd03225 83 N---PDdqffGPTVEEEVAFGL----ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 161 LLLDEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGK 217
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-231 |
1.92e-56 |
|
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: 188.57 E-value: 1.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS-----TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPS---KEV 75
Cdd:COG1123 261 LEVRNLSKRYPVrgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 76 AKKLAILPQSPQA---PEgLTVEELCYFGRHPHKkLLSKhtQEDHDMVEWALEATGMI-ELKDRTLDALSGGQRQRAWIS 151
Cdd:COG1123 341 RRRVQMVFQDPYSslnPR-MTVGDIIAEPLRLHG-LLSR--AERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-231 |
3.82e-54 |
|
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: 182.41 E-value: 3.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPK---SGTVLLEGKDIHRQPSKEVAKK 78
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 79 LAILPQSPQ-APEGLTVEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQG 157
Cdd:COG1123 85 IGMVFQDPMtQLNPVTVGDQIAEA--LENLGLSR--AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 158 TDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-204 |
2.74e-53 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 171.26 E-value: 2.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGkdihrqpskevAKKLAILPQSPQAPEG 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 92 L--TVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTY 169
Cdd:NF040873 70 LplTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 489326441 170 LDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAA 204
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-227 |
9.99e-52 |
|
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: 168.88 E-value: 9.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPsKEVAKKLAILPQS 85
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEE-LCYFGRhphkkLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLD 164
Cdd:COG4555 83 RGLYDRLTVREnIRYFAE-----LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 165 EPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:COG4555 158 EPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-237 |
3.37e-51 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 167.36 E-value: 3.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE---VAKKL 79
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEE--LC-YFGRHPH-KKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALA 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnvLSgRLGRRSTwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 156 QGTDLLLLDEPTTYLD--ISHQieVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDvFTQPFF 233
Cdd:cd03256 161 QQPKLILADEPVASLDpaSSRQ--VMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVL 237
|
....
gi 489326441 234 REVF 237
Cdd:cd03256 238 DEIY 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-218 |
3.62e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.45 E-value: 3.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS----TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK-- 77
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 78 --KLAILPQSPQAPEGLTVEE-----LCYFGRHPhkkllskhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWI 150
Cdd:COG1136 85 rrHIGFVFQFFNLLPELTALEnvalpLLLAGVSR---------KERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 151 SMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLnQAAQYADYLISVLDGKI 218
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-218 |
3.68e-50 |
|
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: 164.20 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS----TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVA--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 77 -KKLAILPQSPQAPEGLTVEE----LCYFGRHPHKkllskhtqEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWIS 151
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALEnvelPLLLAGVPKK--------ERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDlNQAAQYADYLISVLDGKI 218
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-218 |
4.25e-50 |
|
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: 164.22 E-value: 4.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYD----STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH---RQPSKEVA 76
Cdd:cd03257 2 LEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 77 KKLAILPQSPQA---PeGLTVEELCyfgrhphKKLLSKHTQEDhdmVEWALEATGMIELKDRTLDA---------LSGGQ 144
Cdd:cd03257 82 KEIQMVFQDPMSslnP-RMTIGEQI-------AEPLRIHGKLS---KKEARKEAVLLLLVGVGLPEevlnrypheLSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 145 RQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-218 |
9.86e-50 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 161.41 E-value: 9.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPsKEVAKKLAILP 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELcyfgrhphkkllskhtqedhdmvewaleatgmieLKdrtldaLSGGQRQRAWISMALAQGTDLLLL 163
Cdd:cd03230 80 EEPSLYENLTVREN----------------------------------LK------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-231 |
1.33e-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: 163.38 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-LAIL 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEELCYFGRHPHKK---LLSKHTQEDHDMVEWA---LEATGMIELKDRTLDALSGGQRQRAWISMALAQ 156
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGsglLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYlISVLD-GKIYNAGTPEDVFTQP 231
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADR-VTVLDqGRVIAEGTPDEVRNNP 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-235 |
3.64e-49 |
|
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: 161.90 E-value: 3.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE---VAKKLAILPQS 85
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRMGMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEELCYFgrhphkkLLSKHTQEDHDM----VEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:cd03261 86 GALFDSLTVFENVAF-------PLREHTRLSEEEireiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 162 LLDEPTTYLD--ISHQIEvlELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVF--TQPFFRE 235
Cdd:cd03261 159 LYDEPTAGLDpiASGVID--DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPLVRQ 234
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-256 |
4.27e-49 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 163.07 E-value: 4.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLA-RLMAPK-------SGTVLLEGKDIHRQPSKEV 75
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 76 AKKLAILPQSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALA 155
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 156 Q---------GTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPED 226
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250 260 270
....*....|....*....|....*....|
gi 489326441 227 VFTQPFFREVFGLECCIMRSPIDQKPMCLP 256
Cdd:PRK13547 242 VLTPAHIARCYGFAVRLVDAGDGVPPVIVP 271
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-235 |
1.22e-48 |
|
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: 161.12 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS----TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQApeglTVeelcyfgrHPHKK--------LLSKHTQEDHDMVEWALEATGM-IELKDRTLDALSGGQRQRAWI 150
Cdd:COG1124 82 QMVFQDPYA----SL--------HPRHTvdrilaepLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 151 SMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV--- 227
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLlag 229
|
....*...
gi 489326441 228 FTQPFFRE 235
Cdd:COG1124 230 PKHPYTRE 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-229 |
4.99e-48 |
|
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: 159.37 E-value: 4.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE---VAKKLAILP 83
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSpqapeG-----LTVEE-LCYFgrhphkklLSKHT----QEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMA 153
Cdd:COG1127 89 QG-----GalfdsLTVFEnVAFP--------LREHTdlseAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 154 LAQGTDLLLLDEPTTYLD-IShQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFT 229
Cdd:COG1127 156 LALDPEILLYDEPTAGLDpIT-SAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-231 |
5.67e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 158.76 E-value: 5.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 23 DLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvaKKLAILPQS----PQapegLTVEELC 98
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQEnnlfPH----LTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 99 YFGRHPHKKLlskhTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEV 178
Cdd:COG3840 93 GLGLRPGLKL----TAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489326441 179 LELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:COG3840 169 LDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
7.92e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 157.67 E-value: 7.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILP 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGlTVEElcYFgRHPhkkLLSKHTQEDHDMVEWALEATGM-IELKDRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:COG4619 81 QEPALWGG-TVRD--NL-PFP---FQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-227 |
1.72e-47 |
|
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: 157.34 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARL-----MAPKSGTVLLEGKDIH--RQPSKEVAKKLAI 81
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYdlDVDVLELRRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPqAPEGLTVEELCYFGRHPHKKLLSKhtqEDHDMVEWALEATGMI-ELKDRtLDA--LSGGQRQRAWISMALAQGT 158
Cdd:cd03260 86 VFQKP-NPFPGSIYDNVAYGLRLHGIKLKE---ELDERVEEALRKAALWdEVKDR-LHAlgLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLNRDHgrTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-240 |
1.11e-46 |
|
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: 156.84 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPS---KEVAKKLAILPQSP--QAPEgLT 93
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklKDLRKKVGLVFQFPehQLFE-ET 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMIE-LKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDI 172
Cdd:TIGR04521 100 VYKDIAFG--PKNLGLSE--EEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 173 SHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLIsVLD-GKIYNAGTPEDVFTQPFFREVFGLE 240
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVI-VMHkGKIVLDGTPREVFSDVDELEKIGLD 243
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-231 |
1.16e-45 |
|
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: 153.66 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-LAIL 82
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEELCYFGRHPHKK--LLS---------KHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWIS 151
Cdd:COG0411 85 FQNPRLFPELTVLENVLVAAHARLGrgLLAallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYlISVLD-GKIYNAGTPEDVFTQ 230
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR-IVVLDfGRVIAEGTPAEVRAD 243
|
.
gi 489326441 231 P 231
Cdd:COG0411 244 P 244
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-218 |
2.46e-45 |
|
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: 151.52 E-value: 2.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvaKKLAILPQSP 86
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAPEGLTVEELCYFGRhphkKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:cd03259 82 ALFPHLTVAENIAFGL----KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489326441 167 TTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-217 |
2.52e-45 |
|
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: 149.70 E-value: 2.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 8 QLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQspq 87
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 apegltveelcyfgrhphkkllskhtqedhdmvewaleatgmielkdrtldaLSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489326441 168 TYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGK 217
Cdd:cd00267 109 SGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-231 |
2.19e-44 |
|
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: 152.13 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS---TV-IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPK---SGTVLLEGKDIHRQPSKEV- 75
Cdd:COG0444 2 LEVRNLKVYFPTrrgVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 76 ---AKKLAILPQSPQA---P---------EGLTVeelcyfgrhpHKKLlSKhtQEDHDMVEWALEATGmIELKDRTLDA- 139
Cdd:COG0444 82 kirGREIQMIFQDPMTslnPvmtvgdqiaEPLRI----------HGGL-SK--AEARERAIELLERVG-LPDPERRLDRy 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 140 ---LSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYAD-----YLi 211
Cdd:COG0444 148 pheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADrvavmYA- 226
|
250 260
....*....|....*....|
gi 489326441 212 svldGKIYNAGTPEDVFTQP 231
Cdd:COG0444 227 ----GRIVEEGPVEELFENP 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
8.93e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 151.40 E-value: 8.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvaKKLA 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQS----PQapegLTVEELCYFGrhPHKKLLSKHTQEDhdMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQ 156
Cdd:COG3842 81 MVFQDyalfPH----LTVAENVAFG--LRMRGVPKAEIRA--RVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLIsVL-DGKIYNAGTPEDVFTQP 231
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIA-VMnDGRIEQVGTPEEIYERP 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-227 |
9.62e-44 |
|
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: 147.58 E-value: 9.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-LAIL 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEE-L---CYFGRHPHKKllskhtqedhDMVEWALEatgMI-ELKDRtLDA----LSGGQRQRAWISMA 153
Cdd:cd03224 81 PEGRRIFPELTVEEnLllgAYARRRAKRK----------ARLERVYE---LFpRLKER-RKQlagtLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 154 LAQGTDLLLLDEPTtyLDISHQI--EVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLIsVLD-GKIYNAGTPEDV 227
Cdd:cd03224 147 LMSRPKLLLLDEPS--EGLAPKIveEIFEAIREL-RDEGVTILLVEQNARFALEIADRAY-VLErGRVVLEGTAAEL 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-231 |
2.48e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 147.75 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLM-----APKSGTVLLEGKDIHRQPSKEV 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 76 AKKLAILPQSPQAPEGLTVEELCYFGrhPHKKLLSKHTQEDHDMVEWALEATGMI-ELKDRtLDA----LSGGQRQRAWI 150
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWdEVKDR-LDApagkLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 151 SMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
.
gi 489326441 231 P 231
Cdd:PRK14247 236 P 236
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-238 |
5.67e-43 |
|
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: 146.29 E-value: 5.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE---VAKKL 79
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEE---LCYFGRHPH-KKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALA 155
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLEnvlHGRLGYKPTwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 156 QGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVfTQPFFRE 235
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-DDEVLRH 240
|
...
gi 489326441 236 VFG 238
Cdd:TIGR02315 241 IYG 243
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-226 |
7.27e-43 |
|
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: 145.59 E-value: 7.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPsKEVAKKLAILPQS 85
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEELCYFgrhpHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDE 165
Cdd:cd03265 82 LSVDDELTGWENLYI----HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 166 PTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYlISVLD-GKIYNAGTPED 226
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDR-VAIIDhGRIIAEGTPEE 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-227 |
8.22e-43 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 145.51 E-value: 8.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-LAil 82
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 pqspQAPEG------LTVEE-LcyfgrhphkkLLSKHTQEDHDMVEWALEatgMI-----ELKDRtLD----ALSGGQRQ 146
Cdd:COG0410 82 ----YVPEGrrifpsLTVEEnL----------LLGAYARRDRAEVRADLE---RVyelfpRLKER-RRqragTLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 147 RAWISMALAQGTDLLLLDEPTtyLDISHQI--EVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLIsVLD-GKIYNAGT 223
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPS--LGLAPLIveEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAY-VLErGRIVLEGT 219
|
....
gi 489326441 224 PEDV 227
Cdd:COG0410 220 AAEL 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-231 |
1.41e-42 |
|
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: 145.07 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI-----HRQPSKEVAKKLAI 81
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlppHKRPVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQspqapegLTVEELCYFGRhphkKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:cd03300 84 FPH-------LTVFENIAFGL----RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYlISVLD-GKIYNAGTPEDVFTQP 231
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDR-IAVMNkGKIQQIGTPEEIYEEP 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-228 |
6.93e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.77 E-value: 6.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 3 KLAADQLTLSYD--STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLA 80
Cdd:PRK13635 5 IIRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPQAP-EGLTVEELCYFGrhphkklLSKHTQEDHDMVE---WALEATGMIELKDRTLDALSGGQRQRAWISMALAQ 156
Cdd:PRK13635 85 MVFQNPDNQfVGATVQDDVAFG-------LENIGVPREEMVErvdQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVF 228
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-231 |
4.55e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 141.71 E-value: 4.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 3 KLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARL--MAPK---SGTVLLEGKDIHrQPSKEVA- 76
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIY-DPDVDVVe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 77 --KKLAILPQSPQaPEGLTVEE-----LCYFGRHPHKKLlskhtqedHDMVEWALEATGMI-ELKDRtLD----ALSGGQ 144
Cdd:COG1117 90 lrRRVGMVFQKPN-PFPKSIYDnvaygLRLHGIKSKSEL--------DEIVEESLRKAALWdEVKDR-LKksalGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 145 RQRAWISMALAQGTDLLLLDEPTTYLD-IS-HQIEvlELLKKLNRDHgrTVVMVLHDLNQAAQYADYLISVLDGKIYNAG 222
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDpIStAKIE--ELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
....*....
gi 489326441 223 TPEDVFTQP 231
Cdd:COG1117 236 PTEQIFTNP 244
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-236 |
6.14e-41 |
|
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: 142.01 E-value: 6.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEV----AK 77
Cdd:cd03294 23 KGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 78 KLAILPQSpqapegltveelcyFGRHPHKKLLSKHT----------QEDHDMVEWALEATGMIELKDRTLDALSGGQRQR 147
Cdd:cd03294 103 KISMVFQS--------------FALLPHRTVLENVAfglevqgvprAEREERAAEALELVGLEGWEHKYPDELSGGMQQR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 148 AWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:cd03294 169 VGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
250
....*....|....*.
gi 489326441 228 FTQP-------FFREV 236
Cdd:cd03294 249 LTNPandyvreFFRGV 264
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-199 |
8.15e-41 |
|
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: 139.54 E-value: 8.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSkEVAKKLAILP 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYFgrhpHKKLlsKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:COG4133 82 HADGLKPELTVRENLRF----WAAL--YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHD 199
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-217 |
1.64e-40 |
|
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: 138.09 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI--HRQPSKEVAKKLAILPQ 84
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SPQAPEGLTVEELCYFGrhphkkllskhtqedhdmvewaleatgmielkdrtldaLSGGQRQRAWISMALAQGTDLLLLD 164
Cdd:cd03229 84 DFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489326441 165 EPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGK 217
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-226 |
2.40e-40 |
|
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: 146.44 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAIL 82
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGlTVEE-LcyfgrhphkkLLSKHTQEDHDMVEwALEATGMIELKDRT---LDA--------LSGGQRQRAWI 150
Cdd:COG4988 417 PQNPYLFAG-TIREnL----------RLGRPDASDEELEA-ALEAAGLDEFVAALpdgLDTplgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 151 SMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRdhGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPED 226
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
5.60e-40 |
|
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: 135.85 E-value: 5.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGLTVEELC 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 99 YFGRHPhkKLLSKHTQEDHdmVEWALEATGMIELKDRTLDA----LSGGQRQRAWISMALAQGTDLLLLDEPTT 168
Cdd:pfam00005 81 RLGLLL--KGLSKREKDAR--AEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-228 |
5.84e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 139.50 E-value: 5.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 14 DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAP-EGL 92
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQfVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 93 TVEELCYFGRHPHkkllSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDI 172
Cdd:PRK13648 100 IVKYDVAFGLENH----AVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 173 SHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVF 228
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-238 |
5.96e-39 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 139.22 E-value: 5.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 15 STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVA----KKLAILPQSPQAPE 90
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELRevrrKKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 91 GLTVEELCYFGrhphKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYL 170
Cdd:TIGR01186 85 HMTILQNTSLG----PELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 171 DISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP---FFREVFG 238
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPaneYVEEFIG 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-218 |
9.66e-39 |
|
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: 134.31 E-value: 9.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRqpsKEVAKKLAILPQ 84
Cdd:cd03226 2 IENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SPQAP-EGLTVEELCYFGrhphkkllSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:cd03226 79 DVDYQlFTDSVREELLLG--------LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-224 |
1.21e-38 |
|
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: 134.55 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPsKEVAKKLAILPQSPQAPEG 91
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 92 LTVEELCYFgrhpHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:cd03263 90 LTVREHLRF----YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489326441 172 ISHQIEVLELLKKLNRdhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTP 224
Cdd:cd03263 166 PASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-231 |
1.22e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.90 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvaKKLA 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQS----PQapegLTVEELCYFGrhphkkL-LSKHTQEDHD-MVEWALEATGMIELKDRTLDALSGGQRQRAWISMAL 154
Cdd:COG3839 79 MVFQSyalyPH----MTVYENIAFP------LkLRKVPKAEIDrRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 155 AQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYlISVL-DGKIYNAGTPEDVFTQP 231
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADR-IAVMnDGRIQQVGTPEELYDRP 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-238 |
2.10e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 134.35 E-value: 2.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQS 85
Cdd:cd03295 4 ENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEElcYFGRHPhkKLLSKHTQEDHDMVEWALEATGM--IELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:cd03295 84 IGLFPHMTVEE--NIALVP--KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP---FFREVFG 238
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPandFVAEFVG 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-231 |
2.18e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.59 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSK--EVAKKLA 80
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPQ----APeglTVEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQ 156
Cdd:PRK13639 82 IVFQNPDdqlfAP---TVEEDVAFG--PLNLGLSK--EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-231 |
3.34e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.97 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHrQPSKEVAK---KLA 80
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKlrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQS----PQapegLTVEELCYFG-RHPHKklLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALA 155
Cdd:COG1126 81 MVFQQfnlfPH----LTVLENVTLApIKVKK--MSK--AEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 156 QGTDLLLLDEPTTYLD---IShqiEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:COG1126 153 MEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-239 |
4.59e-38 |
|
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: 133.67 E-value: 4.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSG-TVLLEGKDIHRQPSKEVAKKLAIL 82
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQA--PEGLTVEELC---YF---GRHPHkkllskHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMAL 154
Cdd:COG1119 84 SPALQLrfPRDETVLDVVlsgFFdsiGLYRE------PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 155 AQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFR 234
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLS 237
|
....*
gi 489326441 235 EVFGL 239
Cdd:COG1119 238 EAFGL 242
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-231 |
1.14e-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: 132.46 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvaKKLAILPQSPQAPEGLTVEELC 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 99 YFGRHphKKLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEV 178
Cdd:cd03299 93 AYGLK--KRKVDK--KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489326441 179 LELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-218 |
2.04e-37 |
|
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: 131.16 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGkITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKeVAKKLAILP 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEE----LCYFGRHPHKKLlskhtqedHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:cd03264 79 QEFGVYPNFTVREfldyIAWLKGIPSKEV--------KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
9-225 |
2.71e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 132.55 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSP- 86
Cdd:PRK13647 10 LHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 -QAPEGlTVEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDE 165
Cdd:PRK13647 90 dQVFSS-TVWDDVAFG--PVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 166 PTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPE 225
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-208 |
2.83e-37 |
|
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: 131.05 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS----TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGkdihrQPSKEVAKKL 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYFGRhphkKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYAD 208
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLAD 200
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-208 |
3.53e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 131.75 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYDS----TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRqPSKEVa 76
Cdd:COG1116 5 APALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PGPDR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 77 kklAILPQSPQAPEGLTVEELCYFGRhphkKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQ 156
Cdd:COG1116 83 ---GVVFQEPALLPWLTVLDNVALGL----ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 157 GTDLLLLDEPTTYLD----ISHQIEVLELLkklnRDHGRTVVMVLHDLNQAAQYAD 208
Cdd:COG1116 156 DPEVLLMDEPFGALDaltrERLQDELLRLW----QETGKTVLFVTHDVDEAVFLAD 207
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-257 |
9.10e-37 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 130.35 E-value: 9.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 21 GVDLKIEEGKITALIGANGCGKSTILKSLARLmAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGLTVEElcYF 100
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQ--YL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 101 GRHPHKKLlskhtqeDHDMVEWALEA-TGMIELKD---RTLDALSGGQRQRAWISMALAQ-------GTDLLLLDEPTTY 169
Cdd:COG4138 91 ALHQPAGA-------SSEAVEQLLAQlAEALGLEDklsRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 170 LDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLEccIMRSPID 249
Cdd:COG4138 164 LDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVK--FRRLEVE 240
|
....*...
gi 489326441 250 QKPMCLPT 257
Cdd:COG4138 241 GHRWLIPT 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-229 |
1.11e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSP 86
Cdd:PRK13632 13 VSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAP-EGLTVEELCYFG----RHPHKKLlskhtqedHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:PRK13632 93 DNQfIGATVEDDIAFGlenkKVPPKKM--------KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVFT 229
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-231 |
3.32e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 129.19 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLM-----APKSGTVLLEGKDIHRQPSK--EVAKKLAI 81
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDpiEVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPQAPEGLTVEELCYFGRHPHKklLSKHTQEDHDMVEWALEATGMI-ELKDRTLD---ALSGGQRQRAWISMALAQG 157
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNG--LVKSKKELDERVEWALKKAALWdEVKDRLNDypsNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 158 TDLLLLDEPTTYLDISHQIEVLELLKKLNRDHgrTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-216 |
4.02e-36 |
|
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: 126.34 E-value: 4.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDST--VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQ 84
Cdd:cd03228 4 KNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SPQAPEGlTVEE-LcyfgrhphkkllskhtqedhdmvewaleatgmielkdrtldaLSGGQRQRAWISMALAQGTDLLLL 163
Cdd:cd03228 84 DPFLFSG-TIREnI------------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLnrDHGRTVVMVLHDLNqAAQYADYLIsVLDG 216
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAHRLS-TIRDADRII-VLDD 169
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-230 |
5.10e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 129.44 E-value: 5.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 15 STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSK-EVAKKLAILPQSPQAPEGLT 93
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 -VEELCYFGrhPHKklLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDI 172
Cdd:PRK13633 102 iVEEDVAFG--PEN--LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 173 SHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-231 |
7.50e-36 |
|
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: 133.66 E-value: 7.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS----TVIIDGVDLKIEEGKITALIGANGCGKS----TILKSLARLMAPKSGTVLLEGKDIHRQPSKEV 75
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 76 AK----KLAILPQSP------------QAPEGLTVeelcyfgrhpHKKLLSKHTQEDhdMVEWaLEATGMIELKDRtLDA 139
Cdd:COG4172 87 RRirgnRIAMIFQEPmtslnplhtigkQIAEVLRL----------HRGLSGAAARAR--ALEL-LERVGIPDPERR-LDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 140 ----LSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLD 215
Cdd:COG4172 153 yphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|....*.
gi 489326441 216 GKIYNAGTPEDVFTQP 231
Cdd:COG4172 233 GEIVEQGPTAELFAAP 248
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-227 |
8.27e-36 |
|
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: 134.96 E-value: 8.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:COG2274 472 GDIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGlTVEE-LCYFGRHPhkkllskhTQEDhdmVEWALEATGMIELKDR------TL-----DALSGGQRQR 147
Cdd:COG2274 552 GVVLQDVFLFSG-TIREnITLGDPDA--------TDEE---IIEAARLAGLHDFIEAlpmgydTVvgeggSNLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 148 AWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLnrDHGRTVVMVLHDLnQAAQYADYLIsVLD-GKIYNAGTPED 226
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRL-STIRLADRII-VLDkGRIVEDGTHEE 695
|
.
gi 489326441 227 V 227
Cdd:COG2274 696 L 696
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-239 |
2.10e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.50 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKD--IHRQPSKevaKKLAI 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlfTNLPPRE---RRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPQAPEGLTVEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFG--LRVRPPSK--AEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 162 LLDEPTTYLDIS--HQIEvlELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGL 239
Cdd:COG1118 156 LLDEPFGALDAKvrKELR--RWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARF 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-235 |
2.71e-35 |
|
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: 132.58 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYD--STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAI 81
Cdd:COG4987 334 LELEDVSFRYPgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPQAPEGlTVEE-LcyfgrhphkkLLSKHTQEDHDMVEwALEATGMIELKDRT---LDA--------LSGGQRQRAW 149
Cdd:COG4987 414 VPQRPHLFDT-TLREnL----------RLARPDATDEELWA-ALERVGLGDWLAALpdgLDTwlgeggrrLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 150 ISMALAQGTDLLLLDEPTTYLDISHQIEVLELLkkLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPED-VF 228
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEElLA 558
|
....*..
gi 489326441 229 TQPFFRE 235
Cdd:COG4987 559 QNGRYRQ 565
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-240 |
6.33e-35 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 124.96 E-value: 6.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 24 LKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKdihrqPSKEVAKKLAILPQSPQ----APegLTVEELCY 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRHEfawdFP--ISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 100 FGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVL 179
Cdd:TIGR03771 74 SGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 180 ELLKKLNRDhGRTVVMVLHDLNQAAQYADYLIsVLDGKIYNAGTPEDVFTQPFFREVFGLE 240
Cdd:TIGR03771 154 ELFIELAGA-GTAILMTTHDLAQAMATCDRVV-LLNGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-229 |
6.80e-35 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 126.15 E-value: 6.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDS--TVIIDGVdLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGkdihrQPSKEVAKK--L 79
Cdd:PRK15056 7 IVVNDVTVTWRNghTALRDAS-FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG-----QPTRQALQKnlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEG--LTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQG 157
Cdd:PRK15056 81 AYVPQSEEVDWSfpVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 158 TDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVlDGKIYNAGTPEDVFT 229
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFT 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-234 |
1.40e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.03 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI-----HRQPSKEVAKKLAILP 83
Cdd:PRK11607 25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvppYQRPINMMFQSYALFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QspqapegLTVEELCYFGRHPHKklLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:PRK11607 105 H-------MTVEQNIAFGLKQDK--LPK--AEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 164 DEPTTYLDIS----HQIEVLELLKKLnrdhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFR 234
Cdd:PRK11607 174 DEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-222 |
2.23e-34 |
|
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: 123.25 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYD----STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPsKEVAKKL 79
Cdd:cd03266 2 ITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTV-EELCYFGRhphkkLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGT 158
Cdd:cd03266 81 GFVSDSTGLYDRLTArENLEYFAG-----LYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAG 222
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-240 |
2.99e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.91 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSY-DSTV-IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKS---GTVLLEGKDIHRQPSKEVAKKLAI 81
Cdd:PRK13640 9 KHVSFTYpDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPQAP-EGLTVEELCYFGRH----PHKKLLSkhtqedhdMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQ 156
Cdd:PRK13640 89 VFQNPDNQfVGATVGDDVAFGLEnravPRPEMIK--------IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVFTQPFFREV 236
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEMLKE 239
|
....
gi 489326441 237 FGLE 240
Cdd:PRK13640 240 IGLD 243
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-231 |
4.10e-34 |
|
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: 123.22 E-value: 4.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 13 YDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE-----VAKKLAILPQspq 87
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfVFQHYALFRH--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 apegLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:cd03296 89 ----MTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 168 TYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-213 |
5.81e-34 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 128.56 E-value: 5.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAIL 82
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEELcyfgrhphkkLLSKHTQEDHDMVEwALEATGMIELkDRTLDA------------LSGGQRQRAWI 150
Cdd:TIGR02857 402 PQHPFLFAGTIAENI----------RLARPDASDAEIRE-ALERAGLDEF-VAALPQgldtpigeggagLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 151 SMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRdhGRTVVMVLHDLNQAAQyADYLISV 213
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-239 |
1.61e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 123.21 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPS----KEVAKKLAILPQSPQA---PEglTV 94
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKPLRKKVGIVFQFPEHqlfEE--TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMIE-LKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDIS 173
Cdd:PRK13634 104 EKDICFG--PMNFGVSE--EDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 174 HQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGL 239
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGL 245
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-227 |
2.26e-33 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 121.09 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-LAIL 82
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEwALEatgmiELKDRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFP-VLK-----EMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLIsVLD-GKIYNAGTPEDV 227
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYY-VMErGRVVASGAGDEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-222 |
3.02e-33 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 120.29 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 23 DLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI-HRQPSkevAKKLAILPQSPQAPEGLTVEELCYFG 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtAAPPA---DRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 102 RHPHKKLlskhTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLEL 181
Cdd:cd03298 95 LSPGLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489326441 182 LKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAG 222
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
4.98e-33 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 118.30 E-value: 4.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH-RQPSKEVAKKLAIL 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQspqapegltveelcyfgrhphkkllskhtqedhdmvewaleatgmielkdrtldaLSGGQRQRAWISMALAQGTDLLL 162
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYlISVL-DGKI 218
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADR-VTVLrDGRV 160
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-204 |
6.78e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.56 E-value: 6.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKdihrqpskevaKKLAILPQS 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEELCYFGRHPHKKLL-------SKHTQEDHDMVE-------------WALEA------TGM---IELKDRT 136
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEaeleeleAKLAEPDEDLERlaelqeefealggWEAEAraeeilSGLgfpEEDLDRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 137 LDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDIsHQIEVLE-LLKklNRDHgrTVVMVLHD---LNQAA 204
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLEeFLK--NYPG--TVLVVSHDryfLDRVA 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-218 |
6.85e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.39 E-value: 6.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK---KLAIL 82
Cdd:COG2884 5 ENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEE-----LCYFGRHPHkkllskhtqEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQG 157
Cdd:COG2884 85 FQDFRLLPDRTVYEnvalpLRVTGKSRK---------EIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 158 TDLLLLDEPTTYLDISHQIEVLELLKKLNRdHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-240 |
1.27e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.54 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 16 TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSK--EVAKKLAILPQSP--QAPEG 91
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQYPeyQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 92 lTVEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMI--ELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTY 169
Cdd:PRK13637 100 -TIEKDIAFG--PINLGLSE--EEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 170 LDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVftqpfFREVFGLE 240
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV-----FKEVETLE 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-218 |
1.96e-32 |
|
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: 118.02 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI--HRQPSKEVAKKLAILP 83
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYFGrhPHK-KLLSKHTQEDHDMVewALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:cd03262 83 QQFNLFPHLTVLENITLA--PIKvKGMSKAEAEERALE--LLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-226 |
1.37e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.20 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYD-STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLA 80
Cdd:COG1132 338 GEIEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPQapegL---TVEE-LCYfGRhphkkllSKHTQEDhdmVEWALEATG---MIELKDRTLDA--------LSGGQR 145
Cdd:COG1132 418 VVPQDTF----LfsgTIREnIRY-GR-------PDATDEE---VEEAAKAAQaheFIEALPDGYDTvvgergvnLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 146 QRawISMA--LAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRdhGRTVVMVLHDLNQAAQyADYLIsVLD-GKIYNAG 222
Cdd:COG1132 483 QR--IAIAraLLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRIL-VLDdGRIVEQG 556
|
....
gi 489326441 223 TPED 226
Cdd:COG1132 557 THEE 560
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-235 |
1.61e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.54 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 21 GVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPS----KEVAKKLAILPQSPQA---PEglT 93
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPESqlfEE--T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYFGrhPHKKLLSKHTQEdhdmvEWALEATGMI----ELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTY 169
Cdd:PRK13649 103 VLKDVAFG--PQNFGVSQEEAE-----ALAREKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 170 LDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFRE 235
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-218 |
1.64e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.11 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 17 VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQ---APeGLT 93
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMmgtAP-SMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEE---LCYfGRHPHKKLLSKHTQEDHDMVEWALEATGMiELKDRtLDA----LSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:COG1101 99 IEEnlaLAY-RRGKRRGLRRGLTKKRRELFRELLATLGL-GLENR-LDTkvglLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489326441 167 TTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-200 |
2.09e-31 |
|
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: 121.31 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAIL 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQApEGLTVEELCYFGRhphkkllSKHTQEDhdmVEWALEATGMIELKDRTLD-----------ALSGGQRQRAWIS 151
Cdd:TIGR02868 415 AQDAHL-FDTTVRENLRLAR-------PDATDEE---LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLkkLNRDHGRTVVMVLHDL 200
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
9-231 |
2.47e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 117.21 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTV-IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQ 87
Cdd:PRK13652 9 LCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 ----APeglTVEELCYFGrhPHKKLLSKHTQEDHdmVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:PRK13652 89 dqifSP---TVEQDIAFG--PINLGLDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
2.77e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.89 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvAKKL--AI 81
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAgiAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPQ-APEgLTVEELCYFGRHPHKKLLSKHTQedhdMVEWALEATGMIELK---DRTLDALSGGQRQRAWISMALAQG 157
Cdd:COG1129 84 IHQELNlVPN-LSVAENIFLGREPRRGGLIDWRA----MRRRARELLARLGLDidpDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 158 TDLLLLDEPTTYLDiSHQIEVL-ELLKKLnRDHGRTVVMVLHDLNQAAQYADYlISVL-DGKI 218
Cdd:COG1129 159 ARVLILDEPTASLT-EREVERLfRIIRRL-KAQGVAIIYISHRLDEVFEIADR-VTVLrDGRL 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-237 |
4.12e-31 |
|
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: 115.33 E-value: 4.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-LAIL 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEE--LCYFGRHPHKKllskhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDL 160
Cdd:cd03218 81 PQEASIFRKLTVEEniLAVLEIRGLSK------KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 161 LLLDEPTTYLD-ISHQiEVLELLKKLnRDHGRTVVMVLHDLNQAAQYAD--YLISvlDGKIYNAGTPEDVFTQPFFREVF 237
Cdd:cd03218 155 LLLDEPFAGVDpIAVQ-DIQKIIKIL-KDRGIGVLITDHNVRETLSITDraYIIY--EGKVLAEGTPEEIAANELVRKVY 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
14-230 |
4.29e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.49 E-value: 4.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 14 DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGK--DIHRQPSKEVAKKLAILPQSPQAPE- 90
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPDNQLf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 91 GLTVEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYL 170
Cdd:PRK13636 97 SASVYQDVSFG--AVNLKLPE--DEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 171 DISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-231 |
5.16e-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: 120.17 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 20 DGVDLKIEEGKITALIGANGCGKSTILKSLARLMaPKSGTVLLEGKDIHRQPSKE---VAKKLAILPQSPQA---PEgLT 93
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPFGslsPR-MT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYFGRHPHKKLLSKhtQEDHDMVEWALEATGM-IELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDI 172
Cdd:COG4172 381 VGQIIAEGLRVHGPGLSA--AERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 173 SHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLIsVL-DGKIYNAGTPEDVFTQP 231
Cdd:COG4172 459 SVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVM-VMkDGKVVEQGPTEQVFDAP 517
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-218 |
5.32e-31 |
|
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: 114.27 E-value: 5.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE-----VAKKLAI 81
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQspqapegLTVEELCYFGrhphkkLLSKHTQEDH--DMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:cd03301 84 YPH-------MTVYDNIAFG------LKLRKVPKDEidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-230 |
1.94e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 119.59 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:TIGR03375 462 GEIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYFGRHPhkkllskhtqEDHDMVEwALEATGMIELKDRT---LD--------ALSGGQRQRA 148
Cdd:TIGR03375 542 GYVPQDPRLFYGTLRDNIALGAPYA----------DDEEILR-AAELAGVTEFVRRHpdgLDmqigergrSLSGGQRQAV 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 149 WISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNrdHGRTVVMVLHDLnQAAQYADYLISVLDGKIYNAGTPEDVF 228
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVL 687
|
..
gi 489326441 229 TQ 230
Cdd:TIGR03375 688 EA 689
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-231 |
2.64e-30 |
|
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: 113.06 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 15 STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEV---AKKLAILPQspqapeg 91
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQ------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 92 ltveelcyfgrhpHKKLLSKHT----------------QEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALA 155
Cdd:cd03258 90 -------------HFNLLSSRTvfenvalpleiagvpkAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 156 QGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYlISVLD-GKIYNAGTPEDVFTQP 231
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDR-VAVMEkGEVVEEGTVEEVFANP 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-235 |
7.25e-30 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 111.79 E-value: 7.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQ-PSKEVA-KKLAILPQspqapegLTVEE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDRMVVfQNYSLLPW-------LTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 97 LCYFGRHPHKKLLSKHTQEDhdMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQI 176
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRA--IVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 177 EVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV-FTQPFFRE 235
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDRL 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-231 |
7.60e-30 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 112.49 E-value: 7.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 3 KLAADQLTLSYDStVIIDGVDLKIEEGKITALIGANGCGKStiLKSLARL-MAPK-----SGTVLLEGKDIHrqPSKEVA 76
Cdd:PRK10418 4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgILPAgvrqtAGRVLLDGKPVA--PCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 77 KKLAILPQSPQApeglTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMiELKDRTLDA----LSGGQRQRAWISM 152
Cdd:PRK10418 79 RKIATIMQNPRS----AFNPLHTMHTHARETCLALGKPADDATLTAALEAVGL-ENAARVLKLypfeMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 153 ALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-218 |
9.26e-30 |
|
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: 111.66 E-value: 9.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 13 YDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGL 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 93 TVEELCYFGRHPHKkLLSKHTQEDHDMVEWALEATgmiELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDI 172
Cdd:cd03267 111 PVIDSFYLLAAIYD-LPPARFKKRLDELSELLDLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489326441 173 SHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-236 |
9.43e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.77 E-value: 9.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSY-DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHrQPSK--EVAKKLAILP 83
Cdd:PRK13644 5 ENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-DFSKlqGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAP-EGLTVEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:PRK13644 84 QNPETQfVGRTVEEDLAFG--PENLCLPP--IEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQaAQYADYLISVLDGKIYNAGTPEDVFTQPFFREV 236
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-231 |
1.71e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 20 DGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVA---KKLAILPQSPQA---PEgLT 93
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQDPYAslnPR-MT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYFGRHPHkKLLSKHTQEdhDMVEWALEATGM-IELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDI 172
Cdd:COG4608 114 VGDIIAEPLRIH-GLASKAERR--ERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 173 SHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYAD-----YLisvldGKIYNAGTPEDVFTQP 231
Cdd:COG4608 191 SIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDrvavmYL-----GKIVEIAPRDELYARP 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-233 |
3.20e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.75 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTV----LLEGKDIHRQPSKEVAKKLAILPQSPQAP--EGLTVE 95
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPVRKKVGVVFQFPESQlfEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 96 ELCyFGrhPHKKLLSKhtQEDHDMVEWALEATGMI-ELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISH 174
Cdd:PRK13643 105 DVA-FG--PQNFGIPK--EKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 175 QIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFF 233
Cdd:PRK13643 180 RIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDF 237
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-218 |
3.26e-29 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 109.95 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 23 DLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvaKKLAILPQSPQAPEGLTVEELCYFGR 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 103 HPHKKLlskhTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELL 182
Cdd:TIGR01277 96 HPGLKL----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 489326441 183 KKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-231 |
3.58e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.57 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH---------RQPSKEVAKKLAIL 82
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvderliRQEAGMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQspqapegLTVEELCYFGrhP-HKKLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:PRK09493 90 PH-------LTALENVMFG--PlRVRGASK--EEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-226 |
4.15e-29 |
|
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: 109.94 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGlTVEEL 97
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-TIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CYFGRHPhkkllskHTQED----------HDMVEwALEATGMIELKDRTLDaLSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:cd03249 97 IRYGKPD-------ATDEEveeaakkaniHDFIM-SLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 168 TYLDISHQIEVLELLKKLNRdhGRTVVMVLHDLNqAAQYADYLISVLDGKIYNAGTPED 226
Cdd:cd03249 168 SALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-228 |
7.25e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.59 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 8 QLTLSYDS---TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQ 84
Cdd:PRK13650 9 NLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SPQAP-EGLTVEELCYFGRH----PHKKLLSKhtqedhdmVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:PRK13650 89 NPDNQfVGATVEDDVAFGLEnkgiPHEEMKER--------VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAqYADYLISVLDGKIYNAGTPEDVF 228
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
1.27e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.57 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYD----STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIhRQPSKE-- 74
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADrg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 75 -VAKKLAILPQspqapegLTVEELCYFGRhphkKL--LSKHtqEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWIS 151
Cdd:COG4525 80 vVFQKDALLPW-------LNVLDNVAFGL----RLrgVPKA--ERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQA 203
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-230 |
1.29e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.52 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 23 DLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDiHRQ--PSKevaKKLAILPQSPQAPEGLTVEELCYF 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTtpPSR---RPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 101 GRHPHKKLlskhTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLE 180
Cdd:PRK10771 95 GLNPGLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489326441 181 LLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSG 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-231 |
2.20e-28 |
|
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: 110.28 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 34 LIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI-----HRQPSKEVAKKLAILPQspqapegLTVEELCYFGRhphkKL 108
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtnvppHLRHINMVFQSYALFPH-------MTVEENVAFGL----KM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 109 LSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRD 188
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489326441 189 HGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-230 |
2.22e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPS----KEVAKKLAILPQSPQAP--EGl 92
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVRKRIGMVFQFPESQlfED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 93 TVEELCYFGRHPHKKLLSKHTQEDHD-MVEWALEATGMielkDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEVKNYAHRlLMDLGFSRDVM----SQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 172 ISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-248 |
2.36e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.66 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 24 LKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVA----KKLAILPQSPQAPEGLTVEELCY 99
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 100 FGRhphkKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVL 179
Cdd:PRK10070 129 FGM----ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 180 ELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP-------FFR-----EVFGLECCIMRSP 247
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPandyvrtFFRgvdisQVFSAKDIARRTP 284
|
.
gi 489326441 248 I 248
Cdd:PRK10070 285 N 285
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
2.40e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.61 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTvLLEGkdihRQPSKEVAKKLAILP 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAG----TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQApegltveelcyfgrHPHKKL-------LSKHTQEDhdmVEWALEATGmieLKDRTLD---ALSGGQRQRAWISMA 153
Cdd:PRK11247 88 QDARL--------------LPWKKVidnvglgLKGQWRDA---ALQALAAVG---LADRANEwpaALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 154 LAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-231 |
3.03e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.81 E-value: 3.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 8 QLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE-----VAKKLAIL 82
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhvntVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQspqapegLTVEELCYFGrhphkkLLSKHTQEDhDMVEWALEATGMIELK---DRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:PRK09452 99 PH-------MTVFENVAFG------LRMQKTPAA-EITPRVMEALRMVQLEefaQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 160 LLLLDEPTTYLDI----SHQIEvlelLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK09452 165 VLLLDESLSALDYklrkQMQNE----LKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-253 |
4.55e-28 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 107.71 E-value: 4.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 26 IEEGKITALIGANGCGKSTILKSLARLMaPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGLTVEElcYFGRHPH 105
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQ--YLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 106 KKLlskHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQ-------GTDLLLLDEPTTYLDISHQIEV 178
Cdd:PRK03695 96 DKT---RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 179 LELLKKLNRdHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLEccIMRSPIDQKPM 253
Cdd:PRK03695 173 DRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVN--FRRLDVEGHPM 244
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-220 |
7.95e-28 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 106.28 E-value: 7.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYD----STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK-- 77
Cdd:TIGR02211 2 LKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 78 --KLAILPQSPQAPEGLTVEELCYFgrhphKKLLSKHTQEDHDMVEWA-LEATGMIELKDRTLDALSGGQRQRAWISMAL 154
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAM-----PLLIGKKSVKEAKERAYEmLEKVGLEHRINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 155 AQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLnQAAQYADYLISVLDGKIYN 220
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL-ELAKKLDRVLEMKDGQLFN 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-231 |
9.59e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 108.63 E-value: 9.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDS----TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVA---KKL 79
Cdd:COG1135 5 ENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQspqapegltveelcyfgrhpHKKLLSKHTQEDHdmVEWALEATGM---------------IELKDRtLDA----L 140
Cdd:COG1135 85 GMIFQ--------------------HFNLLSSRTVAEN--VALPLEIAGVpkaeirkrvaellelVGLSDK-ADAypsqL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 141 SGGQRQRAWISMALAQGTDLLLLDEPTTYLD--ISHQIevLELLKKLNRDHGRTVVMVLHDLNQAAQYADYlISVLD-GK 217
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDpeTTRSI--LDLLKDINRELGLTIVLITHEMDVVRRICDR-VAVLEnGR 218
|
250
....*....|....
gi 489326441 218 IYNAGTPEDVFTQP 231
Cdd:COG1135 219 IVEQGPVLDVFANP 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-218 |
2.77e-27 |
|
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: 104.61 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 8 QLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIhrQPSKEVAKKLAILPQSPQ 87
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 APEGLTVEElcyfgrhpHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:cd03268 83 FYPNLTARE--------NLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489326441 168 TYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03268 155 NGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-231 |
3.01e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.90 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAAD-----QLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMA------PKSGTVLLEGKDIHRQ 70
Cdd:PRK14246 4 GKSAEDvfnisRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 71 PSKEVAKKLAILPQSPQAPEGLTV-EELCYfgrhPHKKLLSKHTQEDHDMVEWALEATGMI-ELKDR---TLDALSGGQR 145
Cdd:PRK14246 84 DAIKLRKEVGMVFQQPNPFPHLSIyDNIAY----PLKSHGIKEKREIKKIVEECLRKVGLWkEVYDRlnsPASQLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 146 QRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPE 225
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237
|
....*.
gi 489326441 226 DVFTQP 231
Cdd:PRK14246 238 EIFTSP 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-235 |
3.38e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.63 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARL--MAPK---SGTVLLEGKDIH--RQPSKEVA 76
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYspRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 77 KKLAILPQSPQaPEGLTVEELCYFGRhphkKLLSKHTQEDHD-MVEWALEATGMI-ELKDRTLD---ALSGGQRQRAWIS 151
Cdd:PRK14239 86 KEIGMVFQQPN-PFPMSIYENVVYGL----RLKGIKDKQVLDeAVEKSLKGASIWdEVKDRLHDsalGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 152 MALAQGTDLLLLDEPTTYLD-ISH-QIEvlELLKKLNRDHgrTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFT 229
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDpISAgKIE--ETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
....*.
gi 489326441 230 QPFFRE 235
Cdd:PRK14239 237 NPKHKE 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-218 |
6.15e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.96 E-value: 6.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRqpskEVAKKLAILp 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 qspqaPE--GL----TVEE-LCYFGRhphKKLLSKHtQEDHDMVEWaLEATGMIELKDRTLDALSGGQRQRAWISMALAQ 156
Cdd:COG4152 77 -----PEerGLypkmKVGEqLVYLAR---LKGLSKA-EAKRRADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 157 GTDLLLLDEPTTYLD-ISHQIeVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLI------SVLDGKI 218
Cdd:COG4152 147 DPELLILDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIViinkgrKVLSGSV 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-237 |
8.39e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.71 E-value: 8.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvaKKLAILPQSP 86
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAPEGLTVEELCYFG-----RH--PHKKLLSKHTQEDHDMVEWAleatgmiELKDRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:PRK10851 84 ALFRHMTVFDNIAFGltvlpRRerPNAAAIKAKVTQLLEMVQLA-------HLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVF 237
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVL 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-222 |
1.10e-26 |
|
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: 103.13 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIhrqpSKEVAKKLAILP 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSpqapEGL-----TVEELCYFGRhpHKKLlsKHTQEDHDMVEWaLEATGMIELKDRTLDALSGGQRQRAWISMALAQGT 158
Cdd:cd03269 77 EE----RGLypkmkVIDQLVYLAQ--LKGL--KKEEARRRIDEW-LERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAG 222
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-218 |
1.37e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.01 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYD--STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHrQPSKEVAKKLAI 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS-DLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPqapegltveelcyfgrhphkkllskhtqedhdmveWALEATGMIELKDRtldaLSGGQRQRAWISMALAQGTDLL 161
Cdd:cd03247 80 LNQRP-----------------------------------YLFDTTLRNNLGRR----FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLnQAAQYADYLISVLDGKI 218
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHL-TGIEHMDKILFLENGKI 174
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-230 |
1.68e-26 |
|
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: 103.08 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQ 84
Cdd:cd03251 4 KNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SPQAPEGlTVEELCYFGRHphkkllskhtQEDHDMVEWALEATGMIELKDRTLDA-----------LSGGQRQRAWISMA 153
Cdd:cd03251 84 DVFLFND-TVAENIAYGRP----------GATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 154 LAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-218 |
2.09e-26 |
|
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: 102.49 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 8 QLTLSYDSTVI-IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK---KLAILP 83
Cdd:cd03292 5 NVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYFG----RHPHKKLLSKhtqedhdmVEWALEATGMiELKDRTLDA-LSGGQRQRAWISMALAQGT 158
Cdd:cd03292 85 QDFRLLPDRNVYENVAFAlevtGVPPREIRKR--------VPAALELVGL-SHKHRALPAeLSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLNrDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-237 |
2.84e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.80 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-L 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEE--LCYFGRHPhkklLSKHTQEDhdMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQG 157
Cdd:COG1137 81 GYLPQEASIFRKLTVEDniLAVLELRK----LSKKEREE--RLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 158 TDLLLLDEPTTYLD-IShQIEVLELLKKLnRDHGrtvVMVL---HDLNQAAQYAD--YLISvlDGKIYNAGTPEDVFTQP 231
Cdd:COG1137 155 PKFILLDEPFAGVDpIA-VADIQKIIRHL-KERG---IGVLitdHNVRETLGICDraYIIS--EGKVLAEGTPEEILNNP 227
|
....*.
gi 489326441 232 FFREVF 237
Cdd:COG1137 228 LVRKVY 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-231 |
4.25e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILP 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 -QSPQAPEGLTVEELCYFGRHPHKK--LLS------KHTQEDHDMVEWA---LEATGMIELKDRTLDALSGGQRQRAWIS 151
Cdd:PRK11300 86 fQHVRLFREMTVIENLLVAQHQQLKtgLFSgllktpAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-238 |
5.89e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.34 E-value: 5.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE-----VAKKLAILPQsp 86
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvgmVFQSYALYPH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 qapegLTVEELCYFGRhphkKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:PRK11000 90 -----LSVAENMSFGL----KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 167 TTYLD----ISHQIEVLELLKKLnrdhGRTVVMVLHDLNQAAQYADYlISVLD-GKIYNAGTPEDVFTQPFFREVFG 238
Cdd:PRK11000 161 LSNLDaalrVQMRIEISRLHKRL----GRTMIYVTHDQVEAMTLADK-IVVLDaGRVAQVGKPLELYHYPANRFVAG 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-218 |
6.31e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 102.58 E-value: 6.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH---RQPSKEVAKKLAILPQ-SPQA--PEg 91
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldRKQRRAFRRDVQLVFQdSPSAvnPR- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 92 LTVEELCyfgRHPHKKLLSKHTQEDHDMVEWALEATGM-IELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYL 170
Cdd:TIGR02769 105 MTVRQII---GEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489326441 171 DISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-231 |
7.68e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.03 E-value: 7.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI-HRQPSKE----VAKKLAILP 83
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVtHRSIQQRdicmVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QspqapegLTVEELCYFGRhphkKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:PRK11432 92 H-------MSLGENVGYGL----KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-231 |
1.04e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 101.65 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARlMAPKSGTVLLEGK----------------DIHRQ 70
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRveffnqniyerrvnlnRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 71 PSKeVAKKLAILPQSPQAPEGLTVEelcYFGRHPHKKLlskhtqedHDMVEWALEATGMI-ELKDR----TLDaLSGGQR 145
Cdd:PRK14258 90 VSM-VHPKPNLFPMSVYDNVAYGVK---IVGWRPKLEI--------DDIVESALKDADLWdEIKHKihksALD-LSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 146 QRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLD-----GKIYN 220
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVE 236
|
250
....*....|.
gi 489326441 221 AGTPEDVFTQP 231
Cdd:PRK14258 237 FGLTKKIFNSP 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-238 |
1.04e-25 |
|
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: 106.25 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKeVAKKLAILPQSPQAPEGLTVEELC 98
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-VRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 99 YFgrhpHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEV 178
Cdd:TIGR01257 1025 LF----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 179 LELLKKLNRdhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEdvftqpFFREVFG 238
Cdd:TIGR01257 1101 WDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL------FLKNCFG 1152
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-231 |
1.24e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.21 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPS----KEVAKKLAILPQSPQAP--EGl 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQFPEAQlfEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 93 TVEELCYFGrhPhKKLLSKHTQEDHDMVEWaLEATGMIE-LKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:PRK13641 102 TVLKDVEFG--P-KNFGFSEDEAKEKALKW-LKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 172 ISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
1.40e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.62 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDST-----VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLE----GKDIHRQPS-- 72
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 73 ----------KEVAKKLAILPQSPQAPegL---TVEELCYFGrhphKKLLSKHTQEDHDMVEWALEATGmieLKDRTLD- 138
Cdd:PRK13631 102 npyskkiknfKELRRRVSMVFQFPEYQ--LfkdTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMG---LDDSYLEr 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 139 ---ALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKlNRDHGRTVVMVLHDLNQAAQYADYLISVLD 215
Cdd:PRK13631 173 spfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
250
....*....|....*...
gi 489326441 216 GKIYNAGTPEDVFTQPFF 233
Cdd:PRK13631 252 GKILKTGTPYEIFTDQHI 269
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
1.66e-25 |
|
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: 99.97 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYDSTVI--IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYFGRHphkkllskhtQEDHDMVEwALEATGMIELKDRT---LD--------ALSGGQRQRA 148
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPL----------ADDERILR-AAELAGVTDFVNKHpngLDlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 149 WISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNqAAQYADYLISVLDGKI 218
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-218 |
1.91e-25 |
|
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: 99.68 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 20 DGVDLKIE---EGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEG-------KDIHRQPSKevaKKLAILPQSPQAP 89
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQ---RKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 90 EGLTVEELCYFGrhphkkLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTY 169
Cdd:cd03297 88 PHLNVRENLAFG------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489326441 170 LDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-198 |
2.27e-25 |
|
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: 100.04 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLM---APKSGTVLLEGKDIHRQpskEVAKKLAILPQSPQAPEGLTV 94
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPD---QFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELCYFG---RHPHKKLLSKHTQEDHDMVEWALeATGMIelKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:cd03234 99 RETLTYTailRLPRKSSDAIRKKRVEDVLLRDL-ALTRI--GGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180
....*....|....*....|....*..
gi 489326441 172 ISHQIEVLELLKKLNRdHGRTVVMVLH 198
Cdd:cd03234 176 SFTALNLVSTLSQLAR-RNRIVILTIH 201
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-204 |
2.36e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.48 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPK---SGTVLLEGKDIHRQPSKevAKKLA 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPQAPEGLTVEELCYFG--RHPHKkllskhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGT 158
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFAlpPTIGR-------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAA 204
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-240 |
2.52e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 102.19 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 20 DGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK---KLAILPQspqapegltvee 96
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrQIGMIFQ------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 97 lcyfgrhpHKKLLSKHTQEDHdmVEWALEATGM--IELKDRTL------------DA----LSGGQRQRAWISMALAQGT 158
Cdd:PRK11153 90 --------HFNLLSSRTVFDN--VALPLELAGTpkAEIKARVTellelvglsdkaDRypaqLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADyLISVLD-GKIYNAGTPEDVFTQP------ 231
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICD-RVAVIDaGRLVEQGTVSEVFSHPkhpltr 238
|
250
....*....|
gi 489326441 232 -FFREVFGLE 240
Cdd:PRK11153 239 eFIQSTLHLD 248
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-198 |
3.20e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 98.78 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTV------IIDGVDLKIEEGKITALIGANGCGKSTILKSLA-RLMAPK-SGTVLLEGKDIHRQpskEV 75
Cdd:cd03213 4 LSFRNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGvSGEVLINGRPLDKR---SF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 76 AKKLAILPQSPQAPEGLTVEELCYFGRHphkkllskhtqedhdmvewaleatgmielkdrtLDALSGGQRQRAWISMALA 155
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLMFAAK---------------------------------LRGLSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489326441 156 QGTDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLH 198
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-240 |
3.32e-25 |
|
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: 102.10 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEG-------KDIHRQPSKevaKKLAILPQSPQAPEGLTV 94
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGIFLPPHR---RRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELCYFGRHPHKKLLSKHTQEDhdMVEW-ALEAtgmieLKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDIS 173
Cdd:COG4148 95 RGNLLYGRKRAPRAERRISFDE--VVELlGIGH-----LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 174 HQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLIsVLD-GKIYNAGTPEDVFTQPFFREVFGLE 240
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVV-LLEqGRVVASGPLAEVLSRPDLLPLAGGE 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-209 |
3.49e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.24 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 3 KLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARL-----MAPKSGTVLLEGKDIHRQ---PSkE 74
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLYAPdvdPV-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 75 VAKKLAILPQSPQAPEGLTVEELCYFGRhphkklLSKHTQEDHDMVEWAL-EATGMIELKDRTLD---ALSGGQRQRAWI 150
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGAR------INGYKGDMDELVERSLrQAALWDEVKDKLKQsglSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 151 SMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHgrTVVMVLHDLNQAAQYADY 209
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDM 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-231 |
5.31e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 99.66 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 3 KLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAIL 82
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEeLCYFGRHPHK-----------KLLSKHTQEDHDMVEWALEATGMIE-LKDRTLDALSGGQRQRAWI 150
Cdd:PRK10619 85 NQLRLLRTRLTMV-FQHFNLWSHMtvlenvmeapiQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 151 SMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
.
gi 489326441 231 P 231
Cdd:PRK10619 243 P 243
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-218 |
7.11e-25 |
|
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: 98.66 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDST----VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK-- 77
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 78 --KLAILPQSPQAPEGLTVEE-----LCYFGRHphkkllskhtqEDHDMVEWALEATGmieLKDRtLDA----LSGGQRQ 146
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALEnvmlpLELAGRR-----------DARARARALLERVG---LGHR-LDHypaqLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 147 RAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKI 218
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-231 |
7.30e-25 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 99.49 E-value: 7.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 3 KLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI--------HRQPS-- 72
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgELVPAdr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 73 KEVAK---KLAILPQSpqapegltveelcyFGRHPHKKLLSK------HTQ--EDHDMVEWA---LEATGMIELKDRTLD 138
Cdd:COG4598 88 RQLQRirtRLGMVFQS--------------FNLWSHMTVLENvieapvHVLgrPKAEAIERAealLAKVGLADKRDAYPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 139 ALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:COG4598 154 HLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
250
....*....|...
gi 489326441 219 YNAGTPEDVFTQP 231
Cdd:COG4598 233 EEQGPPAEVFGNP 245
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-225 |
9.94e-25 |
|
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: 98.46 E-value: 9.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTV-IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQS 85
Cdd:cd03253 4 ENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 pqapeglTV-------EELCYfGRhphkkllskHTQEDHDMVEWALEA---TGMIELKD--------RTLdALSGGQRQR 147
Cdd:cd03253 84 -------TVlfndtigYNIRY-GR---------PDATDEEVIEAAKAAqihDKIMRFPDgydtivgeRGL-KLSGGEKQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 148 AWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRdhGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPE 225
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHE 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-212 |
1.91e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILP 83
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPqAPEGLTVEELCYF-----GRHPHKKLLSKhtqedhDMVEWALEATgmieLKDRTLDALSGGQRQRAWISMALAQGT 158
Cdd:PRK10247 88 QTP-TLFGDTVYDNLIFpwqirNQQPDPAIFLD------DLERFALPDT----ILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQaAQYADYLIS 212
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVIT 209
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-230 |
3.55e-24 |
|
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: 96.91 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 8 QLTLSYDSTV-IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSP 86
Cdd:cd03254 7 NVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAPEGlTVEELCYFGRhphkkllSKHTQEDhdmVEWALEATGMIELKDRTLDA-----------LSGGQRQRAWISMALA 155
Cdd:cd03254 87 FLFSG-TIMENIRLGR-------PNATDEE---VIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 156 QGTDLLLLDEPTTYLDISHQIEVLELLKKLNrdHGRTVVMVLHDLNqAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-225 |
1.09e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 96.62 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLM----APKSGTVLLeGKDIHRQP--SKEVAKKLA 80
Cdd:PRK09984 8 EKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGSHIELL-GRTVQREGrlARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ---ILPQSPQAPEGLTVEE---LCYFGRHPH-KKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMA 153
Cdd:PRK09984 87 ntgYIFQQFNLVNRLSVLEnvlIGALGSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 154 LAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPE 225
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-231 |
1.19e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.70 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAP-----KSGTVLLEGKDI-HRQPSKEVAK 77
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 78 KLAILPQSPQaPEGLTVEELCYFGRHPHKKLLSKhtqEDHDMVEWALEATGMIE-LKDRTLDA---LSGGQRQRAWISMA 153
Cdd:PRK14271 102 RVGMLFQRPN-PFPMSIMDNVLAGVRAHKLVPRK---EFRGVAQARLTEVGLWDaVKDRLSDSpfrLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 154 LAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-230 |
1.22e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 99.79 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:TIGR02203 329 GDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYfgrhphkkllSKHTQEDHDMVEWALEATGMIELKDRTLDA-----------LSGGQRQRA 148
Cdd:TIGR02203 409 ALVSQDVVLFNDTIANNIAY----------GRTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 149 WISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRdhGRTVVMVLHDLNqAAQYADYLISVLDGKIYNAGTPEDVF 228
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELL 555
|
..
gi 489326441 229 TQ 230
Cdd:TIGR02203 556 AR 557
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-233 |
1.35e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.88 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEG-------KDIHRQPSKevaKKLAILPQSPQAPEGLTV 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELCYFGRhphKKLLSKHTQEDHDMVewaLEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISH 174
Cdd:TIGR02142 93 RGNLRYGM---KRARPSERRISFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 175 QIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFF 233
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-231 |
2.18e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.20 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLegKDIHRQPSKEVAKKLA 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--GDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPQAPeGLTVEELCYFgrhPHKKLLS----------KHTQEDHDMVEWALEA-TGMIELKDRTLDALSGGQRQRAW 149
Cdd:PRK11264 79 LIRQLRQHV-GFVFQNFNLF---PHRTVLEniiegpvivkGEPKEEATARARELLAkVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 150 ISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHgRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFT 229
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
..
gi 489326441 230 QP 231
Cdd:PRK11264 234 DP 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-203 |
2.40e-23 |
|
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: 93.96 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQpSKEVAKKLAILP 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYFGRHPHkkllskhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRawisMALAQ----GTD 159
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIH--------GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRR----LALARlwlsRRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489326441 160 LLLLDEPTTYLDISHQievlELLKKLNRDH---GRTVVMVLH-DLNQA 203
Cdd:TIGR01189 148 LWILDEPTTALDKAGV----ALLAGLLRAHlarGGIVLLTTHqDLGLV 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-227 |
3.32e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.92 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPS------------------------KE 74
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekekvleklviqktrfkkikkiKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 75 VAKKLAILPQ--SPQAPEGlTVEELCYFGrhPHKKLLSKhtQEDHDMVEWALEATGM-IELKDRTLDALSGGQRQRAWIS 151
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQ-TIEKDIIFG--PVSMGVSK--EEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNrDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-203 |
4.61e-23 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 93.33 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSkEVAKKLAILP 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYFGRHPHkkllskhtqeDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWHADH----------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489326441 164 DEPTTYLDISHqievLELLKKLNRDH---GRTVVMVLH-DLNQA 203
Cdd:cd03231 150 DEPTTALDKAG----VARFAEAMAGHcarGGMVVLTTHqDLGLS 189
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-218 |
6.67e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.49 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 14 DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKklailpqspqapegLT 93
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ--------------LR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYFGRHPHkkLLSKHTQEDHDMV-------------EWALEATGMIELKDRT---LDALSGGQRQRAWISMALAQG 157
Cdd:PRK10535 85 REHFGFIFQRYH--LLSHLTAAQNVEVpavyaglerkqrlLRAQELLQRLGLEDRVeyqPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 158 TDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQyADYLISVLDGKI 218
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-218 |
8.10e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLeGKDIhrqpskevakKLAILP 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSpqapegltVEELcyfgrHPHKKLLskhtqeDHdMVEWaleATGMIELKDRTL---------------DALSGGQRQRA 148
Cdd:COG0488 385 QH--------QEEL-----DPDKTVL------DE-LRDG---APGGTEQEVRGYlgrflfsgddafkpvGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 149 WISMALAQGTDLLLLDEPTTYLDishqIEVLELLKKLNRDHGRTVVMVLHD---LNQAaqyADYLISVLDGKI 218
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDryfLDRV---ATRILEFEDGGV 507
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-229 |
8.62e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.69 E-value: 8.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHR-----QPSKEVAKKLAILPQSPQAPE-GL 92
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRKEIGLVFQFPEYQLfQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 93 TVEELCYFGrhPHKklLSKHTQEDHDMVEWALEATGMI-ELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:PRK13645 107 TIEKDIAFG--PVN--LGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 172 ISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFT 229
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-242 |
9.49e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.92 E-value: 9.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGK--DIHRQPSKEVAKKLAI 81
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPQAPEGLT--VEELCYFGRHphkklLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:PRK13638 82 VFQDPEQQIFYTdiDSDIAFSLRN-----LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRdHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVF----------- 228
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFacteameqagl 235
|
250
....*....|....*..
gi 489326441 229 TQPFFREV---FGLECC 242
Cdd:PRK13638 236 TQPWLVKLhtqLGLPLC 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-228 |
1.09e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.00 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAP-EGLTVEEL 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQfVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CYFGRH----PHKKLLSKhtqedhdmVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDIS 173
Cdd:PRK13642 103 VAFGMEnqgiPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 174 HQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVF 228
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-232 |
1.17e-22 |
|
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: 93.59 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 27 EEGKITALIGANGCGKSTILKSLARLMAPKSG---------TVLLE--GKDIHRQPSKEVAKKL--AILPQS----PQAP 89
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILDEfrGSELQNYFTKLLEGDVkvIVKPQYvdliPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 90 EGLTVEelcyfgrhphkkLLSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTY 169
Cdd:cd03236 104 KGKVGE------------LLKK--KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 170 LDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYlISVLDGKIYNAGtpedVFTQPF 232
Cdd:cd03236 170 LDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDY-IHCLYGEPGAYG----VVTLPK 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-231 |
1.19e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.65 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYD---------STV-IIDGVDLKIEEGKITALIGANGCGKSTilksLARLM----APKSGTVLLEGKDIhR 69
Cdd:PRK11308 6 LQAIDLKKHYPvkrglfkpeRLVkALDGVSFTLERGKTLAVVGESGCGKST----LARLLtmieTPTGGELYYQGQDL-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 70 QPSKEVAK----KLAILPQSPqapegltveelcYFGRHPHKKL-------LSKHTQED-HDMVEWALEATGMIELK---- 133
Cdd:PRK11308 81 KADPEAQKllrqKIQIVFQNP------------YGSLNPRKKVgqileepLLINTSLSaAERREKALAMMAKVGLRpehy 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 134 DRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISV 213
Cdd:PRK11308 149 DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
250
....*....|....*...
gi 489326441 214 LDGKIYNAGTPEDVFTQP 231
Cdd:PRK11308 229 YLGRCVEKGTKEQIFNNP 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-218 |
1.23e-22 |
|
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: 91.12 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDST--VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAI 81
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSpqapegltveelcyfgrhphkkllskhtqedhdmvewaleatgmIELKDRTL--DALSGGQRQRAWISMALAQGTD 159
Cdd:cd03246 81 LPQD--------------------------------------------DELFSGSIaeNILSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQyADYLISVLDGKI 218
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-217 |
1.90e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 20 DGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH-RQPSKEVAKKLAILPQSPQAPEGLTVEE-- 96
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIALGIGMVHQHFMLVPNLTVAEni 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 97 -LcyfGRHPHKKLLSKHTQEDHDMVEwALEATGM-IELkDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISH 174
Cdd:COG3845 102 vL---GLEPTKGGRLDRKAARARIRE-LSERYGLdVDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489326441 175 QIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYlISVL-DGK 217
Cdd:COG3845 177 ADELFEILRRL-AAEGKSIIFITHKLREVMAIADR-VTVLrRGK 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
29-231 |
1.92e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.41 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 29 GKITALIGANGCGKSTILKSLARLMAPK---SGTVLLEGKDIHRQPSKEV----AKKLAILPQSP------------QAP 89
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELnklrAEQISMIFQDPmtslnpymrvgeQLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 90 EGLTVeelcyfgrhpHKKLlSKHT--QEDHDMvewaLEATGMIELKDRTL---DALSGGQRQRAWISMALAQGTDLLLLD 164
Cdd:PRK09473 122 EVLML----------HKGM-SKAEafEESVRM----LDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 165 EPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-217 |
2.14e-22 |
|
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: 92.47 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 20 DGVDLKIEEGKIT-----ALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIhrqpskevakklAILPQSPQAPEGLTV 94
Cdd:cd03237 11 GEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELcyfgrhphkklLSKHTQEDHDMVEWALEAT---GMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:cd03237 79 RDL-----------LSSITKDFYTHPYFKTEIAkplQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489326441 172 ISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLIsVLDGK 217
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI-VFEGE 192
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-227 |
2.46e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.91 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI---HRQPSKEVAKKLAILPQS 85
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEELCYFgrhPhkklLSKHTQED----HDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:PRK11831 93 GALFTDMNVFDNVAY---P----LREHTQLPapllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 162 LLDEPTTYLD-ISHQIEVlELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:PRK11831 166 MFDEPFVGQDpITMGVLV-KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-237 |
2.68e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.26 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-L 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYFGRHPHKKLlskhTQEDH-DMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGT 158
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDL----SAEQReDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVF 237
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-218 |
2.75e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.83 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIhRQPSKEVAKKL-----AILPQSPQA--PE 90
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL-AKLNRAQRKAFrrdiqMVFQDSISAvnPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 91 GlTVEELCyfgRHPHKKLLSKHTQEDHDMVEWALEATGM-IELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTY 169
Cdd:PRK10419 106 K-TVREII---REPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489326441 170 LDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-204 |
3.08e-22 |
|
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: 89.43 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLeGKDIhrqpskevakKLAILP 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTV----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QspqapegltveelcyfgrhphkkllskhtqedhdmvewaleatgmielkdrtldaLSGGQRQRAWISMALAQGTDLLLL 163
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNrdhgRTVVMVLHD---LNQAA 204
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYP----GTVILVSHDryfLDQVA 134
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-231 |
4.69e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.23 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSK---EVAKKLAILPQSPQA---PEgL 92
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDPLAslnPR-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 93 TV-----EELCYFgrHPHkklLSKhtQEDHDMVEWALEATGMIE-LKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:PRK15079 116 TIgeiiaEPLRTY--HPK---LSR--QEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 167 TTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-238 |
8.64e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.94 E-value: 8.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTvllegkdIHRQPSKE---VAKKLA 80
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRNGKLRigyVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPqapegLTVEElcYFGRHPHKKllskhtqeDHDMVEwALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDL 160
Cdd:PRK09544 78 LDTTLP-----LTVNR--FLRLRPGTK--------KEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 161 LLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLIsVLDGKIYNAGTPEDVFTQPFFREVFG 238
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL-CLNHHICCSGTPEVVSLHPEFISMFG 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-222 |
1.50e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.90 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVllegkDIHRQPSKEVAKKLAILPQspqapegLTVEEL 97
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----TVRGRVSSLLGLGGGFNPE-------LTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CYF-GRhphkkLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQI 176
Cdd:cd03220 105 IYLnGR-----LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489326441 177 EVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAG 222
Cdd:cd03220 180 KCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-218 |
1.63e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.69 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQpSKEVAKKLAI-----------LPqspq 87
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-RKEFARRIGVvfgqrsqlwwdLP---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 APEGLTVEELCYfgRHPHKKLlsKHTQEdhdmvewalEATGMIELKD------RTLdalSGGQRQRAWISMALAQGTDLL 161
Cdd:COG4586 113 AIDSFRLLKAIY--RIPDAEY--KKRLD---------ELVELLDLGElldtpvRQL---SLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-227 |
1.74e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQpSKEVAKKLAILPQSP 86
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHARQRVGVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAPEGLTV-EELCYFGRHphkklLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDE 165
Cdd:PRK13537 90 NLDPDFTVrENLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 166 PTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-230 |
1.74e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.35 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELcyfgrhphkkLLSKHTQEDHDMVEwALEATGMIEL--KDRTLDA--------LSGGQRQRAW 149
Cdd:PRK11160 417 SVVSQRVHLFSATLRDNL----------LLAAPNASDEALIE-VLQQVGLEKLleDDKGLNAwlgeggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 150 ISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNQAAQYaDYLISVLDGKIYNAGTPEDVFT 229
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLA 562
|
.
gi 489326441 230 Q 230
Cdd:PRK11160 563 Q 563
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-240 |
3.29e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK-KLAILPQS 85
Cdd:PRK09700 9 AGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELK---DRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:PRK09700 89 LSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKvdlDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 163 LDEPTTYLdISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLE 240
Cdd:PRK09700 169 MDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRE 245
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-228 |
7.47e-21 |
|
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: 91.35 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:COG4618 329 GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGlTVEE-LCYFGrhphkkllskhtQEDHDMVEWALEATG---MIeLK-----DRTLDA----LSGGQRQ 146
Cdd:COG4618 409 GYLPQDVELFDG-TIAEnIARFG------------DADPEKVVAAAKLAGvheMI-LRlpdgyDTRIGEggarLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 147 RawISMALAQGTD--LLLLDEPTTYLDisHQIE--VLELLKKLnRDHGRTVVMVLHDLNqAAQYADYLISVLDGKIYNAG 222
Cdd:COG4618 475 R--IGLARALYGDprLVVLDEPNSNLD--DEGEaaLAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFG 548
|
....*.
gi 489326441 223 TPEDVF 228
Cdd:COG4618 549 PRDEVL 554
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-200 |
8.87e-21 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 91.38 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 27 EEGKITALIGANGCGKSTILKSLARLMAPKSGtvllegkDIHRQPSKE-----------------VAK---KLAILPQS- 85
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSWDevlkrfrgtelqdyfkkLANgeiKVAHKPQYv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 ---PQAPEGlTVEELcyfgrhphkklLSKhTQEdHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:COG1245 170 dliPKVFKG-TVREL-----------LEK-VDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*...
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDL 200
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-231 |
1.04e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 14 DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKsGTVLLEGKDIHRQPSKE---VAKKLAILPQSPQA-- 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 89 -PEgLTVEELCYFGRHPHKKLLSKHTQEDHdmVEWALEATGM-IELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:PRK15134 376 nPR-LNVLQIIEEGLRVHQPTLSAAQREQQ--VIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 167 TTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1-226 |
1.13e-20 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 91.17 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK 78
Cdd:TIGR03797 449 SGAIEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 79 LAILPQSPQAPEGLTVEELCyfGRHPHkkllskhTQEDhdmvewALEATGMIELKD---------RTL-----DALSGGQ 144
Cdd:TIGR03797 529 LGVVLQNGRLMSGSIFENIA--GGAPL-------TLDE------AWEAARMAGLAEdirampmgmHTViseggGTLSGGQ 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 145 RQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNrdhgRTVVMVLHDLNqAAQYADYLISVLDGKIYNAGTP 224
Cdd:TIGR03797 594 RQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTY 668
|
..
gi 489326441 225 ED 226
Cdd:TIGR03797 669 DE 670
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-230 |
1.22e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 90.87 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:TIGR01842 315 GHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYFGRHPhkkllskhtqEDHDMVEwALEATGMIELKDRTLD-----------ALSGGQRQRA 148
Cdd:TIGR01842 395 GYLPQDVELFPGTVAENIARFGENA----------DPEKIIE-AAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 149 WISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNqAAQYADYLISVLDGKIYNAGTPEDVF 228
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVL 541
|
..
gi 489326441 229 TQ 230
Cdd:TIGR01842 542 AK 543
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-231 |
1.36e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 87.96 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKD-----IHRQPSKEvAKK 78
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAE-RRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 79 LA-----ILPQSPQAPEGLTVEElcyfGRHPHKKLLSKHTQEDHDMVEWALEATGMIEL-KDRTLD---ALSGGQRQRAW 149
Cdd:TIGR02323 83 LMrtewgFVHQNPRDGLRMRVSA----GANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDlprAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 150 ISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFT 229
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLD 238
|
..
gi 489326441 230 QP 231
Cdd:TIGR02323 239 DP 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-208 |
1.44e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.63 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-LAIL 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEE-LCYFGRHPHKKLLSKHTQEDHDMVewaleaTGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:PRK11614 86 PEGRRVFSRMTVEEnLAMGGFFAERDQFQERIKWVYELF------PRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYAD 208
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLAD 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-225 |
1.80e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.43 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPK--SGTVLLEGKDIHRQPSKEVAKK-LAILPQS 85
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLgIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEELCyfgrhphkkllskhtqedhdmvewaleatgmielkdRTLDA-LSGGQRQRAWISMALAQGTDLLLLD 164
Cdd:cd03217 86 PPEIPGVKNADFL------------------------------------RYVNEgFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 165 EPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHdLNQAAQY--ADYLISVLDGKIYNAGTPE 225
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKL-REEGKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSGDKE 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-211 |
1.99e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.45 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIhRQPSKE---VAKKLA 80
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAErgvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILP-QSPQAPEGLTVEeLCYFGRhphkkllSKHTQEDHDMvewaLEATGMIELKDRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:PRK11248 81 LLPwRNVQDNVAFGLQ-LAGVEK-------MQRLEIAHQM----LKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLI 211
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELV 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-198 |
2.11e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.97 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 20 DGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE-VAKKLAILPQSPQ-APEgLTVEEL 97
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHlVPE-MTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CYFGRHPHK------KLLSKHTQEdhdmvewALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:PRK11288 100 LYLGQLPHKggivnrRLLNYEARE-------QLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180
....*....|....*....|....*...
gi 489326441 172 iSHQIEVL-ELLKKLnRDHGRTVVMVLH 198
Cdd:PRK11288 173 -AREIEQLfRVIREL-RAEGRVILYVSH 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-216 |
3.09e-20 |
|
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: 86.37 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYDS---TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK 78
Cdd:cd03248 10 GIVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 79 LAILPQSPQAPEGLTVEELCY-FGRHPHKKLL-SKHTQEDHDMVewALEATGMIELKDRTLDALSGGQRQRAWISMALAQ 156
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYgLQSCSFECVKeAAQKAHAHSFI--SELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNqAAQYADyLISVLDG 216
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLS-TVERAD-QILVLDG 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-227 |
5.57e-20 |
|
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: 86.00 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 14 DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQS-------- 85
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQEnvlfnrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 ----PQAPEGLTVEELCYFGRhphkkllskhTQEDHDMVEWALEATGMIeLKDRTLdALSGGQRQRAWISMALAQGTDLL 161
Cdd:cd03252 93 rdniALADPGMSMERVIEAAK----------LAGAHDFISELPEGYDTI-VGEQGA-GLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRdhGRTVVMVLHDLNqAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-231 |
6.01e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.01 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGLTVEEL 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CY-FGRHPHKKLLSKHTQED-HDMVewaleaTGMIELKDRTLDA----LSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:TIGR00958 576 AYgLTDTPDEEIMAAAKAANaHDFI------MEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 172 ishqIEVLELLKKLNRDHGRTVVMVLHDLnQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:TIGR00958 650 ----AECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-216 |
9.72e-20 |
|
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: 84.69 E-value: 9.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK----LAILPQSPQAPEGlTV 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELCYFGRhPHKKLLSKHT------QEDHDMVEWALEAtgmiELKDRTLDaLSGGQRQRAWISMALAQGTDLLLLDEPTT 168
Cdd:cd03290 96 EENITFGS-PFNKQRYKAVtdacslQPDIDLLPFGDQT----EIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489326441 169 YLDI---SH--QIEVLELLkklnRDHGRTVVMVLHDLnQAAQYADYLISVLDG 216
Cdd:cd03290 170 ALDIhlsDHlmQEGILKFL----QDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-230 |
1.45e-19 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 87.88 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDihrqpskevakkL 79
Cdd:TIGR01846 454 GAITFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVD------------L 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AIL-PQSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATG----MIELK---DRTLD----ALSGGQRQR 147
Cdd:TIGR01846 522 AIAdPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGahdfISELPqgyNTEVGekgaNLSGGQRQR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 148 AWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRdhGRTVVMVLHDLNqAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:TIGR01846 602 IAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEEL 678
|
...
gi 489326441 228 FTQ 230
Cdd:TIGR01846 679 LAL 681
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
18-231 |
2.25e-19 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 87.31 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGLTVEEL 97
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNL 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CyfgrhphkklLSKHTQEDHDMVEWALEATGMIELKDRT--LDA--------LSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:TIGR03796 574 T----------LWDPTIPDADLVRACKDAAIHDVITSRPggYDAelaegganLSGGQRQRLEIARALVRNPSILILDEAT 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 168 TYLDISHQIEVLELLkklnRDHGRTVVMVLHDLNqAAQYADyLISVLD-GKIYNAGTPEDVFTQP 231
Cdd:TIGR03796 644 SALDPETEKIIDDNL----RRRGCTCIIVAHRLS-TIRDCD-EIIVLErGKVVQRGTHEELWAVG 702
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-224 |
2.67e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 83.23 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:cd03369 5 GEIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYFGRHPHKKLLSkhtqedhdmvewALEATGmielkdrTLDALSGGQRQRAWISMALAQGTD 159
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFDEYSDEEIYG------------ALRVSE-------GGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNQAAQYADYLisVLD-GKIYNAGTP 224
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTN--STILTIAHRLRTIIDYDKIL--VMDaGEVKEYDHP 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-203 |
2.68e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.10 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYD----STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAK-- 77
Cdd:PRK11629 6 LQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 78 --KLAILPQSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMvewaLEATGMIELKDRTLDALSGGQRQRAWISMALA 155
Cdd:PRK11629 86 nqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489326441 156 QGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQA 203
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-225 |
2.79e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.96 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMA--PKSGTVLLEGKDIHRQPSKEVAKK---LAIlp 83
Cdd:COG0396 6 LHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARAgifLAF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCyfgrhphKKLLSKHTQEDHDMVEW------ALEATGM-IELKDRTLDA-LSGGQRQRAWISMALA 155
Cdd:COG0396 84 QYPVEIPGVSVSNFL-------RTALNARRGEELSAREFlkllkeKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 156 QGTDLLLLDEPTTYLDI-SHQIeVLELLKKLnRDHGRTVVMVLHdlNQAA-QY--ADYLISVLDGKIYNAGTPE 225
Cdd:COG0396 157 LEPKLAILDETDSGLDIdALRI-VAEGVNKL-RSPDRGILIITH--YQRIlDYikPDFVHVLVDGRIVKSGGKE 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-217 |
2.84e-19 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 86.76 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 25 KIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVllegkdihrqpskEVAKKLAILPQSPQAPEGLTVEELcyfgrhp 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQYISPDYDGTVEEF------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 105 hkklLSKHTQEDHDMVEWALEAT---GMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLEL 181
Cdd:COG1245 422 ----LRSANTDDFGSSYYKTEIIkplGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170 180 190
....*....|....*....|....*....|....*....
gi 489326441 182 LKKLNRDHGRTVVMVLHDLnqaaQYADYL---ISVLDGK 217
Cdd:COG1245 498 IRRFAENRGKTAMVVDHDI----YLIDYIsdrLMVFEGE 532
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-224 |
3.19e-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: 83.31 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQ 84
Cdd:cd03244 6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SPQAPEGlTVEE-LCYFGRHPHKKLLSkhtqedhdmvewALEATGMIEL---KDRTLDA--------LSGGQRQRAWISM 152
Cdd:cd03244 86 DPVLFSG-TIRSnLDPFGEYSDEELWQ------------ALERVGLKEFvesLPGGLDTvveeggenLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 153 ALAQGTDLLLLDEPTTYLDISHQIEVLELLKklNRDHGRTVVMVLHDLNQAAQYAdyLISVLD-GKIYNAGTP 224
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIIDSD--RILVLDkGRVVEFDSP 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-231 |
3.44e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLM-APK----SGTVLLEGKDIHRQPSKEV----AKKLAILPQSPQA 88
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPvvypSGDIRFHGESLLHASEQTLrgvrGNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 89 peGL----TVEELCYfgrhphkKLLSKHTQEDHD-----MVEwALEATGMIELKDRTLD---ALSGGQRQRAWISMALAQ 156
Cdd:PRK15134 104 --SLnplhTLEKQLY-------EVLSLHRGMRREaargeILN-CLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-218 |
3.51e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHR----QPSKEVAKKLAILPQS----P--Q 87
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRAKHVGFVFQSfmliPtlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 APEGLTVEELcyfgrhphkkLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:PRK10584 105 ALENVELPAL----------LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489326441 168 TYLDISHQIEVLELLKKLNRDHGRTVVMVLHDlNQAAQYADYLISVLDGKI 218
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-237 |
6.21e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 85.95 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYD-STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLA 80
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPQAPEGLTVEELcyfgrhphkkLLSKHTQEDHDMVEWALEatgMIELKDRTLD--------------ALSGGQRQ 146
Cdd:TIGR01193 552 YLPQEPYIFSGSILENL----------LLGAKENVSQDEIWAACE---IAEIKDDIENmplgyqtelseegsSISGGQKQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 147 RAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRdhgRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPED 226
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDE 694
|
250
....*....|..
gi 489326441 227 VFTQP-FFREVF 237
Cdd:TIGR01193 695 LLDRNgFYASLI 706
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-235 |
6.28e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.05 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLT-LSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMaPKSGTVLLEGKDIHRQPSKEVAKKLAILPQ 84
Cdd:PRK11174 352 AEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SPQAPEGLTVEELcyfgrhphkkLLSKHTQEDHDmVEWALEATGMIELKDRT---LD--------ALSGGQRQRAWISMA 153
Cdd:PRK11174 431 NPQLPHGTLRDNV----------LLGNPDASDEQ-LQQALENAWVSEFLPLLpqgLDtpigdqaaGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 154 LAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHgrTVVMVLHDLNQAAQYaDYlISVLD-GKIYNAGTPEDVFTQP- 231
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQ-IWVMQdGQIVQQGDYAELSQAGg 575
|
....
gi 489326441 232 FFRE 235
Cdd:PRK11174 576 LFAT 579
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-198 |
6.77e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.23 E-value: 6.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 17 VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAilPQSPQAPEgLTVEE 96
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPA-LTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 97 -LC----YFGRHPHkkllskhtqedhdMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:PRK13539 93 nLEfwaaFLGGEEL-------------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|
gi 489326441 172 ISHQievlELLKKLNRDH---GRTVVMVLH 198
Cdd:PRK13539 160 AAAV----ALFAELIRAHlaqGGIVIAATH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-227 |
7.21e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.82 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 17 VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKdihrqpskeVAkklAILpqSPQA---PEgLT 93
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VS---ALL--ELGAgfhPE-LT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYF-GR---HPHKKLLSKhtqEDhDMVEWAleatgmiELKD------RTldaLSGGQRQRAWISMALAQGTDLLLL 163
Cdd:COG1134 105 GRENIYLnGRllgLSRKEIDEK---FD-EIVEFA-------ELGDfidqpvKT---YSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLIsVLD-GKIYNAGTPEDV 227
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAI-WLEkGRLVMDGDPEEV 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-200 |
1.33e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.86 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 26 IEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKdihrqpskeVAKKlailPQSPQAPEGLTVEELcyfgrhph 105
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK---------ISYK----PQYIKPDYDGTVEDL-------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 106 kklLSKHTQEDHDMVEWA--LEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLK 183
Cdd:PRK13409 421 ---LRSITDDLGSSYYKSeiIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170
....*....|....*..
gi 489326441 184 KLNRDHGRTVVMVLHDL 200
Cdd:PRK13409 498 RIAEEREATALVVDHDI 514
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-230 |
1.59e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYDS--TVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:PRK11176 340 GDIEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYFGRhphkkllSKHTQEDHDMVEWALEATGMIELKDRTLDA--------LSGGQRQRAWIS 151
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAYART-------EQYSREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDhgRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-200 |
1.71e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.47 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 26 IEEGKITALIGANGCGKSTILKSLARLMAPK-----------------SGTVL------LEGKDIhrqpskEVAKKLAIL 82
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELqnyfkkLYNGEI------KVVHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGlTVEELCyfgrhphkkllsKHTQEdHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLL 162
Cdd:PRK13409 170 DLIPKVFKG-KVRELL------------KKVDE-RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*...
gi 489326441 163 LDEPTTYLDISHQIEVLELLKKLNRdhGRTVVMVLHDL 200
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-231 |
1.85e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 83.25 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKStiLKSLA---------RLMAPKsgtVLLEGKDIHRQPSKE----VAKKLAILPQS 85
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKS--VSSLAimglidypgRVMAEK---LEFNGQDLQRISEKErrnlVGAEVAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PqapegLTVEELCYFGRHPHKKLLSKHTQEDH-DMVEWALEATGMIELKDRT--LDA----LSGGQRQRAWISMALAQGT 158
Cdd:PRK11022 98 P-----MTSLNPCYTVGFQIMEAIKVHQGGNKkTRRQRAIDLLNQVGIPDPAsrLDVyphqLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 159 DLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-227 |
2.61e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.96 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQpSKEVAKKLAILPQSPQA 88
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-ARLARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 89 PEGLTVEE-LCYFGRHphkklLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:PRK13536 126 DLEFTVREnLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 168 TYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:PRK13536 201 TGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-230 |
3.80e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILkSL---ARlmAPKSGTVLLEGKDI----HRQpskEVAKKLAI 81
Cdd:NF033858 7 VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLiagAR--KIQQGRVEVLGGDMadarHRR---AVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQspqapeGL--------TVEE-LCYFGRhphkkLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISM 152
Cdd:NF033858 81 MPQ------GLgknlyptlSVFEnLDFFGR-----LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 153 ALAQGTDLLLLDEPTTYLD-ISHQiEVLELLKKLNRDH-GRTVVMVLHDLNQAAQYaDYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDpLSRR-QFWELIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-226 |
1.22e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHR-QPSKevAKKLAI--LPQSPQA 88
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAK--AHQLGIylVPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 89 PEGLTVEELCYFGRHPHKKLLSKHTQEDHDM-VEWALEAT-GMIELKDrtldalsggqRQRAWISMALAQGTDLLLLDEP 166
Cdd:PRK15439 98 FPNLSVKENILFGLPKRQASMQKMKQLLAALgCQLDLDSSaGSLEVAD----------RQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 167 TTYLDishQIEVLELLKKLN--RDHGRTVVMVLHDLNQAAQYADYlISVL-DGKIYNAGTPED 226
Cdd:PRK15439 168 TASLT---PAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADR-ISVMrDGTIALSGKTAD 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-231 |
1.46e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEG------KDIHRQPSKEVAKKLAILPQS 85
Cdd:COG4161 11 FYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGLTVEElcYFGRHPHKKL-LSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLD 164
Cdd:COG4161 91 YNLWPHLTVME--NLIEAPCKVLgLSK--EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 165 EPTTYLDISHQIEVLELLKKLNrDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEdVFTQP 231
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQP 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-232 |
1.67e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 80.72 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLmAPKSGTV-----LLEGKDIHRQPSKE----VAKKLAILPQSPQA 88
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRErrkiIGREIAMIFQEPSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 89 ---PEGLTVEELC-----------YFGRHPHKK-----LLSKHTQEDHD--MVEWALEatgmielkdrtldaLSGGQRQR 147
Cdd:COG4170 101 cldPSAKIGDQLIeaipswtfkgkWWQRFKWRKkraieLLHRVGIKDHKdiMNSYPHE--------------LTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 148 AWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYlISVL-DGKIYNAGTPED 226
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADT-ITVLyCGQTVESGPTEQ 245
|
....*.
gi 489326441 227 VFTQPF 232
Cdd:COG4170 246 ILKSPH 251
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-217 |
2.03e-17 |
|
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: 78.28 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVllegkdihrqpskEVAKKLAILPQSPQAPEG 91
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 92 lTVEELCYFGRhphkkllskhtQEDHDMVEWALEATG------MIELKDRTL-----DALSGGQRQRawISMALA--QGT 158
Cdd:cd03250 81 -TIRENILFGK-----------PFDEERYEKVIKACAlepdleILPDGDLTEigekgINLSGGQKQR--ISLARAvySDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489326441 159 DLLLLDEPTTYLDI---SHQIE--VLELLKKlnrdhGRTVVMVLHDLnQAAQYADYLISVLDGK 217
Cdd:cd03250 147 DIYLLDDPLSAVDAhvgRHIFEncILGLLLN-----NKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-198 |
3.62e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.62 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTL-SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLegkdihrqPSKEvakKLA 80
Cdd:COG4178 361 GALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGA---RVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPQAPEGLTVEELCYfgrhPHkkllsKHTQEDHDMVEWALEATGMIELKDRtLDA-------LSGGQRQRawISMA 153
Cdd:COG4178 430 FLPQRPYLPLGTLREALLY----PA-----TAEAFSDAELREALEAVGLGHLAER-LDEeadwdqvLSLGEQQR--LAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489326441 154 --LAQGTDLLLLDEPTTYLDISHQIEVLELLKKlnRDHGRTVVMVLH 198
Cdd:COG4178 498 rlLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-223 |
6.03e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYD-STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLA 80
Cdd:PRK13657 333 GAVEFDDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPqapeGLtveelcyFGRHPHKKL-LSKHTQEDHDMVEwALE---ATGMIELKDRTLDA--------LSGGQRQRA 148
Cdd:PRK13657 413 VVFQDA----GL-------FNRSIEDNIrVGRPDATDEEMRA-AAEraqAHDFIERKPDGYDTvvgergrqLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 149 WISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNrdHGRTVVMVLHDLNQAAQyADyLISVLD-GKIYNAGT 223
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-AD-RILVFDnGRVVESGS 552
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-218 |
7.03e-17 |
|
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: 76.32 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH-RQPSKEVAKKLAILPQSPQApEGLtveel 97
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAGIAYVPEDRKR-EGL----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 cyFGRHPhkkllskhtqedhdmVEWALEATGMielkdrtldaLSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIE 177
Cdd:cd03215 90 --VLDLS---------------VAENIALSSL----------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489326441 178 VLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:cd03215 143 IYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-217 |
9.12e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.59 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMaPK---SGTVLLEGKDIHRQPSKEVAKK-LAILPQ 84
Cdd:PRK13549 11 ITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAgIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 SPQAPEGLTVEELCYFGRHPHKkllskhtqedHDMVEWA---LEATGMI-ELK-----DRTLDALSGGQRQRAWISMALA 155
Cdd:PRK13549 90 ELALVKELSVLENIFLGNEITP----------GGIMDYDamyLRAQKLLaQLKldinpATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 156 QGTDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADyLISVL-DGK 217
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISD-TICVIrDGR 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-231 |
9.48e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.27 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDihrqpskEVAKKLAILP 83
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-------GQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSP-------------QAP-EGL--TV-------EELCYFG-RHpHKKLLSKhtqedhdmvewALEATGMIEL-KDRTLD 138
Cdd:PRK11701 80 EAErrrllrtewgfvhQHPrDGLrmQVsaggnigERLMAVGaRH-YGDIRAT-----------AGDWLERVEIdAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 139 ---ALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLD 215
Cdd:PRK11701 148 lptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250
....*....|....*.
gi 489326441 216 GKIYNAGTPEDVFTQP 231
Cdd:PRK11701 228 GRVVESGLTDQVLDDP 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-239 |
1.08e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.10 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLM--APKSGTVLLEGKDIHRQPSKEV-AKKLA 80
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQSPQAPEGLTVEELCYFGrhpHKKLLSKHTQEDHDMVEWALEATGMIELKD----RTLDALSGGQRQRAWISMALAQ 156
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLG---NEITLPGGRMAYNAMYLRAKNLLRELQLDAdnvtRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRdHGRTVVMVLHDLNQAAQYADYLISVLDG-----KIYNAGTPEDVFTQP 231
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGqhvatKDMSTMSEDDIITMM 237
|
....*...
gi 489326441 232 FFREVFGL 239
Cdd:TIGR02633 238 VGREITSL 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-231 |
1.35e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGK--DIHRQPSkevAKKLAILPQ 84
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPS---DKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 85 S-----------PQapegLTV-EELCyfgRHPHKKL-LSKhtQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWIS 151
Cdd:PRK11124 83 NvgmvfqqynlwPH----LTVqQNLI---EAPCRVLgLSK--DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 152 MALAQGTDLLLLDEPTTYLD--ISHQIevLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTpEDVFT 229
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDpeITAQI--VSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFT 229
|
..
gi 489326441 230 QP 231
Cdd:PRK11124 230 QP 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-241 |
1.95e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAP---KSGTVLLEGKDIHRqpsKEVAKKLAILPQSPQAPEGLTV 94
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA---KEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELCYF------GRHPHKKllskhtqEDHDMVEWALEATGMIELKD------RTLDALSGGQRQRawISMALAQGTD--L 160
Cdd:TIGR00955 117 REHLMFqahlrmPRRVTKK-------EKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKR--LAFASELLTDppL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 161 LLLDEPTTYLDISHQIEVLELLKKLNrDHGRTVVMVLHD-LNQAAQYADYLISVLDGKIYNAGTPEDVFtqPFFREvFGL 239
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAV--PFFSD-LGH 263
|
..
gi 489326441 240 EC 241
Cdd:TIGR00955 264 PC 265
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-205 |
2.63e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSkEVAKKLAILP 83
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEE-LCYFGRHphkkllskHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAwismALA----QGT 158
Cdd:PRK13538 81 HQPGIKTELTALEnLRFYQRL--------HGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRV----ALArlwlTRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489326441 159 DLLLLDEPTTYLDiSHQIEVLELLKKLNRDHGRTVVMVLH-DLNQAAQ 205
Cdd:PRK13538 149 PLWILDEPFTAID-KQGVARLEALLAQHAEQGGMVILTTHqDLPVASD 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-219 |
2.93e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVA---KKLAILPQSPQAPEGLTVe 95
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQDHHLLMDRTV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 96 elcyFGRHPHKKLLSKHTQED-HDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISH 174
Cdd:PRK10908 97 ----YDNVAIPLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489326441 175 QIEVLELLKKLNRdHGRTVVMVLHDLNQAAQYADYLISVLDGKIY 219
Cdd:PRK10908 173 SEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-231 |
4.77e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.81 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLTLSYD-STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI-HRQPSKE---- 74
Cdd:PRK11650 1 MAGLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEPADRdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 75 VAKKLAILPQspqapegLTVEELCYFG---RHPHKKLLSKHTQEDHDMVEwaLEatgmiELKDRTLDALSGGQRQRAWIS 151
Cdd:PRK11650 81 VFQNYALYPH-------MSVRENMAYGlkiRGMPKAEIEERVAEAARILE--LE-----PLLDRKPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEV-LELlKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAKLRVQMrLEI-QRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
.
gi 489326441 231 P 231
Cdd:PRK11650 226 P 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-231 |
4.99e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQpSKEVakkLAILPQSPQAPEGLTVEELCYFG 101
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRR-SRQV---IELSEQSAAQMRHVRGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 102 RHPHKKL-------------LSKHTQEDHDmvEWALEATGMIELK---------DRTLDALSGGQRQRAWISMALAQGTD 159
Cdd:PRK10261 111 QEPMTSLnpvftvgeqiaesIRLHQGASRE--EAMVEAKRMLDQVripeaqtilSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 160 LLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-231 |
8.12e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE---VAKKLAILPQSPQA---PEgL 92
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqaLRRDIQFIFQDPYAsldPR-Q 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 93 TVEELCYFGRHPHKKLLSKHTQEdhdMVEWALEATGMI-ELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAA---RVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 172 ISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-223 |
1.13e-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: 73.89 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYD--STVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSkEVAKKLAI 81
Cdd:TIGR01257 1938 LRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPQAPEGLTVEELCYFgrhpHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYL----YARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGT 223
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
30-206 |
1.50e-14 |
|
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: 73.05 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 30 KItALIGANGCGKSTILKSLARLMAPKSGTVLLegkdihrQPSKevakKLAILPQSPQAPEGLTVEELCYFGRHPHKKLL 109
Cdd:TIGR03719 33 KI-GVLGLNGAGKSTLLRIMAGVDKDFNGEARP-------QPGI----KVGYLPQEPQLDPTKTVRENVEEGVAEIKDAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 110 S-------KHTQEDHDM---------VEWALEATGMIELkDRTL----DAL------------SGGQRQRAWISMALAQG 157
Cdd:TIGR03719 101 DrfneisaKYAEPDADFdklaaeqaeLQEIIDAADAWDL-DSQLeiamDALrcppwdadvtklSGGERRRVALCRLLLSK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489326441 158 TDLLLLDEPTTYLDishqIEVLELLKKLNRDHGRTVVMVLHD---LNQAAQY 206
Cdd:TIGR03719 180 PDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHDryfLDNVAGW 227
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-198 |
1.84e-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: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLA--RLMAPKSGTVLLEGkdihRQPSKEVAKKLAILPQSPQAPEGLTVE 95
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILING----RPLDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 96 ElcyfgrhphkkllskhtqedhdmvewALEATGMielkdrtLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQ 175
Cdd:cd03232 98 E--------------------------ALRFSAL-------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|...
gi 489326441 176 IEVLELLKKLnRDHGRTVVMVLH 198
Cdd:cd03232 145 YNIVRFLKKL-ADSGQAILCTIH 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-199 |
1.89e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 11 LSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEgKDIhrqpskevakKLAILPQSPQAPE 90
Cdd:PRK11147 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDL----------IVARLQQDPPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 91 GLTV-----EELCYFGRH--------------PHKKLLSK--HTQEDHDMVE-WALEAT-----GMIELK-DRTLDALSG 142
Cdd:PRK11147 80 EGTVydfvaEGIEEQAEYlkryhdishlvetdPSEKNLNElaKLQEQLDHHNlWQLENRinevlAQLGLDpDAALSSLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 143 GQRQRAWISMALAQGTDLLLLDEPTTYLDIShQIEVLE-LLKklnrDHGRTVVMVLHD 199
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIE-TIEWLEgFLK----TFQGSIIFISHD 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-199 |
3.98e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGK------DIHRQ--- 70
Cdd:PRK11147 316 GKIVFEMENVNYqiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevayfDQHRAeld 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 71 PSKEVAKKLAilpqspqapEGltVEELCYFGRHPHkkLLSkHTQED--HDMvewaleaTGMIELKdrtldALSGGQRQRA 148
Cdd:PRK11147 396 PEKTVMDNLA---------EG--KQEVMVNGRPRH--VLG-YLQDFlfHPK-------RAMTPVK-----ALSGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489326441 149 WISMALAQGTDLLLLDEPTTYLDIshqiEVLELLKKLNRDHGRTVVMVLHD 199
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-230 |
4.24e-14 |
|
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: 71.76 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVI--IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTV-LLEGKD----IHRQPSKE--VAKKLAIL 82
Cdd:TIGR03269 291 SVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdmTKPGPDGRgrAKRYIGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSpqapegltveelcyFGRHPHKKLLSKHTQ----EDHDmvEWA-------LEATGMIELK-----DRTLDALSGGQRQ 146
Cdd:TIGR03269 371 HQE--------------YDLYPHRTVLDNLTEaiglELPD--ELArmkavitLKMVGFDEEKaeeilDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 147 RAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPED 226
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
....
gi 489326441 227 VFTQ 230
Cdd:TIGR03269 515 IVEE 518
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-198 |
4.30e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 10 TLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLA-RLMAPK-SGTVLLEGkdihRQPSKEVAKKLAILPQSPQ 87
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN----RKPTKQILKRTGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 APEGLTVEE---LCYFGRHPhkKLLSKHTQ---EDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:PLN03211 151 LYPHLTVREtlvFCSLLRLP--KSLTKQEKilvAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190
....*....|....*....|....*....|....*..
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRdHGRTVVMVLH 198
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMH 264
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-217 |
6.09e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKK-LAILPQSPQAPEGLTVEEL 97
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDaLSGGQRQRAWISMALAQGTDLLLLDEPTTYL---DISH 174
Cdd:PRK10982 94 MWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNH 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489326441 175 QIEVLELLKklnrDHGRTVVMVLHDLNQAAQYADYLISVLDGK 217
Cdd:PRK10982 173 LFTIIRKLK----ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-196 |
8.33e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH-RQPSKEVAKKLAILPQSPQApEGL----T 93
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYVPEDRKG-EGLvldlS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEE---LCYFGRHPHKKLLSKHTQEdhdmvEWALEATGMIELKDRTLDA----LSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:COG1129 347 IREnitLASLDRLSRGGLLDRRRER-----ALAEEYIKRLRIKTPSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190
....*....|....*....|....*....|
gi 489326441 167 TTYLDISHQIEVLELLKKLNRDhGRTVVMV 196
Cdd:COG1129 422 TRGIDVGAKAEIYRLIRELAAE-GKAVIVI 450
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-198 |
8.78e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 17 VIIDGVDLKIEEGKITALIGANGCGKSTILKSLA-RLMAP--KSGTVLLEGkdihRQPSKEVAKKLAILPQSPQAPEGLT 93
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAeRVTTGviTGGDRLVNG----RPLDSSFQRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYFG---RHPHKklLSKhtQEDHDMVEWALEATGMIELKDRTL----DALSGGQRQRAWISMALAQGTDLLL-LDE 165
Cdd:TIGR00956 853 VRESLRFSaylRQPKS--VSK--SEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190
....*....|....*....|....*....|...
gi 489326441 166 PTTYLDISHQIEVLELLKKLNrDHGRTVVMVLH 198
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-223 |
9.72e-14 |
|
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: 70.62 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYDST-VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIhRQPSKE-VAKKL 79
Cdd:COG5265 356 GEVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQAsLRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSpqapeglTV-------EELCYfGRhPHKkllskhTQEDhdmVEWALEAT---GMIE-LKD--------RTLDaL 140
Cdd:COG5265 435 GIVPQD-------TVlfndtiaYNIAY-GR-PDA------SEEE---VEAAARAAqihDFIEsLPDgydtrvgeRGLK-L 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 141 SGGQRQRAWISMALAQGTDLLLLDEPTTYLDiSH-QIEVLELLKKLNRdhGRTVVMVLHDLNQAAqYADyLISVLD-GKI 218
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALD-SRtERAIQAALREVAR--GRTTLVIAHRLSTIV-DAD-EILVLEaGRI 570
|
....*
gi 489326441 219 YNAGT 223
Cdd:COG5265 571 VERGT 575
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-216 |
2.44e-13 |
|
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: 67.46 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLL----EGKDIHRQPSKEVakkLAILPQspqapegltv 94
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREI---LALRRR---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 eELCY---FGRH-PHKKLLskhtqedhDMVEWALEATGM--IELKDRTLDAL-----------------SGGQRQRAWIS 151
Cdd:COG4778 94 -TIGYvsqFLRViPRVSAL--------DVVAEPLLERGVdrEEARARARELLarlnlperlwdlppatfSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYLISVLDG 216
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-198 |
3.25e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 9 LTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSgtvlleGKDIHRQPSKEVAKKLAILPQSPQa 88
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP------VAGCVDVPDNQFGREASLIDAIGR- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 89 pegltveelcyfgrhphkkllskhtqeDHDMVEwALEATGMIELKD-----RTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:COG2401 109 ---------------------------KGDFKD-AVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLH 198
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-236 |
3.86e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGlTVEel 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TVR-- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 cyFGRHPhkklLSKHTqeDHDMVEwALEATGMIELKDRT---LDA--------LSGGQRQRAWISMALAQGTDLLLLDEP 166
Cdd:PLN03232 1328 --FNIDP----FSEHN--DADLWE-ALERAHIKDVIDRNpfgLDAevseggenFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 167 TTYLDishqIEVLELLKKLNRDHGRTVVMVL--HDLNQAAQyADYLISVLDGKIYNAGTPEDVF---TQPFFREV 236
Cdd:PLN03232 1399 TASVD----VRTDSLIQRTIREEFKSCTMLViaHRLNTIID-CDKILVLSSGQVLEYDSPQELLsrdTSAFFRMV 1468
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-204 |
4.72e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIhrqpskeVAKKLAI---- 81
Cdd:NF033858 269 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-------DAGDIATrrrv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 --LPQSPQAPEGLTVE---ELcyfgrhpHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRawISMALA- 155
Cdd:NF033858 342 gyMSQAFSLYGELTVRqnlEL-------HARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQR--LSLAVAv 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489326441 156 -QGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAA 204
Cdd:NF033858 413 iHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAE 462
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
8-209 |
7.25e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 7.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 8 QLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKeVAKKLAILPQSPQ 87
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT-YQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 APEGLTVEELCYFGRHphkklLSKHTQEDHDMVE-WALEatgmiELKDRTLDALSGGQRQ-----RAWISmalaqGTDLL 161
Cdd:PRK13540 85 INPYLTLRENCLYDIH-----FSPGAVGITELCRlFSLE-----HLIDYPCGLLSSGQKRqvallRLWMS-----KAKLW 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489326441 162 LLDEPTTYLDishQIEVLELLKKL--NRDHGRTVVMVLHD---LNQaAQYADY 209
Cdd:PRK13540 150 LLDEPLVALD---ELSLLTIITKIqeHRAKGGAVLLTSHQdlpLNK-ADYEEY 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-198 |
2.52e-12 |
|
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: 63.33 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTL-SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVllegkDIHRQPskevakKLAIL 82
Cdd:cd03223 1 IELENLSLaTPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMPEGE------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 83 PQSPQAPEGLTVEELCYfgrhPhkkllskhtqedhdmveWAleatgmielkdrtlDALSGGQRQRawISMA--LAQGTDL 160
Cdd:cd03223 70 PQRPYLPLGTLREQLIY----P-----------------WD--------------DVLSGGEQQR--LAFArlLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 489326441 161 LLLDEPTTYLDISHQIEVLELLKklnrDHGRTVVMVLH 198
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-242 |
2.57e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 17 VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEgkdihrqpskevaKKLAILPQSPQAPEGLTVEE 96
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 97 LCYFgrhphkkllskhTQED----HDMVEWA-LEA------TGM-IELKDRTLDaLSGGQRQRAWISMALAQGTDLLLLD 164
Cdd:PTZ00243 741 ILFF------------DEEDaarlADAVRVSqLEAdlaqlgGGLeTEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 165 EPTTYLD--ISHQIeVLELLkkLNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVFTQPFFREVFGLECC 242
Cdd:PTZ00243 808 DPLSALDahVGERV-VEECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLAAELKE 883
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-219 |
2.98e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHrqpskevakklailPQSPQAPEGLTVEELCYFg 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT--------------AEQPEDYRKLFSAVFTDF- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 102 rHPHKKLL-SKHTQEDHDMVEWALEATGM---IELKD-RTLD-ALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQ 175
Cdd:PRK10522 407 -HLFDQLLgPEGKPANPALVEKWLERLKMahkLELEDgRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489326441 176 IEVLELLKKLNRDHGRTVVMVLHDlNQAAQYADYLISVLDGKIY 219
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-226 |
3.40e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVllegkdihrqpsK--EVAkKLAI 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KwsENA-NIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQ--SPQAPEGLTVEElcyfgrhphkkLLSKHTQEDHDmvEWALEAT------GMIELKdRTLDALSGGQRQRAWISMA 153
Cdd:PRK15064 387 YAQdhAYDFENDLTLFD-----------WMSQWRQEGDD--EQAVRGTlgrllfSQDDIK-KSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 154 LAQGTDLLLLDEPTTYLDIsHQIEVLEL-LKKLNrdhGrTVVMVLHDLNQAAQYADYLISVLDGKIYN-AGTPED 226
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDM-ESIESLNMaLEKYE---G-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-217 |
3.51e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.97 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 20 DGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKS--GTVLLEG-----KDIHRqpSKEVA-----KKLAILPQspq 87
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRD--SEALGiviihQELALIPY--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 88 apegLTVEELCYFGRHPHKKLL------SKHTQEdhdmvewALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLL 161
Cdd:NF040905 93 ----LSIAENIFLGNERAKRGVidwnetNRRARE-------LLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADYlISVL-DGK 217
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADS-ITVLrDGR 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-223 |
3.90e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.12 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGkdihrqpskevakKLAILPQspQA-PEGLTVEEL 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQ--QAwIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CYFGrHPHKKLLSKHTQE------DHDMvewaLEATGMIELKDRTLDaLSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:TIGR00957 719 ILFG-KALNEKYYQQVLEacallpDLEI----LPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 172 -------ISHQIEVLELLKklnrdhGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGT 223
Cdd:TIGR00957 793 ahvgkhiFEHVIGPEGVLK------NKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGS 844
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-231 |
3.92e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.21 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLA-------RLMAPKsgtvlLEGKDIH------RQPSKEVAKKLAILPQS 85
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwRVTADR-----MRFDDIDllrlspRERRKLVGHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQA---PEGLTVEEL-------CYFGR-----HPHKK----LLSKHTQEDHD--MVEWALEatgmielkdrtldaLSGGQ 144
Cdd:PRK15093 98 PQScldPSERVGRQLmqnipgwTYKGRwwqrfGWRKRraieLLHRVGIKDHKdaMRSFPYE--------------LTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 145 RQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTP 224
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
....*..
gi 489326441 225 EDVFTQP 231
Cdd:PRK15093 244 KELVTTP 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-238 |
5.94e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI-HRQPSKEVAKKLAILPQSPQ-------APEGLT 93
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInALSTAQRLARGLVYLPEDRQssglyldAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYfgrhpHKKLLSKHTQEDHDMVEWALEATGM-IELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDI 172
Cdd:PRK15439 362 VCALTH-----NRRGFWIKPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 173 SHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQPFFREVFG 238
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-229 |
7.76e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGLTVEEL 97
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CYFGRHphkkllskhtqEDHDMVEwALEATgmiELKD------RTLDA--------LSGGQRQRAWISMALAQGTDLLLL 163
Cdd:PLN03130 1334 DPFNEH-----------NDADLWE-SLERA---HLKDvirrnsLGLDAevseagenFSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 164 DEPTTYLDISHQIevleLLKKLNRDHGRTVVMVL--HDLNQAAQyADYLIsVLD-GKIYNAGTPEDVFT 229
Cdd:PLN03130 1399 DEATAAVDVRTDA----LIQKTIREEFKSCTMLIiaHRLNTIID-CDRIL-VLDaGRVVEFDTPENLLS 1461
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-227 |
8.84e-12 |
|
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: 64.82 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 7 DQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKslarlmapksgtvLLEGKDIHRQPSKEVAKKLAILP--- 83
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-------------VLRGMDQYEPTSGRIIYHVALCEkcg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 ----------QSPQAPEGLTVEELCYFG-RHPHKKLLSKHTQ----------------------------EDHDMVEWAL 124
Cdd:TIGR03269 71 yverpskvgePCPVCGGTLEPEEVDFWNlSDKLRRRIRKRIAimlqrtfalygddtvldnvlealeeigyEGKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 125 EATGMIELKDRTLDA---LSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLN 201
Cdd:TIGR03269 151 DLIEMVQLSHRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 489326441 202 QAAQYADYLISVLDGKIYNAGTPEDV 227
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-192 |
1.27e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRqpsKEVAKKLAILP 83
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 QSPQAPEGLTVEELCYF-----GRHPHKkllskhtqedhdMVEWALEATGMIELKDRTLDALSGGQRQR-----AWISMA 153
Cdd:PRK13543 89 HLPGLKADLSTLENLHFlcglhGRRAKQ------------MPGSALAIVGLAGYEDTLVRQLSAGQKKRlalarLWLSPA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 489326441 154 laqgtDLLLLDEPTTYLDishqIEVLELLKKLNRDHGRT 192
Cdd:PRK13543 157 -----PLWLLDEPYANLD----LEGITLVNRMISAHLRG 186
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-230 |
1.38e-11 |
|
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: 64.58 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 14 DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGLT 93
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 94 VEELCYFGrhphkkllsKHTQEDhdmVEWALEAT---GMIELKDRTLD--------ALSGGQRQRAWISMALAQGTDLLL 162
Cdd:TIGR00957 1377 RMNLDPFS---------QYSDEE---VWWALELAhlkTFVSALPDKLDhecaeggeNLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 163 LDEPTTYLDishqIEVLELLKKLNRDHGR--TVVMVLHDLNQAAQYADYLisVLD-GKIYNAGTPEDVFTQ 230
Cdd:TIGR00957 1445 LDEATAAVD----LETDNLIQSTIRTQFEdcTVLTIAHRLNTIMDYTRVI--VLDkGEVAEFGAPSNLLQQ 1509
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-205 |
1.79e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 17 VIIDGVDLKIEEG-KItALIGANGCGKSTILKSLARLMAPKSG-TVLLEGkdihrqpskevaKKLAILPQSPQAPEGLTV 94
Cdd:PRK11819 21 QILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPG------------IKVGYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELCYFGRHPHKKLLS-------KHTQEDHDM---------VEWALEATGMIELkDRTL----DAL------------SG 142
Cdd:PRK11819 88 RENVEEGVAEVKAALDrfneiyaAYAEPDADFdalaaeqgeLQEIIDAADAWDL-DSQLeiamDALrcppwdakvtklSG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 143 GQRQRAWISMALAQGTDLLLLDEPTTYLDishqIEVLELLKKLNRDHGRTVVMVLHD---LNQAAQ 205
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHDryfLDNVAG 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-199 |
1.80e-11 |
|
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: 63.80 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLeGKDIhrqpskevakKLAILPQS 85
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEG-LTV-EELcyfgrhphkkllskhtQEDHDMVEwaleaTGMIELKDRT---------------LDALSGGQRQRA 148
Cdd:TIGR03719 394 RDALDPnKTVwEEI----------------SGGLDIIK-----LGKREIPSRAyvgrfnfkgsdqqkkVGQLSGGERNRV 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489326441 149 WISMALAQGTDLLLLDEPTTYLDishqIEVLELLKKLNRDHGRTVVMVLHD 199
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD 499
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-218 |
1.88e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTL-SYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEV-AKKLAI 81
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 82 LPQSPQApEGL----TVEELCYFGRHpHKKLLSKHTQEDHD-MVEWALEA-------TGMIELKDRtldALSGGQRQRAW 149
Cdd:COG3845 338 IPEDRLG-RGLvpdmSVAENLILGRY-RRPPFSRGGFLDRKaIRAFAEELieefdvrTPGPDTPAR---SLSGGNQQKVI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 150 ISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQYADyLISVL-DGKI 218
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSD-RIAVMyEGRI 480
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-218 |
2.32e-11 |
|
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: 61.51 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPK---SGTVL---LEGKDIHRQPSKEVAkklaILPQSPQAPEG 91
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHyngIPYKEFAEKYPGEII----YVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 92 LTVEELCYFgrhphkkllskhtqedhdmvewALEATGmielkDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLD 171
Cdd:cd03233 98 LTVRETLDF----------------------ALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489326441 172 ISHQIEVLELLKKLNRDHGRTVVMVLHdlnQAAQ--YA--DYLISVLDGKI 218
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTFVSLY---QASDeiYDlfDKVLVLYEGRQ 198
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-234 |
1.39e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGK---DIHRQPSkevakklaiLPqspqaPE----GLTV 94
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGIC---------LP-----PEkrriGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EELCYFgrhPHKKL-------LSKHTQEDHDMVewaLEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:PRK11144 83 QDARLF---PHYKVrgnlrygMAKSMVAQFDKI---VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 168 TYLDISHQIEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLIsVLD-GKIYNAGTPEDVFTQPFFR 234
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVV-VLEqGKVKAFGPLEEVWASSAMR 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-208 |
3.12e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEG----KDIHRqpsKEVAKKLAILPQSP------- 86
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINL---KWWRSKIGVVSQDPllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 --------------QAPEGLTVEE--LCYFGRHPHKKLLSKHTQEDHDMVEwALEATGMIELKD--RTLD---------- 138
Cdd:PTZ00265 477 knnikyslyslkdlEALSNYYNEDgnDSQENKNKRNSCRAKCAGDLNDMSN-TTDSNELIEMRKnyQTIKdsevvdvskk 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 139 -----------------------ALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVM 195
Cdd:PTZ00265 556 vlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 635
|
250
....*....|...
gi 489326441 196 VLHDLNqAAQYAD 208
Cdd:PTZ00265 636 IAHRLS-TIRYAN 647
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
12-213 |
4.92e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 57.62 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDgvdlkIEEGkITALIGANGCGKSTILK----SLARLMAPKSGTVLLEGKDIHRQPSK-------------- 73
Cdd:cd03240 11 SFHERSEIE-----FFSP-LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIREGEVRaqvklafenangkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 74 -EVAKKLAILpqspqapegltveELCYFGRhphkkllskhtQEDHDmveWALEatgmielkdRTLDALSGGQRQRAWISM 152
Cdd:cd03240 85 yTITRSLAIL-------------ENVIFCH-----------QGESN---WPLL---------DMRGRCSGGEKVLASLII 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489326441 153 ALA------QGTDLLLLDEPTTYLDISHQIEVL-ELLKKLNRDHGRTVVMVLHDlNQAAQYADYLISV 213
Cdd:cd03240 129 RLAlaetfgSNCGILALDEPTTNLDEENIEESLaEIIEERKSQKNFQLIVITHD-EELVDAADHIYRV 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-223 |
5.09e-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: 59.92 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 11 LSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKsgtvllEGKDIHrqpskevAKKLAILPQSPQAPE 90
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS------EGKIKH-------SGRISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 91 GlTVEELCYFG-RHPHKKLLS--KHTQEDHDMVEWALeatgmielKDRTL-----DALSGGQRQRAWISMALAQGTDLLL 162
Cdd:TIGR01271 501 G-TIKDNIIFGlSYDEYRYTSviKACQLEEDIALFPE--------KDKTVlgeggITLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 163 LDEPTTYLDISHQIEVLE-LLKKLNRDHGRTVVMV-LHDLNQaaqyADYLISVLDGKIYNAGT 223
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFEsCLCKLMSNKTRILVTSkLEHLKK----ADKILLLHEGVCYFYGT 630
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
12-214 |
6.69e-10 |
|
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: 56.60 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 12 SYDSTVIIDGVdlkieEGKITALIGANGCGKSTILKSLArlmapksgtvLLEGKDIHRQPSKEVAKklailpqsPQAPEG 91
Cdd:cd03227 9 SYFVPNDVTFG-----EGSLTIITGPNGSGKSTILDAIG----------LALGGAQSATRRRSGVK--------AGCIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 92 LTVEELCYfgrhphkkllskhtqedhdmvewaleatgmielkdrTLDALSGGQRQRAWISMALA----QGTDLLLLDEPT 167
Cdd:cd03227 66 AVSAELIF------------------------------------TRLQLSGGEKELSALALILAlaslKPRPLYILDEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489326441 168 TYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLNQAAQyADYLISVL 214
Cdd:cd03227 110 RGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAEL-ADKLIHIK 154
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-217 |
6.79e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.81 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 26 IEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEvakklailpqspqapegltveelcyfgrhph 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 106 kkllskhtqedhdmvewaleatgmielkdrtldALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKL 185
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|..
gi 489326441 186 NRDHGRTVVMVLHDLNQAAQYADYLIsVLDGK 217
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIH-VFEGE 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-202 |
7.89e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVllegkdihrqpSKEVAKKLAILPQSPQAPEGLTVEELCYFG 101
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----------SLDPNERLGKLRQDQFAFEEFTVLDTVIMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 102 rhpHKKL------------LSKHTQEDHDMV--------------------EWALEATGMIELKDRTLDALSGGQRQRAW 149
Cdd:PRK15064 89 ---HTELwevkqerdriyaLPEMSEEDGMKVadlevkfaemdgytaearagELLLGVGIPEEQHYGLMSEVAPGWKLRVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 150 ISMALAQGTDLLLLDEPTTYLDIsHQIEVLE-LLKKLNrdhgRTVVMVLHD---LNQ 202
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLDI-NTIRWLEdVLNERN----STMIIISHDrhfLNS 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-218 |
1.30e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLegkdihrqpskevAKKLailp 83
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-------------AKGI---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 84 qspqapegltveELCYFGRHPHKKLLSKHTQEDHdMVEWALEAT---------GMIELKDRTLDA---LSGGQRQRAWIS 151
Cdd:PRK10636 376 ------------KLGYFAQHQLEFLRADESPLQH-LARLAPQELeqklrdylgGFGFQGDKVTEEtrrFSGGEKARLVLA 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 152 MALAQGTDLLLLDEPTTYLDISHQIEVLELLKklnrDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALI----DFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-227 |
1.64e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 58.10 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 140 LSGGQRQRAWISMAL---AQGTDLLLLDEPTTYL---DISHQIEVLELLkklnRDHGRTVVMVLHDLNQAAQyADYLIS- 212
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDIKKLLEVLQRL----VDKGNTVVVIEHNLDVIKT-ADYIIDl 904
|
90 100
....*....|....*....|
gi 489326441 213 -----VLDGKIYNAGTPEDV 227
Cdd:TIGR00630 905 gpeggDGGGTVVASGTPEEV 924
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-218 |
1.67e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 21 GVDLkieEGKItALIGANGCGKSTILKSLARLMAPKSGTVLLEGKdihrqpskevaKKLAILPQSPQAPEGLTVEELCYF 100
Cdd:PLN03073 531 GIDL---DSRI-AMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-----------VRMAVFSQHHVDGLDLSSNPLLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 101 GR----HPHKKLLSkHTQedhdmvewALEATGMIELKdrTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDIShqi 176
Cdd:PLN03073 596 MRcfpgVPEQKLRA-HLG--------SFGVTGNLALQ--PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD--- 661
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489326441 177 EVLELLKKLNRDHGrTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:PLN03073 662 AVEALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
140-227 |
2.30e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 57.73 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 140 LSGGQRQRawISMAL-----AQGTDLLLLDEPTTYL---DISHQIEVLELLkklnRDHGRTVVMVLHDLNQAAQyADYLI 211
Cdd:COG0178 827 LSGGEAQR--VKLASelskrSTGKTLYILDEPTTGLhfhDIRKLLEVLHRL----VDKGNTVVVIEHNLDVIKT-ADWII 899
|
90 100
....*....|....*....|....*
gi 489326441 212 svlD---------GKIYNAGTPEDV 227
Cdd:COG0178 900 ---DlgpeggdggGEIVAEGTPEEV 921
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-217 |
2.53e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKE--------VAKKLAILPQspqape 90
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagigiIHQELNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 91 gLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTtyl 170
Cdd:PRK10762 94 -LTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT--- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489326441 171 DISHQIEVLELLKKLN--RDHGRTVVMVLHDLNQAAQYADYlISVL-DGK 217
Cdd:PRK10762 170 DALTDTETESLFRVIRelKSQGRGIVYISHRLKEIFEICDD-VTVFrDGQ 218
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
140-227 |
3.30e-09 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 57.00 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 140 LSGGQRQRawisMALAQ-------GTDLLLLDEPTTYL---DISHQIEVLELLkklnRDHGRTVVMVLHDL----Nqaaq 205
Cdd:PRK00349 831 LSGGEAQR----VKLAKelskrstGKTLYILDEPTTGLhfeDIRKLLEVLHRL----VDKGNTVVVIEHNLdvikT---- 898
|
90 100 110
....*....|....*....|....*....|.
gi 489326441 206 yADYLIsvlD---------GKIYNAGTPEDV 227
Cdd:PRK00349 899 -ADWII---DlgpeggdggGEIVATGTPEEV 925
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-240 |
3.40e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.02 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKdihrqpskevakkLAILPQSPQAPEGlTVEEL 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 98 CYFG----RHPHKKLLsKHTQEDHDMVEWALeatgmielKDRTLDA-----LSGGQRQRAWISMALAQGTDLLLLDEPTT 168
Cdd:cd03291 118 IIFGvsydEYRYKSVV-KACQLEEDITKFPE--------KDNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 169 YLDISHQIEVLE-LLKKLNRDhgRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGT-PEDVFTQP-FFREVFGLE 240
Cdd:cd03291 189 YLDVFTEKEIFEsCVCKLMAN--KTRILVTSKMEHLKK-ADKILILHEGSSYFYGTfSELQSLRPdFSSKLMGYD 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-218 |
3.50e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH-RQPSKEVAKKLAILPQSPQapegltveELCYF 100
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITESRR--------DNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 101 GRHPHKKLLSKHTQ-------------EDHDMVEWALEATGMIELK----DRTLDALSGGQRQRAWISMALAQGTDLLLL 163
Cdd:PRK09700 354 PNFSIAQNMAISRSlkdggykgamglfHEVDEQRTAENQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 164 DEPTTYLDISHQIEVLELLKKLNrDHGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-219 |
3.94e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 29 GKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAIlpqspqapegltveelcyfgrhphkkl 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 109 lskhtqedhdmvewaleatgmielkDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLEL-----LK 183
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180 190
....*....|....*....|....*....|....*.
gi 489326441 184 KLNRDHGRTVVMVLHDLNQAAqyADYLISVLDGKIY 219
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIV 143
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-230 |
7.14e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 54.91 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSYDSTV--IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:cd03288 18 GEIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTveelcYFGRHPHKKLLskhtqedhDMVEWalEATGMIELKDRT------LDAL--------SGGQR 145
Cdd:cd03288 98 SIILQDPILFSGSI-----RFNLDPECKCT--------DDRLW--EALEIAQLKNMVkslpggLDAVvteggenfSVGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 146 QRAWISMALAQGTDLLLLDEPTTYLDISHQievlELLKK--LNRDHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGT 223
Cdd:cd03288 163 QLFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDT 237
|
....*..
gi 489326441 224 PEDVFTQ 230
Cdd:cd03288 238 PENLLAQ 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-231 |
7.14e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQA---PEGLTVEELC 98
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTslnPRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 99 YfgrhPHKKLLSKHTQEDHDMVEWALEATGMieLKDRTL---DALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQ 175
Cdd:PRK15112 112 F----PLRLNTDLEPEQREKQIIETLRQVGL--LPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489326441 176 IEVLELLKKLNRDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQP 231
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-218 |
1.15e-08 |
|
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: 55.19 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDI-------HRQpskevakkL--AILPQspqapegl 92
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtadnreaYRQ--------LfsAVFSD-------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 93 tveelcyFgrHPHKKLLSKHTQEDHDMVEWALEATGM---IELKDRTLD--ALSGGQRQR-AWIsMALAQGTDLLLLDE- 165
Cdd:COG4615 415 -------F--HLFDRLLGLDGEADPARARELLERLELdhkVSVEDGRFSttDLSQGQRKRlALL-VALLEDRPILVFDEw 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 166 -----PtTYLDISHQiEVLELLKKLnrdhGRTVVMVLHDlnqaAQY---ADYLISVLDGKI 218
Cdd:COG4615 485 aadqdP-EFRRVFYT-ELLPELKAR----GKTVIAISHD----DRYfdlADRVLKMDYGKL 535
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-172 |
1.36e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 6 ADQLTLSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLeGKDIhrqpskevakKLAILPQS 85
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 pqaPEGL----TV-EELcyfgrhphkkllskhtQEDHDMVEwaleaTGMIELKDRT---------------LDALSGGQR 145
Cdd:PRK11819 396 ---RDALdpnkTVwEEI----------------SGGLDIIK-----VGNREIPSRAyvgrfnfkggdqqkkVGVLSGGER 451
|
170 180
....*....|....*....|....*..
gi 489326441 146 QRAWISMALAQGTDLLLLDEPTTYLDI 172
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-218 |
2.35e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 22 VDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH-RQPSKEVAKKLAILPQSPQApEGL----TVEE 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPEDRKA-EGIipvhSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 97 ---LCYFGRHPHKKLLSKHTQEDhdmvEWALEATGMIELKDRTLD----ALSGGQRQRAWISMALAQGTDLLLLDEPTTY 169
Cdd:PRK11288 351 ninISARRHHLRAGCLINNRWEA----ENADRFIRSLNIKTPSREqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489326441 170 LDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-230 |
2.50e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 1 MGKLAADQLT--LSYDSTVIIDgvDLKIEEGKITALIGANGCGKStilkSLARLMAPKsgTVLLEGkdiHRQpskevakk 78
Cdd:PRK10938 1 MSSLQISQGTfrLSDTKTLQLP--SLTLNAGDSWAFVGANGSGKS----ALARALAGE--LPLLSG---ERQ-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 79 lailpQSPQAPEGLTVEELcyfgrhphKKLLSKHTQE-DHDMVEWALEATG-----MIE--------------------L 132
Cdd:PRK10938 62 -----SQFSHITRLSFEQL--------QKLVSDEWQRnNTDMLSPGEDDTGrttaeIIQdevkdparceqlaqqfgitaL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 133 KDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRdHGRTVVMVLHDLNQAAQYADYlIS 212
Cdd:PRK10938 129 LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQF-AG 206
|
250
....*....|....*....
gi 489326441 213 VL-DGKIYNAGTPEDVFTQ 230
Cdd:PRK10938 207 VLaDCTLAETGEREEILQQ 225
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-227 |
2.93e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 54.25 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 134 DRTLDALSGGQRQRawISMALAQGTDLL----LLDEPTTYLdisHQIEVLELLKKLN--RDHGRTVVMVLHDlNQAAQYA 207
Cdd:TIGR00630 483 SRAAGTLSGGEAQR--IRLATQIGSGLTgvlyVLDEPSIGL---HQRDNRRLINTLKrlRDLGNTLIVVEHD-EDTIRAA 556
|
90 100
....*....|....*....|....*.
gi 489326441 208 DYLIS------VLDGKIYNAGTPEDV 227
Cdd:TIGR00630 557 DYVIDigpgagEHGGEVVASGTPEEI 582
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-211 |
3.12e-08 |
|
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: 51.94 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 134 DRTLDALSGGQRQRAWISMALAQGTD--LLLLDEPTTYLdisHQIEVLELLKKLNR--DHGRTVVMVLHDLnQAAQYADY 209
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL---HQQDINQLLEVIKGliDLGNTVILIEHNL-DVLSSADW 157
|
..
gi 489326441 210 LI 211
Cdd:cd03238 158 II 159
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
140-224 |
3.45e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.00 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 140 LSGGQRQRAWISMAL---AQGTDLLLLDEPTTYL---DISHQIEVLELLkklnRDHGRTVVMVLHDLNQAAQyADYLIS- 212
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfhDVKKLLEVLQRL----VDKGNTVVVIEHNLDVIKC-ADWIIDl 244
|
90
....*....|....*..
gi 489326441 213 -----VLDGKIYNAGTP 224
Cdd:cd03271 245 gpeggDGGGQVVASGTP 261
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
134-213 |
5.97e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.87 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 134 DRTLDALSGGQRQRawISMALAQGTDLL----LLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDLnQAAQYADY 209
Cdd:cd03270 132 SRSAPTLSGGEAQR--IRLATQIGSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADH 207
|
....
gi 489326441 210 LISV 213
Cdd:cd03270 208 VIDI 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-218 |
6.03e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPK-SGTVLLEGKDIH-RQPSKEVAKKLAILPQS-------PQAP 89
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 90 EG--LTVEELCYFgrhphkkllSKHTQEDHDMVEWALEAtGMIELKDRT------LDALSGGQRQRAWISMALAQGTDLL 161
Cdd:TIGR02633 356 VGknITLSVLKSF---------CFKMRIDAAAELQIIGS-AIQRLKVKTaspflpIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 162 LLDEPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-237 |
7.88e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:PRK10789 312 GELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGlTVEELCYFGRhphkkllSKHTQED----------HDMVeWALEATGMIELKDRTLdALSGGQRQRAW 149
Cdd:PRK10789 392 AVVSQTPFLFSD-TVANNIALGR-------PDATQQEiehvarlasvHDDI-LRLPQGYDTEVGERGV-MLSGGQKQRIS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 150 ISMALAQGTDLLLLDEPTTYLD--ISHQIevlelLKKLNR-DHGRTVVMVLHDLNqAAQYADYLISVLDGKIYNAGTPED 226
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDgrTEHQI-----LHNLRQwGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQ 535
|
250
....*....|..
gi 489326441 227 VFTQP-FFREVF 237
Cdd:PRK10789 536 LAQQSgWYRDMY 547
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-194 |
9.21e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 52.31 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGkITALIGANGCGKSTILKSLARLMAPKSGTVlLEGKDIHRQ-----PSKEVA-------KKLAILPQSP 86
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRK-FDEEDFYLGddpdlPEIEIEltfgsllSRLLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAPEGLT--VEELcyfgrhphKKLLSKHTQE-----DHDMVEWALEATGMIELKDRTLDALSG----------------- 142
Cdd:COG3593 92 EDKEELEeaLEEL--------NEELKEALKAlnellSEYLKELLDGLDLELELSLDELEDLLKslslriedgkelpldrl 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489326441 143 GQRQRAWISMALAQ---------GTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVV 194
Cdd:COG3593 164 GSGFQRLILLALLSalaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-235 |
1.68e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 17 VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPSKEVAKKLAILPQSPQAPEGlTVee 96
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TV-- 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 97 lcyfgRHPHKKLLSKHTQEdhdmVEWALEATGMIE--------LKDRTLDA---LSGGQRQRAWISMA-LAQGTDLLLLD 164
Cdd:PTZ00243 1401 -----RQNVDPFLEASSAE----VWAALELVGLRErvasesegIDSRVLEGgsnYSVGQRQLMCMARAlLKKGSGFILMD 1471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 165 EPTTYLD--ISHQIE--VLELLKklnrdhGRTVVMVLHDLNQAAQYaDYLISVLDGKIYNAGTPEDVF--TQPFFRE 235
Cdd:PTZ00243 1472 EATANIDpaLDRQIQatVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVmnRQSIFHS 1541
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-228 |
1.76e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 11 LSYDSTV---IIDGVDLKIEEGKITALIGANGCGKSTILKS-LARLMAPKSGTVLLEGKdihrqpskevakkLAILPQSP 86
Cdd:PLN03232 622 FSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGS-------------VAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 87 QAPEGlTVEELCYFGRHPH-----KKLLSKHTQEDHDMvewaLEATGMIELKDRTLDaLSGGQRQRAWISMALAQGTDLL 161
Cdd:PLN03232 689 WIFNA-TVRENILFGSDFEserywRAIDVTALQHDLDL----LPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 162 LLDEPTTYLD--ISHQIEVLELLKKLnrdHGRTVVMVLHDLNQAAQyADYLISVLDGKIYNAGTPEDVF 228
Cdd:PLN03232 763 IFDDPLSALDahVAHQVFDSCMKDEL---KGKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFAELS 827
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-198 |
2.25e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 29 GKITALIGANGCGKSTILKSLArlmAPKSGTVLLEGKDIHRQPSKE--VAKKLAILPQ----SPQapegLTVEE-LCY-- 99
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLA---GRKTGGYIEGDIRISGFPKKQetFARISGYCEQndihSPQ----VTVREsLIYsa 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 100 FGRHPhkKLLSKhtQEDHDMVEWALEATGMIELKDRT-----LDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISH 174
Cdd:PLN03140 979 FLRLP--KEVSK--EEKMMFVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180
....*....|....*....|....
gi 489326441 175 QIEVLELLKKlNRDHGRTVVMVLH 198
Cdd:PLN03140 1055 AAIVMRTVRN-TVDTGRTVVCTIH 1077
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
19-230 |
2.26e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCgkstilkSLARLMAPKSgtvlLEGKDIHRQP-------SKEVAKKLAILPQSPQAP-- 89
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GA-------A**RGALPAH----V*GPDAGRRPwrf*twcANRRALRRTIG*HRPVR*gr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 90 -EGLTVEELCYF-GRHphkklLSKHTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPT 167
Cdd:NF000106 98 rESFSGRENLYMiGR*-----LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489326441 168 TYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-199 |
2.41e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 17 VIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKdihrqpskevaKKLAILPQSPQApegLTVEE 96
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-----------WQLAWVNQETPA---LPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 97 LCYF--GRHPHKKLLSK--HTQEDHD-------------MVEWALEATGMIELK---------DRTLDALSGGQRQRAWI 150
Cdd:PRK10636 81 LEYVidGDREYRQLEAQlhDANERNDghaiatihgkldaIDAWTIRSRAASLLHglgfsneqlERPVSDFSGGWRMRLNL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489326441 151 SMALAQGTDLLLLDEPTTYLDISHQIevleLLKKLNRDHGRTVVMVLHD 199
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVI----WLEKWLKSYQGTLILISHD 205
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-226 |
2.50e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 134 DRTLDALSGGQRQRAwismALAQ--GTDLL----LLDEPTTYLDISHQIEVLELLKKLnRDHGRTVVMVLHDlNQAAQYA 207
Cdd:PRK00635 471 ERALATLSGGEQERT----ALAKhlGAELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMISLA 544
|
90 100
....*....|....*....|....*
gi 489326441 208 DYLISV------LDGKIYNAGTPED 226
Cdd:PRK00635 545 DRIIDIgpgagiFGGEVLFNGSPRE 569
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-227 |
4.63e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 134 DRTLDALSGGQRQRawISMALAQGTDLL----LLDEPTTYLdisHQ------IEVLellKKLnRDHGRTVVMVLHDLnQA 203
Cdd:COG0178 480 DRSAGTLSGGEAQR--IRLATQIGSGLVgvlyVLDEPSIGL---HQrdndrlIETL---KRL-RDLGNTVIVVEHDE-DT 549
|
90 100 110
....*....|....*....|....*....|
gi 489326441 204 AQYADYLI------SVLDGKIYNAGTPEDV 227
Cdd:COG0178 550 IRAADYIIdigpgaGEHGGEVVAQGTPEEI 579
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-176 |
6.24e-07 |
|
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: 49.47 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 2 GKLAADQLTLSY--DSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKsGTVLLEGKDIHRQPSKEVAKKL 79
Cdd:cd03289 1 GQMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 80 AILPQSPQAPEGLTVEELCYFGRHPHKKL--------LSKHTQEDHDMVEWALEATGMIelkdrtldaLSGGQRQRAWIS 151
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIwkvaeevgLKSVIEQFPGQLDFVLVDGGCV---------LSHGHKQLMCLA 150
|
170 180
....*....|....*....|....*.
gi 489326441 152 MALAQGTDLLLLDEPTTYLD-ISHQI 176
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDpITYQV 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-226 |
6.45e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 10 TLSYDSTV---IIDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKS-GTVLLEGKdihrqpskevakkLAILPQS 85
Cdd:PLN03130 621 YFSWDSKAerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------VAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 PQAPEGlTVEELCYFGrhphkkllskhTQEDHDMVEWALEATGM------------IELKDRTLDaLSGGQRQRAWISMA 153
Cdd:PLN03130 688 SWIFNA-TVRDNILFG-----------SPFDPERYERAIDVTALqhdldllpggdlTEIGERGVN-ISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489326441 154 LAQGTDLLLLDEPTTYLDISHQIEVLEllKKLNRD-HGRTVVMV---LHDLNQaaqyADYLISVLDGKIYNAGTPED 226
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVtnqLHFLSQ----VDRIILVHEGMIKEEGTYEE 825
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-218 |
4.48e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH-RQPSKEVAKKLAILPQSPQAPE---GLTV 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRKRDGlvlGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 EE---LCYFGRHPHKKLLSKHTQEdhdmvewALEATGMIEL-------KDRTLDALSGGQRQRAWISMALAQGTDLLLLD 164
Cdd:PRK10762 348 KEnmsLTALRYFSRAGGSLKHADE-------QQAVSDFIRLfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489326441 165 EPTTYLDISHQIEVLELLKKLNRDhGRTVVMVLHDLNQAAQYADYLISVLDGKI 218
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-213 |
6.55e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 133 KDRTLDALSGGQRQ------RAWISMALAQGTDLLLLDEPTTYLDISHQIEVLEL----LKKLNRdhgrtVVMVLHD--L 200
Cdd:PRK03918 782 KERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDImeryLRKIPQ-----VIIVSHDeeL 856
|
90
....*....|...
gi 489326441 201 NQAaqyADYLISV 213
Cdd:PRK03918 857 KDA---ADYVIRV 866
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-252 |
1.01e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 135 RTLDALSGGQRQR---AWISMALAQGTDLLLLDEPTTYL---DISHQIEVLELLKklnrDHGRTVVMVLHDLNqAAQYAD 208
Cdd:PRK00635 805 RPLSSLSGGEIQRlklAYELLAPSKKPTLYVLDEPTTGLhthDIKALIYVLQSLT----HQGHTVVIIEHNMH-VVKVAD 879
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489326441 209 YLISV------LDGKIYNAGTPEDVFT---------QPFFREVFGLECCIMRSPIDQKP 252
Cdd:PRK00635 880 YVLELgpeggnLGGYLLASCSPEELIHlhtptakalRPYLSSPQELPYLPDPSPKPPVP 938
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-230 |
1.26e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKdihrqpskevAKKLAILPQSPQAPEGLTVEELc 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLNGQLTGIENIEL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 99 yfgrhphKKLLSKHTQED-HDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPttyLDISHQIE 177
Cdd:PRK13545 109 -------KGLMMGLTKEKiKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA---LSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 178 VLELLKKLN--RDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK13545 179 TKKCLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-230 |
1.78e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGtvllegkDIHRQPSKEVAKKLAILPQSPQAPEGLTVEELC 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-------KVDRNGEVSVIAISAGLSGQLTGIENIEFKMLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 99 Y-FGRHPHKKLLSKhtqedhdmvewALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPttyLDISHQIE 177
Cdd:PRK13546 113 MgFKRKEIKAMTPK-----------IIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA---LSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489326441 178 VLELLKKLN--RDHGRTVVMVLHDLNQAAQYADYLISVLDGKIYNAGTPEDVFTQ 230
Cdd:PRK13546 179 AQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-198 |
2.30e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 57 SGTVLLEGKDIHRQPSKEVAKKLAILPQSPQApEGLTVEELCYFGRHphkkllsKHTQEDHDMVEWALEATGMIELKDRT 136
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGKE-------DATREDVKRACKFAAIDEFIESLPNK 1347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 137 LD--------ALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLH 198
Cdd:PTZ00265 1348 YDtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-171 |
2.51e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 4 LAADQLTLSYDSTVIIDgVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIHRQPS---KEVAKKLA 80
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpycTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 81 ILPQspqapegLTVEElcyfgrhpHKKLLSKhTQEDHDMVEWALEATGMIELKDRTLDALSGGQRQRAWISMALAQGTDL 160
Cdd:PRK13541 81 LKLE-------MTVFE--------NLKFWSE-IYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170
....*....|.
gi 489326441 161 LLLDEPTTYLD 171
Cdd:PRK13541 145 WLLDEVETNLS 155
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
134-227 |
3.23e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 134 DRTLDALSGGQRQRawISMALAQGTDLL----LLDEPTTYLdisHQIE---VLELLKKLnRDHGRTVVMVLHDlNQAAQY 206
Cdd:PRK00349 484 SRSAGTLSGGEAQR--IRLATQIGSGLTgvlyVLDEPSIGL---HQRDndrLIETLKHL-RDLGNTLIVVEHD-EDTIRA 556
|
90 100
....*....|....*....|....*..
gi 489326441 207 ADYLIS------VLDGKIYNAGTPEDV 227
Cdd:PRK00349 557 ADYIVDigpgagVHGGEVVASGTPEEI 583
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
23-55 |
8.97e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.06 E-value: 8.97e-05
10 20 30
....*....|....*....|....*....|....*.
gi 489326441 23 DLKIE---EGKITALIGANGCGKSTILKSLARLMAP 55
Cdd:COG3950 16 DLEIDfdnPPRLTVLVGENGSGKTTLLEAIALALSG 51
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-213 |
2.77e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 138 DALSGGQRQ------RAWISMALAQGTD------LLLLDEPTTYLDISHQIEVLELLKKLnRDHG-RTVVMVLHDlNQAA 204
Cdd:PRK02224 780 EQLSGGERAlfnlslRCAIYRLLAEGIEgdaplpPLILDEPTVFLDSGHVSQLVDLVESM-RRLGvEQIVVVSHD-DELV 857
|
....*....
gi 489326441 205 QYADYLISV 213
Cdd:PRK02224 858 GAADDLVRV 866
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-198 |
4.68e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 4.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 131 ELKDRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDIsHQIEVLE--LLKklnrdHGRTVVMVLH 198
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAVLWLEtyLLK-----WPKTFIVVSH 399
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
15-52 |
6.24e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 6.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489326441 15 STVIIDG----VDLKIEEGKITALIGANGCGKSTILKSLARL 52
Cdd:COG4637 3 TRIRIKNfkslRDLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-52 |
8.06e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 8.06e-04
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
11-52 |
8.79e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.03 E-value: 8.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489326441 11 LSYDSTVIIDGVDLKIEEGKITALIGANGCGKSTILKSLARL 52
Cdd:COG1106 11 RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-196 |
2.42e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.76 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVDLKIEEGKITALIGANGCGKSTILKSL-----ARlmapKSGTVLLEGKDIH-RQPSKEVAKKLAILPQS------ 85
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR----WEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 86 -PQAPEG--LTVEELCYFgrhphkkllSKHTQEDHDMVEWALEaTGMIELKDRTLDA------LSGGQRQRAWISMALAQ 156
Cdd:PRK13549 353 vPVMGVGknITLAALDRF---------TGGSRIDDAAELKTIL-ESIQRLKVKTASPelaiarLSGGNQQKAVLAKCLLL 422
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489326441 157 GTDLLLLDEPTTYLDISHQIEVLELLKKLNRdHGRTVVMV 196
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVI 461
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
23-53 |
3.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.03 E-value: 3.22e-03
10 20 30
....*....|....*....|....*....|.
gi 489326441 23 DLKIEEGKITALIGANGCGKSTILKSLARLM 53
Cdd:COG4938 14 EAELELKPLTLLIGPNGSGKSTLIQALLLLL 44
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-190 |
4.59e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.17 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 19 IDGVDLKIEEGKITALIGANGCGKSTILKSLARLMAPKSGTVLLEGKDIH-RQPSKEVAKKLAILPQSPQAP---EGLTV 94
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINHGFALVTEERRSTgiyAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 95 E---ELCYFGRHPHKKLLSKHTQEDHDmVEWALEATGMIELKDRT-LDALSGGQRQRAWISMALAQGTDLLLLDEPTTYL 170
Cdd:PRK10982 344 GfnsLISNIRNYKNKVGLLDNSRMKSD-TQWVIDSMRVKTPGHRTqIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180
....*....|....*....|.
gi 489326441 171 DISHQIEVLELLKKL-NRDHG 190
Cdd:PRK10982 423 DVGAKFEIYQLIAELaKKDKG 443
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
18-132 |
5.65e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 36.98 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 18 IIDGVdlkIEEGKITALIGANGCGKSTILKSLARLMA-----------PKSGTVLL---EGkdihrqPSKEVAKKLAILP 83
Cdd:pfam13481 25 LIKGL---LPAGGLGLLAGAPGTGKTTLALDLAAAVAtgkpwlggprvPEQGKVLYvsaEG------PADELRRRLRAAG 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489326441 84 QSPQAPEGLTVEELCYFGRHPHKKLLSKHTQEDHDMVEWALEATGMIEL 132
Cdd:pfam13481 96 ADLDLPARLLFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVEDPDL 144
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
134-241 |
5.85e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489326441 134 DRTLDALSGGQRQRAWISMALAQGTDLLLLDEPTTYLDISHQIEVLELLKKLNRDHGRTVVMVLhdLNQAAQYADY---L 210
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSL--LQPAPETFDLfddI 408
|
90 100 110
....*....|....*....|....*....|.
gi 489326441 211 ISVLDGKIYNAGTPEDVFTqpFFrEVFGLEC 241
Cdd:PLN03140 409 ILLSEGQIVYQGPRDHILE--FF-ESCGFKC 436
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
23-49 |
6.88e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 6.88e-03
10 20
....*....|....*....|....*...
gi 489326441 23 DLKIE-EGKITALIGANGCGKSTILKSL 49
Cdd:pfam13476 11 DQTIDfSKGLTLITGPNGSGKTTILDAI 38
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
30-49 |
7.84e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 37.19 E-value: 7.84e-03
|
| |
